메뉴 건너뛰기




Volumn 1841, Issue 7, 2014, Pages 919-933

Physiological regulation of lipoprotein lipase

Author keywords

Adipose tissue; Angiopoietin like proteins; Apolipoproteins; Lipoprotein lipase; Muscle; Triglyceride rich lipoproteins

Indexed keywords

ADIPOSE TISSUE; ANGIOPOIETIN-LIKE PROTEINS; APOLIPOPROTEINS; LIPOPROTEIN LIPASE; MUSCLE; TRIGLYCERIDE-RICH LIPOPROTEINS;

EID: 84899465714     PISSN: 13881981     EISSN: 18792618     Source Type: Journal    
DOI: 10.1016/j.bbalip.2014.03.013     Document Type: Review
Times cited : (417)

References (299)
  • 1
    • 84873766944 scopus 로고
    • Clearing factor, a heparin-activated lipoprotein lipase. I. Isolation and characterization of the enzyme from normal rat heart
    • E.D. Korn Clearing factor, a heparin-activated lipoprotein lipase. I. Isolation and characterization of the enzyme from normal rat heart J. Biol. Chem. 215 1955 1 14
    • (1955) J. Biol. Chem. , vol.215 , pp. 1-14
    • Korn, E.D.1
  • 5
    • 0017052558 scopus 로고
    • Lipoprotein lipase from bovine milk. Isolation procedure, chemical characterization, and molecular weight analysis
    • P.H. Iverius, and A.M. Ostlund-Lindqvist Lipoprotein lipase from bovine milk. Isolation procedure, chemical characterization, and molecular weight analysis J. Biol. Chem. 251 1976 7791 7795 (Pubitemid 8015789)
    • (1976) Journal of Biological Chemistry , vol.251 , Issue.24 , pp. 7791-7795
    • Iverius, P.H.1    Ostlund Lindqvist, A.M.2
  • 6
    • 0036379409 scopus 로고    scopus 로고
    • Molecular modeling of the dimeric structure of human lipoprotein lipase and functional studies of the carboxyl-terminal domain
    • Y. Kobayashi, T. Nakajima, and I. Inoue Molecular modeling of the dimeric structure of human lipoprotein lipase and functional studies of the carboxyl-terminal domain Eur. J. Biochem. 269 2002 4701 4710
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4701-4710
    • Kobayashi, Y.1    Nakajima, T.2    Inoue, I.3
  • 7
    • 79956354120 scopus 로고    scopus 로고
    • Comparative studies of vertebrate lipoprotein lipase: A key enzyme of very low density lipoprotein metabolism
    • R.S. Holmes, J.L. Vandeberg, and L.A. Cox Comparative studies of vertebrate lipoprotein lipase: a key enzyme of very low density lipoprotein metabolism Comp. Biochem. Physiol. Part D Genomics Proteomics 6 2011 224 234
    • (2011) Comp. Biochem. Physiol. Part D Genomics Proteomics , vol.6 , pp. 224-234
    • Holmes, R.S.1    Vandeberg, J.L.2    Cox, L.A.3
  • 8
    • 0028129833 scopus 로고
    • Lipoprotein lipase. Molecular model based on the pancreatic lipase X-ray structure: Consequences for heparin binding and catalysis
    • H. van Tilbeurgh, A. Roussel, J.M. Lalouel, and C. Cambillau Lipoprotein lipase. Molecular model based on the pancreatic lipase X-ray structure: consequences for heparin binding and catalysis J. Biol. Chem. 269 1994 4626 4633
    • (1994) J. Biol. Chem. , vol.269 , pp. 4626-4633
    • Van Tilbeurgh, H.1    Roussel, A.2    Lalouel, J.M.3    Cambillau, C.4
  • 10
    • 0031811576 scopus 로고    scopus 로고
    • Identification of a heparin-binding domain in the distal carboxyl- terminal region of lipoprotein lipase by site-directed mutagenesis
    • R.A. Sendak, and A. Bensadoun Identification of a heparin-binding domain in the distal carboxyl-terminal region of lipoprotein lipase by site-directed mutagenesis J. Lipid Res. 39 1998 1310 1315 (Pubitemid 28270096)
    • (1998) Journal of Lipid Research , vol.39 , Issue.6 , pp. 1310-1315
    • Sendak, R.A.1    Bensadoun, A.2
  • 11
    • 77956234052 scopus 로고    scopus 로고
    • Angiopoietin-like protein 3 inhibits lipoprotein lipase activity through enhancing its cleavage by proprotein convertases
    • J. Liu, H. Afroza, D.J. Rader, and W. Jin Angiopoietin-like protein 3 inhibits lipoprotein lipase activity through enhancing its cleavage by proprotein convertases J. Biol. Chem. 285 2010 27561 27570
    • (2010) J. Biol. Chem. , vol.285 , pp. 27561-27570
    • Liu, J.1    Afroza, H.2    Rader, D.J.3    Jin, W.4
  • 12
    • 0025974363 scopus 로고
    • The familial hyperchylomicronemia syndrome. New insights into underlying genetic defects
    • S. Santamarina-Fojo, and H.B. Brewer Jr. The familial hyperchylomicronemia syndrome. New insights into underlying genetic defects JAMA 265 1991 904 908
    • (1991) JAMA , vol.265 , pp. 904-908
    • Santamarina-Fojo, S.1    Brewer, Jr.H.B.2
  • 13
    • 0029079312 scopus 로고
    • COOH-terminal disruption of lipoprotein lipase in mice is lethal in homozygotes, but heterozygotes have elevated triglycerides and impaired enzyme activity
    • T. Coleman, R.L. Seip, J.M. Gimble, D. Lee, N. Maeda, and C.F. Semenkovich COOH-terminal disruption of lipoprotein lipase in mice is lethal in homozygotes, but heterozygotes have elevated triglycerides and impaired enzyme activity J. Biol. Chem. 270 1995 12518 12525
    • (1995) J. Biol. Chem. , vol.270 , pp. 12518-12525
    • Coleman, T.1    Seip, R.L.2    Gimble, J.M.3    Lee, D.4    Maeda, N.5    Semenkovich, C.F.6
  • 14
    • 0028819754 scopus 로고
    • Severe hypertriglyceridemia, reduced high density lipoprotein, and neonatal death in lipoprotein lipase knockout mice. Mild hypertriglyceridemia with impaired very low density lipoprotein clearance in heterozygotes
    • P.H. Weinstock, C.L. Bisgaier, K. Aalto-Setala, H. Radner, R. Ramakrishnan, S. Levak-Frank, A.D. Essenburg, R. Zechner, and J.L. Breslow Severe hypertriglyceridemia, reduced high density lipoprotein, and neonatal death in lipoprotein lipase knockout mice. Mild hypertriglyceridemia with impaired very low density lipoprotein clearance in heterozygotes J. Clin. Invest. 96 1995 2555 2568
    • (1995) J. Clin. Invest. , vol.96 , pp. 2555-2568
    • Weinstock, P.H.1    Bisgaier, C.L.2    Aalto-Setala, K.3    Radner, H.4    Ramakrishnan, R.5    Levak-Frank, S.6    Essenburg, A.D.7    Zechner, R.8    Breslow, J.L.9
  • 19
    • 0027296725 scopus 로고
    • Overexpression of human lipoprotein lipase in transgenic mice. Resistance to diet-induced hypertriglyceridemia and hypercholesterolemia
    • M. Shimada, H. Shimano, T. Gotoda, K. Yamamoto, M. Kawamura, T. Inaba, Y. Yazaki, and N. Yamada Overexpression of human lipoprotein lipase in transgenic mice. Resistance to diet-induced hypertriglyceridemia and hypercholesterolemia J. Biol. Chem. 268 1993 17924 17929 (Pubitemid 23260307)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.24 , pp. 17924-17929
    • Shimada, M.1    Shimano, H.2    Gotoda, T.3    Yamamoto, K.4    Kawamura, M.5    Inaba, T.6    Yazaki, Y.7    Yamada, N.8
  • 20
    • 0023871823 scopus 로고
    • Regulation of lipoprotein lipase mRNA content in 3T3-L1 cells by tumour necrosis factor
    • P. Cornelius, S. Enerback, G. Bjursell, T. Olivecrona, and P.H. Pekala Regulation of lipoprotein lipase mRNA content in 3T3-L1 cells by tumour necrosis factor Biochem. J. 249 1988 765 769 (Pubitemid 18042796)
    • (1988) Biochemical Journal , vol.249 , Issue.3 , pp. 765-769
    • Cornelius, P.1    Enerback, S.2    Bjursell, G.3    Olivecrona, T.4    Pekala, P.H.5
  • 22
    • 0028131210 scopus 로고
    • Transcriptional regulation of lipoprotein lipase in the heart during development in the rat
    • DOI 10.1006/bbrc.1994.2006
    • A. Singh-Bist, M.C. Komaromy, and F.B. Kraemer Transcriptional regulation of lipoprotein lipase in the heart during development in the rat Biochem. Biophys. Res. Commun. 202 1994 838 843 (Pubitemid 24259290)
    • (1994) Biochemical and Biophysical Research Communications , vol.202 , Issue.2 , pp. 838-843
    • Singh-Bist, A.1    Komaromy, M.C.2    Kraemer, F.B.3
  • 23
    • 0033015655 scopus 로고    scopus 로고
    • Role of apoCs in lipoprotein metabolism: Functional differences between ApoC1, ApoC2, and ApoC3
    • M.C. Jong, M.H. Hofker, and L.M. Havekes Role of ApoCs in lipoprotein metabolism: functional differences between ApoC1, ApoC2, and ApoC3 Arterioscler. Thromb. Vasc. Biol. 19 1999 472 484 (Pubitemid 29135144)
    • (1999) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.19 , Issue.3 , pp. 472-484
    • Jong, M.C.1    Hofker, M.H.2    Havekes, L.M.3
  • 25
    • 84862117973 scopus 로고    scopus 로고
    • A review of the role of apolipoprotein C-II in lipoprotein metabolism and cardiovascular disease
    • A.A. Kei, T.D. Filippatos, V. Tsimihodimos, and M.S. Elisaf A review of the role of apolipoprotein C-II in lipoprotein metabolism and cardiovascular disease Metabolism 61 2012 906 921
    • (2012) Metabolism , vol.61 , pp. 906-921
    • Kei, A.A.1    Filippatos, T.D.2    Tsimihodimos, V.3    Elisaf, M.S.4
  • 26
    • 0029791717 scopus 로고    scopus 로고
    • Further characterization of the metabolic properties of triglyceride- rich lipoproteins from human and mouse apoC-III transgenic mice
    • K. Aalto-Setala, P.H. Weinstock, C.L. Bisgaier, L. Wu, J.D. Smith, and J.L. Breslow Further characterization of the metabolic properties of triglyceride-rich lipoproteins from human and mouse apoC-III transgenic mice J. Lipid Res. 37 1996 1802 1811 (Pubitemid 26275391)
    • (1996) Journal of Lipid Research , vol.37 , Issue.8 , pp. 1802-1811
    • Aalto-Setala, K.1    Weinstock, P.H.2    Bisgaier, C.L.3    Wu, L.4    Smith, J.D.5    Breslow, J.L.6
  • 27
    • 13944253941 scopus 로고    scopus 로고
    • Severe hypertriglyceridemia in human APOC1 transgenic mice is caused by apoC-I-induced inhibition of LPL
    • DOI 10.1194/jlr.M400301-JLR200
    • J.F. Berbee, C.C. van der Hoogt, D. Sundararaman, L.M. Havekes, and P.C. Rensen Severe hypertriglyceridemia in human APOC1 transgenic mice is caused by apoC-I-induced inhibition of LPL J. Lipid Res. 46 2005 297 306 (Pubitemid 40271094)
    • (2005) Journal of Lipid Research , vol.46 , Issue.2 , pp. 297-306
    • Berbee, J.F.P.1    Van Der Hoogt, C.C.2    Sundararaman, D.3    Havekes, L.M.4    Rensen, P.C.N.5
  • 28
    • 0034749662 scopus 로고    scopus 로고
    • Apolipoprotein C-III deficiency accelerates triglyceride hydrolysis by lipoprotein lipase in wild-type and apoE knockout mice
    • M.C. Jong, P.C. Rensen, V.E. Dahlmans, H. van der Boom, T.J. van Berkel, and L.M. Havekes Apolipoprotein C-III deficiency accelerates triglyceride hydrolysis by lipoprotein lipase in wild-type and apoE knockout mice J. Lipid Res. 42 2001 1578 1585 (Pubitemid 33026056)
    • (2001) Journal of Lipid Research , vol.42 , Issue.10 , pp. 1578-1585
    • Jong, M.C.1    Rensen, P.C.N.2    Dahlmans, V.E.H.3    Van Der Boom, H.4    Van Berkel, T.J.C.5    Havekes, L.M.6
  • 29
    • 33744828960 scopus 로고    scopus 로고
    • Endogenous apoC-I increases hyperlipidemia in apoE-knockout mice by stimulating VLDL production and inhibiting LPL
    • DOI 10.1194/jlr.M500434-JLR200
    • M. Westerterp, W. de Haan, J.F. Berbee, L.M. Havekes, and P.C. Rensen Endogenous apoC-I increases hyperlipidemia in apoE-knockout mice by stimulating VLDL production and inhibiting LPL J. Lipid Res. 47 2006 1203 1211 (Pubitemid 43830712)
    • (2006) Journal of Lipid Research , vol.47 , Issue.6 , pp. 1203-1211
    • Westerterp, M.1    De Haan, W.2    Berbee, J.F.P.3    Havekes, L.M.4    Rensen, P.C.N.5
  • 30
    • 84888335913 scopus 로고    scopus 로고
    • Apolipoproteins C-I and C-III inhibit lipoprotein lipase activity by displacement of the enzyme from lipid droplets
    • M. Larsson, E. Vorrsjo, P. Talmud, A. Lookene, and G. Olivecrona Apolipoproteins C-I and C-III inhibit lipoprotein lipase activity by displacement of the enzyme from lipid droplets J. Biol. Chem. 288 2013 33997 34008
    • (2013) J. Biol. Chem. , vol.288 , pp. 33997-34008
    • Larsson, M.1    Vorrsjo, E.2    Talmud, P.3    Lookene, A.4    Olivecrona, G.5
  • 32
    • 36949009469 scopus 로고    scopus 로고
    • Peroxisome proliferator activated receptors and lipoprotein metabolism
    • S. Kersten Peroxisome proliferator activated receptors and lipoprotein metabolism PPAR Res. 2008 2008 132960
    • (2008) PPAR Res. , vol.2008 , pp. 132960
    • Kersten, S.1
  • 34
    • 84893833662 scopus 로고    scopus 로고
    • Homozygosity for a partial deletion of apoprotein A-V signal peptide results in intracellular missorting of the protein and chylomicronemia in a breast-fed infant
    • K. Albers, C. Schlein, K. Wenner, P. Lohse, A. Bartelt, J. Heeren, R. Santer, and M. Merkel Homozygosity for a partial deletion of apoprotein A-V signal peptide results in intracellular missorting of the protein and chylomicronemia in a breast-fed infant Atherosclerosis 233 2014 97 103
    • (2014) Atherosclerosis , vol.233 , pp. 97-103
    • Albers, K.1    Schlein, C.2    Wenner, K.3    Lohse, P.4    Bartelt, A.5    Heeren, J.6    Santer, R.7    Merkel, M.8
  • 37
    • 84878524779 scopus 로고    scopus 로고
    • Apolipoproteins e and AV mediate lipoprotein clearance by hepatic proteoglycans
    • J.C. Gonzales, P.L. Gordts, E.M. Foley, and J.D. Esko Apolipoproteins E and AV mediate lipoprotein clearance by hepatic proteoglycans J. Clin. Invest. 123 2013 2742 2751
    • (2013) J. Clin. Invest. , vol.123 , pp. 2742-2751
    • Gonzales, J.C.1    Gordts, P.L.2    Foley, E.M.3    Esko, J.D.4
  • 40
    • 0038491484 scopus 로고    scopus 로고
    • The human apolipoprotein AV gene is regulated by peroxisome proliferator-activated receptor-α and contains a novel farnesoid X-activated receptor response element
    • DOI 10.1074/jbc.M301302200
    • X. Prieur, H. Coste, and J.C. Rodriguez The human apolipoprotein AV gene is regulated by peroxisome proliferator-activated receptor-alpha and contains a novel farnesoid X-activated receptor response element J. Biol. Chem. 278 2003 25468 25480 (Pubitemid 36835298)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 25468-25480
    • Prieur, X.1    Coste, H.2    Rodriguez, J.C.3
  • 42
    • 67650269599 scopus 로고    scopus 로고
    • Differential regulation of the human versus the mouse apolipoprotein AV gene by PPARalpha. Implications for the study of pharmaceutical modifiers of hypertriglyceridemia in mice
    • X. Prieur, P. Lesnik, M. Moreau, J.C. Rodriguez, C. Doucet, M.J. Chapman, and T. Huby Differential regulation of the human versus the mouse apolipoprotein AV gene by PPARalpha. Implications for the study of pharmaceutical modifiers of hypertriglyceridemia in mice Biochim. Biophys. Acta 1791 2009 764 771
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 764-771
    • Prieur, X.1    Lesnik, P.2    Moreau, M.3    Rodriguez, J.C.4    Doucet, C.5    Chapman, M.J.6    Huby, T.7
  • 44
    • 0036217731 scopus 로고    scopus 로고
    • The APOE locus and the pharmacogenetics of lipid response
    • DOI 10.1097/00041433-200204000-00001
    • J.M. Ordovas, and V. Mooser The APOE locus and the pharmacogenetics of lipid response Curr. Opin. Lipidol. 13 2002 113 117 (Pubitemid 34280761)
    • (2002) Current Opinion in Lipidology , vol.13 , Issue.2 , pp. 113-117
    • Ordovas, J.M.1    Mooser, V.2
  • 45
    • 0030661590 scopus 로고    scopus 로고
    • Hepatic uptake of chylomicron remnants
    • A.D. Cooper Hepatic uptake of chylomicron remnants J. Lipid Res. 38 1997 2173 2192 (Pubitemid 27495377)
    • (1997) Journal of Lipid Research , vol.38 , Issue.11 , pp. 2173-2192
    • Cooper, A.D.1
  • 46
    • 15844414655 scopus 로고    scopus 로고
    • Apolipoprotein E effectively inhibits lipoprotein lipase-mediated lipolysis of chylomicron-like triglyceride-rich lipid emulsions in vitro and in vivo
    • DOI 10.1074/jbc.271.25.14791
    • P.C. Rensen, and T.J. van Berkel Apolipoprotein E effectively inhibits lipoprotein lipase-mediated lipolysis of chylomicron-like triglyceride-rich lipid emulsions in vitro and in vivo J. Biol. Chem. 271 1996 14791 14799 (Pubitemid 26194959)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.25 , pp. 14791-14799
    • Rensen, P.C.N.1    Van Berkel, T.J.C.2
  • 49
    • 0024324398 scopus 로고
    • Inhibition of lipoprotein lipase by the receptor-binding domain of apolipoprotein E
    • DOI 10.1016/0014-5793(89)81464-4
    • W.J. McConathy, and C.S. Wang Inhibition of lipoprotein lipase by the receptor-binding domain of apolipoprotein E FEBS Lett. 251 1989 250 252 (Pubitemid 19181878)
    • (1989) FEBS Letters , vol.251 , Issue.1-2 , pp. 250-252
    • McConathy, W.J.1    Wang, C.-S.2
  • 50
    • 0034666157 scopus 로고    scopus 로고
    • Characterization of the fasting-induced adipose factor FIAF, a novel peroxisome proliferator-activated receptor target gene
    • S. Kersten, S. Mandard, N.S. Tan, P. Escher, D. Metzger, P. Chambon, F.J. Gonzalez, B. Desvergne, and W. Wahli Characterization of the fasting-induced adipose factor FIAF, a novel peroxisome proliferator-activated receptor target gene J. Biol. Chem. 275 2000 28488 28493
    • (2000) J. Biol. Chem. , vol.275 , pp. 28488-28493
    • Kersten, S.1    Mandard, S.2    Tan, N.S.3    Escher, P.4    Metzger, D.5    Chambon, P.6    Gonzalez, F.J.7    Desvergne, B.8    Wahli, W.9
  • 51
    • 0343060983 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor γ target gene encoding a novel angiopoietin-related protein associated with adipose differentiation
    • DOI 10.1128/MCB.20.14.5343-5349.2000
    • J.C. Yoon, T.W. Chickering, E.D. Rosen, B. Dussault, Y. Qin, A. Soukas, J.M. Friedman, W.E. Holmes, and B.M. Spiegelman Peroxisome proliferator- activated receptor gamma target gene encoding a novel angiopoietin-related protein associated with adipose differentiation Mol. Cell. Biol. 20 2000 5343 5349 (Pubitemid 30431587)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.14 , pp. 5343-5349
    • Cliff Yoon, J.1    Chickering, T.W.2    Rosen, E.D.3    Dussault, B.4    Qin, Y.5    Soukas, A.6    Friedman, J.M.7    Holmes, W.E.8    Spiegelman, B.M.9
  • 53
    • 77953810264 scopus 로고    scopus 로고
    • Induction of cardiac Angptl4 by dietary fatty acids is mediated by peroxisome proliferator-activated receptor beta/delta and protects against fatty acid-induced oxidative stress
    • A. Georgiadi, L. Lichtenstein, T. Degenhardt, M.V. Boekschoten, M. van Bilsen, B. Desvergne, M. Muller, and S. Kersten Induction of cardiac Angptl4 by dietary fatty acids is mediated by peroxisome proliferator-activated receptor beta/delta and protects against fatty acid-induced oxidative stress Circ. Res. 106 2010 1712 1721
    • (2010) Circ. Res. , vol.106 , pp. 1712-1721
    • Georgiadi, A.1    Lichtenstein, L.2    Degenhardt, T.3    Boekschoten, M.V.4    Van Bilsen, M.5    Desvergne, B.6    Muller, M.7    Kersten, S.8
  • 54
    • 84862575244 scopus 로고    scopus 로고
    • The natural carotenoid astaxanthin, a PPAR-alpha agonist and PPAR-gamma antagonist, reduces hepatic lipid accumulation by rewiring the transcriptome in lipid-loaded hepatocytes
    • Y. Jia, J.Y. Kim, H.J. Jun, S.J. Kim, J.H. Lee, M.H. Hoang, K.Y. Hwang, S.J. Um, H.I. Chang, and S.J. Lee The natural carotenoid astaxanthin, a PPAR-alpha agonist and PPAR-gamma antagonist, reduces hepatic lipid accumulation by rewiring the transcriptome in lipid-loaded hepatocytes Mol. Nutr. Food Res. 56 2012 878 888
    • (2012) Mol. Nutr. Food Res. , vol.56 , pp. 878-888
    • Jia, Y.1    Kim, J.Y.2    Jun, H.J.3    Kim, S.J.4    Lee, J.H.5    Hoang, M.H.6    Hwang, K.Y.7    Um, S.J.8    Chang, H.I.9    Lee, S.J.10
  • 56
    • 62749136195 scopus 로고    scopus 로고
    • Muscle-derived angiopoietin-like protein 4 is induced by fatty acids via peroxisome proliferator-activated receptor (PPAR)-delta and is of metabolic relevance in humans
    • H. Staiger, C. Haas, J. Machann, R. Werner, M. Weisser, F. Schick, F. Machicao, N. Stefan, A. Fritsche, and H.U. Haring Muscle-derived angiopoietin-like protein 4 is induced by fatty acids via peroxisome proliferator-activated receptor (PPAR)-delta and is of metabolic relevance in humans Diabetes 58 2009 579 589
    • (2009) Diabetes , vol.58 , pp. 579-589
    • Staiger, H.1    Haas, C.2    MacHann, J.3    Werner, R.4    Weisser, M.5    Schick, F.6    MacHicao, F.7    Stefan, N.8    Fritsche, A.9    Haring, H.U.10
  • 59
    • 32644454369 scopus 로고    scopus 로고
    • The fasting-induced adipose factor/angiopoietin-like protein 4 is physically associated with lipoproteins and governs plasma lipid levels and adiposity
    • S. Mandard, F. Zandbergen, E. van Straten, W. Wahli, F. Kuipers, M. Muller, and S. Kersten The fasting-induced adipose factor/angiopoietin-like protein 4 is physically associated with lipoproteins and governs plasma lipid levels and adiposity J. Biol. Chem. 281 2006 934 944
    • (2006) J. Biol. Chem. , vol.281 , pp. 934-944
    • Mandard, S.1    Zandbergen, F.2    Van Straten, E.3    Wahli, W.4    Kuipers, F.5    Muller, M.6    Kersten, S.7
  • 65
    • 84885101882 scopus 로고    scopus 로고
    • Angiopoietin-like protein 4 inhibition of lipoprotein lipase: Evidence for reversible complex formation
    • M.J. Lafferty, K.C. Bradford, D.A. Erie, and S.B. Neher Angiopoietin-like protein 4 inhibition of lipoprotein lipase: evidence for reversible complex formation J. Biol. Chem. 288 2013 28524 28534
    • (2013) J. Biol. Chem. , vol.288 , pp. 28524-28534
    • Lafferty, M.J.1    Bradford, K.C.2    Erie, D.A.3    Neher, S.B.4
  • 68
    • 34047177395 scopus 로고    scopus 로고
    • Population-based resequencing of ANGPTL4 uncovers variations that reduce triglycerides and increase HDL
    • DOI 10.1038/ng1984, PII NG1984
    • S. Romeo, L.A. Pennacchio, Y. Fu, E. Boerwinkle, A. Tybjaerg-Hansen, H.H. Hobbs, and J.C. Cohen Population-based resequencing of ANGPTL4 uncovers variations that reduce triglycerides and increase HDL Nat. Genet. 39 2007 513 516 (Pubitemid 46514768)
    • (2007) Nature Genetics , vol.39 , Issue.4 , pp. 513-516
    • Romeo, S.1    Pennacchio, L.A.2    Fu, Y.3    Boerwinkle, E.4    Tybjaerg-Hansen, A.5    Hobbs, H.H.6    Cohen, J.C.7
  • 75
    • 33644788337 scopus 로고    scopus 로고
    • Angptl3-null mice show low plasma lipid concentrations by enhanced lipoprotein lipase activity
    • DOI 10.1538/expanim.55.27
    • K. Fujimoto, R. Koishi, T. Shimizugawa, and Y. Ando Angptl3-null mice show low plasma lipid concentrations by enhanced lipoprotein lipase activity Exp. Anim. 55 2006 27 34 (Pubitemid 43349428)
    • (2006) Experimental Animals , vol.55 , Issue.1 , pp. 27-34
    • Fujimoto, K.1    Koishi, R.2    Shimizugawa, T.3    Ando, Y.4
  • 77
    • 59449084854 scopus 로고    scopus 로고
    • The angiopoietin-like proteins ANGPTL3 and ANGPTL4 inhibit lipoprotein lipase activity through distinct mechanisms
    • L. Shan, X.C. Yu, Z. Liu, Y. Hu, L.T. Sturgis, M.L. Miranda, and Q. Liu The angiopoietin-like proteins ANGPTL3 and ANGPTL4 inhibit lipoprotein lipase activity through distinct mechanisms J. Biol. Chem. 284 2009 1419 1424
    • (2009) J. Biol. Chem. , vol.284 , pp. 1419-1424
    • Shan, L.1    Yu, X.C.2    Liu, Z.3    Hu, Y.4    Sturgis, L.T.5    Miranda, M.L.6    Liu, Q.7
  • 83
    • 84864501914 scopus 로고    scopus 로고
    • Identification of RIFL, a novel adipocyte-enriched insulin target gene with a role in lipid metabolism
    • G. Ren, J.Y. Kim, and C.M. Smas Identification of RIFL, a novel adipocyte-enriched insulin target gene with a role in lipid metabolism Am. J. Physiol. Endocrinol. Metab. 303 2012 E334 E351
    • (2012) Am. J. Physiol. Endocrinol. Metab. , vol.303
    • Ren, G.1    Kim, J.Y.2    Smas, C.M.3
  • 84
    • 84864809680 scopus 로고    scopus 로고
    • Lipasin, a novel nutritionally-regulated liver-enriched factor that regulates serum triglyceride levels
    • R. Zhang Lipasin, a novel nutritionally-regulated liver-enriched factor that regulates serum triglyceride levels Biochem. Biophys. Res. Commun. 424 2012 786 792
    • (2012) Biochem. Biophys. Res. Commun. , vol.424 , pp. 786-792
    • Zhang, R.1
  • 86
    • 84872493616 scopus 로고    scopus 로고
    • Lipasin, thermoregulated in brown fat, is a novel but atypical member of the angiopoietin-like protein family
    • Z. Fu, F. Yao, A.B. Abou-Samra, and R. Zhang Lipasin, thermoregulated in brown fat, is a novel but atypical member of the angiopoietin-like protein family Biochem. Biophys. Res. Commun. 430 2013 1126 1131
    • (2013) Biochem. Biophys. Res. Commun. , vol.430 , pp. 1126-1131
    • Fu, Z.1    Yao, F.2    Abou-Samra, A.B.3    Zhang, R.4
  • 87
    • 0032965030 scopus 로고    scopus 로고
    • De novo lipogenesis in humans: Metabolic and regulatory aspects
    • M.K. Hellerstein De novo lipogenesis in humans: metabolic and regulatory aspects Eur. J. Clin. Nutr. 53 Suppl. 1 1999 S53 S65
    • (1999) Eur. J. Clin. Nutr. , vol.53 , Issue.SUPPL. 1
    • Hellerstein, M.K.1
  • 88
    • 77952525681 scopus 로고    scopus 로고
    • Comparative approach of the de novo fatty acid synthesis (lipogenesis) between ruminant and non ruminant mammalian species: From biochemical level to the main regulatory lipogenic genes
    • G.P. Laliotis, I. Bizelis, and E. Rogdakis Comparative approach of the de novo fatty acid synthesis (lipogenesis) between ruminant and non ruminant mammalian species: from biochemical level to the main regulatory lipogenic genes Curr. Genomics 11 2010 168 183
    • (2010) Curr. Genomics , vol.11 , pp. 168-183
    • Laliotis, G.P.1    Bizelis, I.2    Rogdakis, E.3
  • 89
    • 84874900503 scopus 로고    scopus 로고
    • Biochemistry and pathophysiology of intravascular and intracellular lipolysis
    • S.G. Young, and R. Zechner Biochemistry and pathophysiology of intravascular and intracellular lipolysis Genes Dev. 27 2013 459 484
    • (2013) Genes Dev. , vol.27 , pp. 459-484
    • Young, S.G.1    Zechner, R.2
  • 90
    • 0037343188 scopus 로고    scopus 로고
    • Contribution of fatty acids released from lipolysis of plasma triglycerides to total plasma fatty acid flux and tissue-specific fatty acid uptake
    • DOI 10.2337/diabetes.52.3.614
    • B. Teusink, P.J. Voshol, V.E. Dahlmans, P.C. Rensen, H. Pijl, J.A. Romijn, and L.M. Havekes Contribution of fatty acids released from lipolysis of plasma triglycerides to total plasma fatty acid flux and tissue-specific fatty acid uptake Diabetes 52 2003 614 620 (Pubitemid 36323566)
    • (2003) Diabetes , vol.52 , Issue.3 , pp. 614-620
    • Teusink, B.1    Voshol, P.J.2    Dahlmans, V.E.H.3    Rensen, P.C.N.4    Pijl, H.5    Romijn, J.A.6    Havekes, L.M.7
  • 91
    • 0029954875 scopus 로고    scopus 로고
    • Chylomicron metabolism in rats: Lipolysis, recirculation of triglyceride-derived fatty acids in plasma FFA, and fate of core lipids as analyzed by compartmental modelling
    • M. Hultin, R. Savonen, and T. Olivecrona Chylomicron metabolism in rats: lipolysis, recirculation of triglyceride-derived fatty acids in plasma FFA, and fate of core lipids as analyzed by compartmental modelling J. Lipid Res. 37 1996 1022 1036
    • (1996) J. Lipid Res. , vol.37 , pp. 1022-1036
    • Hultin, M.1    Savonen, R.2    Olivecrona, T.3
  • 92
    • 0029176539 scopus 로고
    • Coordinated regulation of hormone-sensitive lipase and lipoprotein lipase in human adipose tissue in vivo: Implications for the control of fat storage and fat mobilization
    • K.N. Frayn, S.W. Coppack, B.A. Fielding, and S.M. Humphreys Coordinated regulation of hormone-sensitive lipase and lipoprotein lipase in human adipose tissue in vivo: implications for the control of fat storage and fat mobilization Adv. Enzym. Regul. 35 1995 163 178
    • (1995) Adv. Enzym. Regul. , vol.35 , pp. 163-178
    • Frayn, K.N.1    Coppack, S.W.2    Fielding, B.A.3    Humphreys, S.M.4
  • 94
    • 0037877441 scopus 로고
    • Effect of nutrition on activity and release of lipase from rat adipose tissue
    • C.H. Hollenberg Effect of nutrition on activity and release of lipase from rat adipose tissue Am. J. Physiol. 197 1959 667 670
    • (1959) Am. J. Physiol. , vol.197 , pp. 667-670
    • Hollenberg, C.H.1
  • 96
    • 0023904495 scopus 로고
    • Tissue-specific regulation of guinea pig lipoprotein lipase; Effects of nutritional state and of tumor necrosis factor on mRNA levels in adipose tissue, heart and liver
    • S. Enerback, H. Semb, J. Tavernier, G. Bjursell, and T. Olivecrona Tissue-specific regulation of guinea pig lipoprotein lipase; effects of nutritional state and of tumor necrosis factor on mRNA levels in adipose tissue, heart and liver Gene 64 1988 97 106
    • (1988) Gene , vol.64 , pp. 97-106
    • Enerback, S.1    Semb, H.2    Tavernier, J.3    Bjursell, G.4    Olivecrona, T.5
  • 97
    • 0025856183 scopus 로고
    • Regulation of lipoprotein lipase in adipose and muscle tissues during fasting
    • M.J. Ladu, H. Kapsas, and W.K. Palmer Regulation of lipoprotein lipase in adipose and muscle tissues during fasting Am. J. Physiol. 260 1991 R953 R959
    • (1991) Am. J. Physiol. , vol.260
    • Ladu, M.J.1    Kapsas, H.2    Palmer, W.K.3
  • 98
    • 0026518865 scopus 로고
    • The regulation of lipoprotein lipase gene expression by dexamethasone in isolated rat adipocytes
    • J.M. Ong, R.B. Simsolo, B. Saffari, and P.A. Kern The regulation of lipoprotein lipase gene expression by dexamethasone in isolated rat adipocytes Endocrinology 130 1992 2310 2316
    • (1992) Endocrinology , vol.130 , pp. 2310-2316
    • Ong, J.M.1    Simsolo, R.B.2    Saffari, B.3    Kern, P.A.4
  • 99
    • 70350008227 scopus 로고    scopus 로고
    • Angiopoietin-like 4 (ANGPTL4, fasting-induced adipose factor) is a direct glucocorticoid receptor target and participates in glucocorticoid-regulated triglyceride metabolism
    • S.K. Koliwad, T. Kuo, L.E. Shipp, N.E. Gray, F. Backhed, A.Y. So, R.V. Farese Jr., and J.C. Wang Angiopoietin-like 4 (ANGPTL4, fasting-induced adipose factor) is a direct glucocorticoid receptor target and participates in glucocorticoid-regulated triglyceride metabolism J. Biol. Chem. 284 2009 25593 25601
    • (2009) J. Biol. Chem. , vol.284 , pp. 25593-25601
    • Koliwad, S.K.1    Kuo, T.2    Shipp, L.E.3    Gray, N.E.4    Backhed, F.5    So, A.Y.6    Farese, Jr.R.V.7    Wang, J.C.8
  • 100
    • 0027482040 scopus 로고
    • Lipoprotein lipase regulation by insulin and glucocorticoid in subcutaneous and omental adipose tissues of obese women and men
    • S.K. Fried, C.D. Russell, N.L. Grauso, and R.E. Brolin Lipoprotein lipase regulation by insulin and glucocorticoid in subcutaneous and omental adipose tissues of obese women and men J. Clin. Invest. 92 1993 2191 2198 (Pubitemid 23333523)
    • (1993) Journal of Clinical Investigation , vol.92 , Issue.5 , pp. 2191-2198
    • Fried, S.K.1    Russell, C.D.2    Grauso, N.L.3    Brolin, R.E.4
  • 101
    • 0029303454 scopus 로고
    • Blockade of the glucocorticoid receptor with RU 486: Effects in vitro and in vivo on human adipose tissue lipoprotein lipase activity
    • M. Ottosson, P. Marin, K. Karason, A. Elander, and P. Bjorntorp Blockade of the glucocorticoid receptor with RU 486: effects in vitro and in vivo on human adipose tissue lipoprotein lipase activity Obes. Res. 3 1995 233 240
    • (1995) Obes. Res. , vol.3 , pp. 233-240
    • Ottosson, M.1    Marin, P.2    Karason, K.3    Elander, A.4    Bjorntorp, P.5
  • 103
    • 0345369744 scopus 로고    scopus 로고
    • Response of adipose tissue lipoprotein lipase to the cephalic phase of insulin secretion
    • F. Picard, N. Naimi, D. Richard, and Y. Deshaies Response of adipose tissue lipoprotein lipase to the cephalic phase of insulin secretion Diabetes 48 1999 452 459 (Pubitemid 29106856)
    • (1999) Diabetes , vol.48 , Issue.3 , pp. 452-459
    • Picard, F.1    Naimi, N.2    Richard, D.3    Deshaies, Y.4
  • 104
    • 0023681295 scopus 로고
    • Insulin increases the synthetic rate and messenger RNA level of lipoprotein lipase in isolated rat adipocytes
    • J.M. Ong, T.G. Kirchgessner, M.C. Schotz, and P.A. Kern Insulin increases the synthetic rate and messenger RNA level of lipoprotein lipase in isolated rat adipocytes J. Biol. Chem. 263 1988 12933 12938
    • (1988) J. Biol. Chem. , vol.263 , pp. 12933-12938
    • Ong, J.M.1    Kirchgessner, T.G.2    Schotz, M.C.3    Kern, P.A.4
  • 105
    • 0025052191 scopus 로고
    • Lipoprotein lipase gene expression in rat adipocytes is regulated by isoproterenol and insulin through different mechanisms
    • M.V. Raynolds, P.D. Awald, D.F. Gordon, A. Gutierrez-Hartmann, D.C. Rule, W.M. Wood, and R.H. Eckel Lipoprotein lipase gene expression in rat adipocytes is regulated by isoproterenol and insulin through different mechanisms Mol. Endocrinol. 4 1990 1416 1422 (Pubitemid 20371442)
    • (1990) Molecular Endocrinology , vol.4 , Issue.9 , pp. 1416-1422
    • Raynolds, M.V.1    Awald, P.D.2    Gordon, D.F.3    Gutierrez-Hartmann, A.4    Rule, D.C.5    Wood, W.M.6    Eckel, R.H.7
  • 106
    • 78149350158 scopus 로고    scopus 로고
    • GIP increases human adipocyte LPL expression through CREB and TORC2-mediated trans-activation of the LPL gene
    • S.J. Kim, C. Nian, and C.H. McIntosh GIP increases human adipocyte LPL expression through CREB and TORC2-mediated trans-activation of the LPL gene J. Lipid Res. 51 2010 3145 3157
    • (2010) J. Lipid Res. , vol.51 , pp. 3145-3157
    • Kim, S.J.1    Nian, C.2    McIntosh, C.H.3
  • 107
    • 84873029402 scopus 로고    scopus 로고
    • Resistin knockout mice exhibit impaired adipocyte glucose-dependent insulinotropic polypeptide receptor (GIPR) expression
    • S.J. Kim, C. Nian, and C.H. McIntosh Resistin knockout mice exhibit impaired adipocyte glucose-dependent insulinotropic polypeptide receptor (GIPR) expression Diabetes 62 2013 471 477
    • (2013) Diabetes , vol.62 , pp. 471-477
    • Kim, S.J.1    Nian, C.2    McIntosh, C.H.3
  • 108
    • 0024386369 scopus 로고
    • Insulin regulation of lipoprotein lipase activity in 3T3-L1 adipocytes is mediated at posttranscriptional and posttranslational levels
    • C.F. Semenkovich, M. Wims, L. Noe, J. Etienne, and L. Chan Insulin regulation of lipoprotein lipase activity in 3T3-L1 adipocytes is mediated at posttranscriptional and posttranslational levels J. Biol. Chem. 264 1989 9030 9038 (Pubitemid 19151633)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.15 , pp. 9030-9038
    • Semenkovich, C.F.1    Wims, M.2    Noe, L.3    Etienne, J.4    Chan, L.5
  • 109
    • 0029866946 scopus 로고    scopus 로고
    • Fatty acids regulate the expression of lipoprotein lipase gene and activity in preadipose and adipose cells
    • E.Z. Amri, L. Teboul, C. Vannier, P.A. Grimaldi, and G. Ailhaud Fatty acids regulate the expression of lipoprotein lipase gene and activity in preadipose and adipose cells Biochem. J. 314 Pt 2 1996 541 546 (Pubitemid 26074768)
    • (1996) Biochemical Journal , vol.314 , Issue.2 , pp. 541-546
    • Amri, E.-Z.1    Teboul, L.2    Vannier, C.3    Grimaldi, P.-A.4    Ailhaud, G.5
  • 110
    • 0030325227 scopus 로고    scopus 로고
    • Regulation of triglyceride metabolism by PPARs: Fibrates and thiazolidinediones have distinct effects
    • J. Auwerx, K. Schoonjans, J.C. Fruchart, and B. Staels Regulation of triglyceride metabolism by PPARs: fibrates and thiazolidinediones have distinct effects J. Atheroscler. Thromb. 3 1996 81 89
    • (1996) J. Atheroscler. Thromb. , vol.3 , pp. 81-89
    • Auwerx, J.1    Schoonjans, K.2    Fruchart, J.C.3    Staels, B.4
  • 111
    • 0029791412 scopus 로고    scopus 로고
    • PPARα and PPARγ activators direct a distinct tissue-specific transcriptional response via a PPRE in the lipoprotein lipase gene
    • K. Schoonjans, J. Peinado-Onsurbe, A.M. Lefebvre, R.A. Heyman, M. Briggs, S. Deeb, B. Staels, and J. Auwerx PPARalpha and PPARgamma activators direct a distinct tissue-specific transcriptional response via a PPRE in the lipoprotein lipase gene EMBO J. 15 1996 5336 5348 (Pubitemid 26336216)
    • (1996) EMBO Journal , vol.15 , Issue.19 , pp. 5336-5348
    • Schoonjans, K.1    Peinado-Onsurbe, J.2    Lefebvre, A.-M.3    Heyman, R.A.4    Briggs, M.5    Deeb, S.6    Staels, B.7    Auwerx, J.8
  • 113
    • 33748516743 scopus 로고    scopus 로고
    • Insulin sensitisation affects lipoprotein lipase transport in type 2 diabetes: Role of adipose tissue and skeletal muscle in response to rosiglitazone
    • DOI 10.1007/s00125-006-0370-9
    • G.D. Tan, G. Olivecrona, H. Vidal, K.N. Frayn, and F. Karpe Insulin sensitisation affects lipoprotein lipase transport in type 2 diabetes: role of adipose tissue and skeletal muscle in response to rosiglitazone Diabetologia 49 2006 2412 2418 (Pubitemid 44359103)
    • (2006) Diabetologia , vol.49 , Issue.10 , pp. 2412-2418
    • Tan, G.D.1    Olivecrona, G.2    Vidal, H.3    Frayn, K.N.4    Karpe, F.5
  • 115
    • 0034406804 scopus 로고    scopus 로고
    • Induction of LPL gene expression by sterols is mediated by a sterol regulatory element and is independent of the presence of multiple e boxes
    • K. Schoonjans, L. Gelman, C. Haby, M. Briggs, and J. Auwerx Induction of LPL gene expression by sterols is mediated by a sterol regulatory element and is independent of the presence of multiple E boxes J. Mol. Biol. 304 2000 323 334
    • (2000) J. Mol. Biol. , vol.304 , pp. 323-334
    • Schoonjans, K.1    Gelman, L.2    Haby, C.3    Briggs, M.4    Auwerx, J.5
  • 116
    • 0025997045 scopus 로고
    • Weight reduction increases adipose but decreases cardiac LPL in reduced-obese Zucker rats
    • D.H. Bessesen, A.D. Robertson, and R.H. Eckel Weight reduction increases adipose but decreases cardiac LPL in reduced-obese Zucker rats Am. J. Physiol. 261 1991 E246 E251
    • (1991) Am. J. Physiol. , vol.261
    • Bessesen, D.H.1    Robertson, A.D.2    Eckel, R.H.3
  • 117
    • 0027253433 scopus 로고
    • Changes in lipoprotein lipase activities in adipose tissue, heart and skeletal muscle during continuous or interrupted feeding
    • M.C. Sugden, M.J. Holness, and R.M. Howard Changes in lipoprotein lipase activities in adipose tissue, heart and skeletal muscle during continuous or interrupted feeding Biochem. J. 292 Pt 1 1993 113 119 (Pubitemid 23158969)
    • (1993) Biochemical Journal , vol.292 , Issue.1 , pp. 113-119
    • Sugden, M.C.1    Holness, M.J.2    Howard, R.M.3
  • 118
    • 0030775793 scopus 로고    scopus 로고
    • Regulation of adipose tissue lipoprotein lipase in young and old rats
    • M. Bergo, G. Olivecrona, and T. Olivecrona Regulation of adipose tissue lipoprotein lipase in young and old rats Int. J. Obes. Relat. Metab. Disord. 21 1997 980 986 (Pubitemid 27462401)
    • (1997) International Journal of Obesity , vol.21 , Issue.11 , pp. 980-986
    • Bergo, M.1    Olivecrona, G.2    Olivecrona, T.3
  • 119
  • 120
    • 0031818633 scopus 로고    scopus 로고
    • Effect of dietary macronutrient composition on tissue-specific lipoprotein lipase activity and insulin action in normal-weight subjects
    • T.J. Yost, D.R. Jensen, B.R. Haugen, and R.H. Eckel Effect of dietary macronutrient composition on tissue-specific lipoprotein lipase activity and insulin action in normal-weight subjects Am. J. Clin. Nutr. 68 1998 296 302 (Pubitemid 28355646)
    • (1998) American Journal of Clinical Nutrition , vol.68 , Issue.2 , pp. 296-302
    • Yost, T.J.1    Jensen, D.R.2    Haugen, B.R.3    Eckel, R.H.4
  • 121
    • 0013771080 scopus 로고
    • The ability of actinomycin D to increase the clearing-factor lipase activity of rat adipose tissue
    • G.R. Eagle, and D.S. Robinson The ability of actinomycin D to increase the clearing-factor lipase activity of rat adipose tissue Biochem. J. 93 1964 10C 11C
    • (1964) Biochem. J. , vol.93
    • Eagle, G.R.1    Robinson, D.S.2
  • 122
    • 0014252781 scopus 로고
    • Clearing-factor lipase in adipose tissue. Studies with puromycin and actinomycin
    • D.R. Wing, and D.S. Robinson Clearing-factor lipase in adipose tissue. Studies with puromycin and actinomycin Biochem. J. 106 1968 667 676
    • (1968) Biochem. J. , vol.106 , pp. 667-676
    • Wing, D.R.1    Robinson, D.S.2
  • 123
    • 0013916091 scopus 로고
    • Clearing-factor lipase in adipose tissue. Factors influencing the increase in enzyme activity produced on incubation of tissue from starved rats in vitro
    • D.R. Wing, M.R. Salaman, and D.S. Robinson Clearing-factor lipase in adipose tissue. Factors influencing the increase in enzyme activity produced on incubation of tissue from starved rats in vitro Biochem. J. 99 1966 648 656
    • (1966) Biochem. J. , vol.99 , pp. 648-656
    • Wing, D.R.1    Salaman, M.R.2    Robinson, D.S.3
  • 124
    • 0030040485 scopus 로고    scopus 로고
    • Forms of lipoprotein lipase in rat tissues: In adipose tissue the proportion of inactive lipase increases on fasting
    • M. Bergo, G. Olivecrona, and T. Olivecrona Forms of lipoprotein lipase in rat tissues: in adipose tissue the proportion of inactive lipase increases on fasting Biochem. J. 313 Pt 3 1996 893 898
    • (1996) Biochem. J. , vol.313 , Issue.PART 3 , pp. 893-898
    • Bergo, M.1    Olivecrona, G.2    Olivecrona, T.3
  • 125
    • 0037023683 scopus 로고    scopus 로고
    • Down-regulation of adipose tissue lipoprotein lipase during fasting requires that a gene, separate from the lipase gene, is switched on
    • DOI 10.1074/jbc.M200325200
    • M. Bergo, G. Wu, T. Ruge, and T. Olivecrona Down-regulation of adipose tissue lipoprotein lipase during fasting requires that a gene, separate from the lipase gene, is switched on J. Biol. Chem. 277 2002 11927 11932 (Pubitemid 34952751)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.14 , pp. 11927-11932
    • Bergo, M.1    Wu, G.2    Ruge, T.3    Olivecrona, T.4
  • 126
    • 0038146909 scopus 로고    scopus 로고
    • The distribution of lipoprotein lipase in rat adipose tissue: Changes with nutritional state engage the extracellular enzyme
    • DOI 10.1074/jbc.M212736200
    • G. Wu, G. Olivecrona, and T. Olivecrona The distribution of lipoprotein lipase in rat adipose tissue. Changes with nutritional state engage the extracellular enzyme J. Biol. Chem. 278 2003 11925 11930 (Pubitemid 36800165)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 11925-11930
    • Wu, G.1    Olivecrona, G.2    Olivecrona, T.3
  • 128
    • 0026032958 scopus 로고
    • Tissue-specific regulation of lipoprotein lipase activity by insulin/glucose in normal-weight humans
    • R.V. Farese Jr., T.J. Yost, and R.H. Eckel Tissue-specific regulation of lipoprotein lipase activity by insulin/glucose in normal-weight humans Metabolism 40 1991 214 216
    • (1991) Metabolism , vol.40 , pp. 214-216
    • Farese, Jr.R.V.1    Yost, T.J.2    Eckel, R.H.3
  • 129
    • 33746380871 scopus 로고    scopus 로고
    • Insulin downregulates angiopoietin-like protein 4 mRNA in 3T3-L1 adipocytes
    • DOI 10.1016/j.bbrc.2006.07.032, PII S0006291X06015750
    • T. Yamada, N. Ozaki, Y. Kato, Y. Miura, and Y. Oiso Insulin downregulates angiopoietin-like protein 4 mRNA in 3T3-L1 adipocytes Biochem. Biophys. Res. Commun. 347 2006 1138 1144 (Pubitemid 44118232)
    • (2006) Biochemical and Biophysical Research Communications , vol.347 , Issue.4 , pp. 1138-1144
    • Yamada, T.1    Ozaki, N.2    Kato, Y.3    Miura, Y.4    Oiso, Y.5
  • 130
    • 84899426867 scopus 로고    scopus 로고
    • Repression of glucocorticoid-stimulated angiopoietin-like 4 (Angptl4) gene transcription by insulin
    • T. Kuo, T.C. Chen, S. Yan, F. Foo, C. Ching, A. McQueen, and J.C. Wang Repression of glucocorticoid-stimulated angiopoietin-like 4 (Angptl4) gene transcription by insulin J. Lipid Res. 2014
    • (2014) J. Lipid Res.
    • Kuo, T.1    Chen, T.C.2    Yan, S.3    Foo, F.4    Ching, C.5    McQueen, A.6    Wang, J.C.7
  • 132
    • 4243586069 scopus 로고    scopus 로고
    • Comparative effects of insulin and isoproterenol on lipoprotein lipase in rat adipose cells
    • G.E. Chiappe de Cingalani, J.W. Goers, M. Giannotti, and C.I. Caldiz Comparative effects of insulin and isoproterenol on lipoprotein lipase in rat adipose cells Am. J. Physiol. 270 1996 C1461 C1467
    • (1996) Am. J. Physiol. , vol.270
    • Chiappe De Cingalani, G.E.1    Goers, J.W.2    Giannotti, M.3    Caldiz, C.I.4
  • 133
    • 0031901515 scopus 로고    scopus 로고
    • Insulin regulates lipoprotein lipase activity in rat adipose cells via wortmannin- and rapamycin-sensitive pathways
    • DOI 10.1016/S0026-0495(98)90239-6
    • F.B. Kraemer, D. Takeda, V. Natu, and C. Sztalryd Insulin regulates lipoprotein lipase activity in rat adipose cells via wortmannin- and rapamycin-sensitive pathways Metabolism 47 1998 555 559 (Pubitemid 28214005)
    • (1998) Metabolism: Clinical and Experimental , vol.47 , Issue.5 , pp. 555-559
    • Kraemer, F.B.1    Takeda, D.2    Natu, V.3    Sztalryd, C.4
  • 134
    • 79959562708 scopus 로고    scopus 로고
    • Fatty acids and hypoxia stimulate the expression and secretion of the adipokine ANGPTL4 (angiopoietin-like protein 4/fasting-induced adipose factor) by human adipocytes
    • P. Gonzalez-Muniesa, C. de Oliveira, F. Perez de Heredia, M.P. Thompson, and P. Trayhurn Fatty acids and hypoxia stimulate the expression and secretion of the adipokine ANGPTL4 (angiopoietin-like protein 4/fasting-induced adipose factor) by human adipocytes J. Nutrigenet. Nutrigenomics 4 2011 146 153
    • (2011) J. Nutrigenet. Nutrigenomics , vol.4 , pp. 146-153
    • Gonzalez-Muniesa, P.1    De Oliveira, C.2    Perez De Heredia, F.3    Thompson, M.P.4    Trayhurn, P.5
  • 135
    • 0028115762 scopus 로고
    • Long-chain fatty acids decrease lipoprotein lipase activity of cultured rat adipocyte precursors
    • DOI 10.1016/0026-0495(94)90236-4
    • J.L. Kirkland, C.H. Hollenberg, S. Kindler, and D.A. Roncari Long-chain fatty acids decrease lipoprotein lipase activity of cultured rat adipocyte precursors Metabolism 43 1994 144 151 (Pubitemid 24061844)
    • (1994) Metabolism: Clinical and Experimental , vol.43 , Issue.2 , pp. 144-151
    • Kirkland, J.L.1    Hollenberg, C.H.2    Kindler, S.3    Roncari, D.A.K.4
  • 136
    • 0014676576 scopus 로고
    • Hypertriglyceridemia in rats at simulated high altitudes
    • A. Louhija Hypertriglyceridemia in rats at simulated high altitudes Experientia 25 1969 248 249
    • (1969) Experientia , vol.25 , pp. 248-249
    • Louhija, A.1
  • 137
    • 18344405385 scopus 로고
    • The effect of experimental hypoxic hypoxia on the blood clearing factor
    • V.I. Uspenskii The effect of experimental hypoxic hypoxia on the blood clearing factor Patol. Fiziol. Eksp. Ter. 9 1965 88 89
    • (1965) Patol. Fiziol. Eksp. Ter. , vol.9 , pp. 88-89
    • Uspenskii, V.I.1
  • 138
  • 140
    • 35448934913 scopus 로고    scopus 로고
    • Dysregulation of the expression and secretion of inflammation-related adipokines by hypoxia in human adipocytes
    • DOI 10.1007/s00424-007-0301-8
    • B. Wang, I.S. Wood, and P. Trayhurn Dysregulation of the expression and secretion of inflammation-related adipokines by hypoxia in human adipocytes Pflugers Arch. - Eur. J. Physiol. 455 2007 479 492 (Pubitemid 47624196)
    • (2007) Pflugers Archiv European Journal of Physiology , vol.455 , Issue.3 , pp. 479-492
    • Wang, B.1    Wood, I.S.2    Trayhurn, P.3
  • 142
    • 34147173692 scopus 로고    scopus 로고
    • Retroperitoneal white adipose tissue lipoprotein lipase activity is rapidly down-regulated in response to acute stress
    • DOI 10.1194/jlr.M600487-JLR200
    • A. Casanovas, N. Parramon, F. de la Cruz, O. Andres, J. Terencio, M.D. Lopez-Tejero, and M. Llobera Retroperitoneal white adipose tissue lipoprotein lipase activity is rapidly down-regulated in response to acute stress J. Lipid Res. 48 2007 863 868 (Pubitemid 46557891)
    • (2007) Journal of Lipid Research , vol.48 , Issue.4 , pp. 863-868
    • Casanovas, A.1    Parramon, N.2    De La Cruz, F.3    Andres, O.4    Terencio, J.5    Lopez-Tejero, M.D.6    Llobera, M.7
  • 143
    • 0037044773 scopus 로고    scopus 로고
    • The translational regulation of lipoprotein lipase by epinephrine involves an RNA binding complex including the catalytic subunit of protein kinase A
    • DOI 10.1074/jbc.M202560200
    • G. Ranganathan, D. Phan, I.D. Pokrovskaya, J.E. McEwen, C. Li, and P.A. Kern The translational regulation of lipoprotein lipase by epinephrine involves an RNA binding complex including the catalytic subunit of protein kinase A J. Biol. Chem. 277 2002 43281 43287 (Pubitemid 35285715)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 43281-43287
    • Ranganathan, G.1    Phan, D.2    Pokrovskaya, I.D.3    McEwen, J.E.4    Li, C.5    Kern, P.A.6
  • 144
    • 0028809386 scopus 로고
    • Regulation of lipoprotein lipase translation by epinephrine in 3T3-L1 cells. Importance of the 3′ untranslated region
    • A. Yukht, R.C. Davis, J.M. Ong, G. Ranganathan, and P.A. Kern Regulation of lipoprotein lipase translation by epinephrine in 3T3-L1 cells. Importance of the 3′ untranslated region J. Clin. Invest. 96 1995 2438 2444
    • (1995) J. Clin. Invest. , vol.96 , pp. 2438-2444
    • Yukht, A.1    Davis, R.C.2    Ong, J.M.3    Ranganathan, G.4    Kern, P.A.5
  • 146
    • 27744521834 scopus 로고    scopus 로고
    • Triglyceride-rich lipoproteins as agents of innate immunity
    • A.M. Barcia, and H.W. Harris Triglyceride-rich lipoproteins as agents of innate immunity Clin. Infect. Dis. 41 Suppl. 7 2005 S498 S503
    • (2005) Clin. Infect. Dis. , vol.41 , Issue.SUPPL. 7
    • Barcia, A.M.1    Harris, H.W.2
  • 148
    • 0023177024 scopus 로고
    • Triacylglycerol kinetics in endotoxic rats with suppressed lipoprotein lipase activity
    • G.J. Bagby, C.B. Corll, and R.R. Martinez Triacylglycerol kinetics in endotoxic rats with suppressed lipoprotein lipase activity Am. J. Physiol. 253 1987 E59 E64
    • (1987) Am. J. Physiol. , vol.253
    • Bagby, G.J.1    Corll, C.B.2    Martinez, R.R.3
  • 149
    • 0018992531 scopus 로고
    • Lipoprotein lipase activity in rat heart and adipose tissue during endotoxic shock
    • G.J. Bagby, and J.A. Spitzer Lipoprotein lipase activity in rat heart and adipose tissue during endotoxic shock Am. J. Physiol. 238 1980 H325 H330
    • (1980) Am. J. Physiol. , vol.238
    • Bagby, G.J.1    Spitzer, J.A.2
  • 150
    • 0019447659 scopus 로고
    • Studies of endotoxin-induced decrease in lipoprotein lipase activity
    • DOI 10.1084/jem.154.3.631
    • M. Kawakami, and A. Cerami Studies of endotoxin-induced decrease in lipoprotein lipase activity J. Exp. Med. 154 1981 631 639 (Pubitemid 11060776)
    • (1981) Journal of Experimental Medicine , vol.154 , Issue.3 , pp. 631-639
    • Kawakami, M.1    Cerami, A.2
  • 151
    • 0036061919 scopus 로고    scopus 로고
    • Responses of adipose and muscle lipoprotein lipase to chronic infection and subsequent acute lipopolysaccharide challenge
    • DOI 10.1128/CDLI.9.4.771-776.2002
    • F. Picard, D. Arsenijevic, D. Richard, and Y. Deshaies Responses of adipose and muscle lipoprotein lipase to chronic infection and subsequent acute lipopolysaccharide challenge Clin. Diagn. Lab. Immunol. 9 2002 771 776 (Pubitemid 34773876)
    • (2002) Clinical and Diagnostic Laboratory Immunology , vol.9 , Issue.4 , pp. 771-776
    • Picard, F.1    Arsenijevic, D.2    Richard, D.3    Deshaies, Y.4
  • 152
    • 0027441573 scopus 로고
    • Endotoxin-induced hypertriglyceridemia is mediated by suppression of lipoprotein lipase at a post-transcriptional level
    • I. Gouni, K. Oka, J. Etienne, and L. Chan Endotoxin-induced hypertriglyceridemia is mediated by suppression of lipoprotein lipase at a post-transcriptional level J. Lipid Res. 34 1993 139 146 (Pubitemid 23016629)
    • (1993) Journal of Lipid Research , vol.34 , Issue.1 , pp. 139-146
    • Gouni, I.1    Oka, K.2    Etienne, J.3    Chan, L.4
  • 153
    • 0021836738 scopus 로고
    • Purification of cachectin, a lipoprotein lipase-suppressing hormone secreted by endotoxin-induced RAW 264.7 cells
    • DOI 10.1084/jem.161.5.984
    • B. Beutler, J. Mahoney, N. Le Trang, P. Pekala, and A. Cerami Purification of cachectin, a lipoprotein lipase-suppressing hormone secreted by endotoxin-induced RAW 264.7 cells J. Exp. Med. 161 1985 984 995 (Pubitemid 15011320)
    • (1985) Journal of Experimental Medicine , vol.161 , Issue.5 , pp. 984-995
    • Beutler, B.1    Mahoney, J.2    Le Trang, N.3
  • 154
    • 0024836241 scopus 로고
    • Cachectin/tumor necrosis factor decreases human adipose tissue lipoprotein lipase mRNA levels, synthesis, and activity
    • S.K. Fried, and R. Zechner Cachectin/tumor necrosis factor decreases human adipose tissue lipoprotein lipase mRNA levels, synthesis, and activity J. Lipid Res. 30 1989 1917 1923 (Pubitemid 20030370)
    • (1989) Journal of Lipid Research , vol.30 , Issue.12 , pp. 1917-1923
    • Fried, S.K.1    Zechner, R.2
  • 155
    • 0024600778 scopus 로고
    • Effect of tumor necrosis factor administration in vivo on lipoprotein lipase activity in various tissues of the rat
    • C. Grunfeld, R. Gulli, A.H. Moser, L.A. Gavin, and K.R. Feingold Effect of tumor necrosis factor administration in vivo on lipoprotein lipase activity in various tissues of the rat J. Lipid Res. 30 1989 579 585 (Pubitemid 19107744)
    • (1989) Journal of Lipid Research , vol.30 , Issue.4 , pp. 579-585
    • Grunfeld, C.1    Gulli, R.2    Moser, A.H.3    Gavin, L.A.4    Feingold, K.R.5
  • 156
    • 0025351884 scopus 로고
    • Regulation of lipoprotein lipase activity and mRNA content in rat epididymal adipose tissue in vitro by recombinant tumour necrosis factor
    • A.G. Mackay, J.D. Oliver, and M.P. Rogers Regulation of lipoprotein lipase activity and mRNA content in rat epididymal adipose tissue in vitro by recombinant tumour necrosis factor Biochem. J. 269 1990 123 126 (Pubitemid 20210849)
    • (1990) Biochemical Journal , vol.269 , Issue.1 , pp. 123-126
    • Mackay, A.G.1    Oliver, J.D.2    Rogers, M.P.3
  • 157
  • 158
    • 0023927767 scopus 로고
    • Recombinant human cachectin/tumor necrosis factor but not interleukin-1 alpha downregulates lipoprotein lipase gene expression at the transcriptional level in mouse 3T3-L1 adipocytes
    • R. Zechner, T.C. Newman, B. Sherry, A. Cerami, and J.L. Breslow Recombinant human cachectin/tumor necrosis factor but not interleukin-1 alpha downregulates lipoprotein lipase gene expression at the transcriptional level in mouse 3T3-L1 adipocytes Mol. Cell. Biol. 8 1988 2394 2401
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2394-2401
    • Zechner, R.1    Newman, T.C.2    Sherry, B.3    Cerami, A.4    Breslow, J.L.5
  • 159
    • 1942486763 scopus 로고    scopus 로고
    • Rapid downregulation of adipose tissue lipoprotein lipase activity on food deprivation: Evidence that TNF-alpha is involved
    • G. Wu, P. Brouckaert, and T. Olivecrona Rapid downregulation of adipose tissue lipoprotein lipase activity on food deprivation: evidence that TNF-alpha is involved Am. J. Physiol. Endocrinol. Metab. 286 2004 E711 E717
    • (2004) Am. J. Physiol. Endocrinol. Metab. , vol.286
    • Wu, G.1    Brouckaert, P.2    Olivecrona, T.3
  • 160
    • 53049093871 scopus 로고    scopus 로고
    • Regulation of angiopoietin-like protein 4/fasting-induced adipose factor (Angptl4/FIAF) expression in mouse white adipose tissue and 3T3-L1 adipocytes
    • S. Dutton, and P. Trayhurn Regulation of angiopoietin-like protein 4/fasting-induced adipose factor (Angptl4/FIAF) expression in mouse white adipose tissue and 3T3-L1 adipocytes Br. J. Nutr. 100 2008 18 26
    • (2008) Br. J. Nutr. , vol.100 , pp. 18-26
    • Dutton, S.1    Trayhurn, P.2
  • 161
  • 162
    • 33749170655 scopus 로고    scopus 로고
    • Intramyocellular lipid content in human skeletal muscle
    • V.B. Schrauwen-Hinderling, M.K. Hesselink, P. Schrauwen, and M.E. Kooi Intramyocellular lipid content in human skeletal muscle Obesity (Silver Spring) 14 2006 357 367 (Pubitemid 46219752)
    • (2006) Obesity , vol.14 , Issue.3 , pp. 357-367
    • Schrauwen-Hinderling, V.B.1    Hesselink, M.K.C.2    Schrauwen, P.3    Kooi, M.E.4
  • 163
    • 1442276967 scopus 로고    scopus 로고
    • Systemic and Forearm Triglyceride Metabolism: Fate of Lipoprotein Lipase-Generated Glycerol and Free Fatty Acids
    • DOI 10.2337/diabetes.53.3.521
    • J.M. Miles, Y.S. Park, D. Walewicz, C. Russell-Lopez, S. Windsor, W.L. Isley, S.W. Coppack, and W.S. Harris Systemic and forearm triglyceride metabolism: fate of lipoprotein lipase-generated glycerol and free fatty acids Diabetes 53 2004 521 527 (Pubitemid 38270618)
    • (2004) Diabetes , vol.53 , Issue.3 , pp. 521-527
    • Miles, J.M.1    Park, Y.S.2    Walewicz, D.3    Russell-Lopez, C.4    Windsor, S.5    Isley, W.L.6    Coppack, S.W.7    Harris, W.S.8
  • 164
    • 0032426039 scopus 로고    scopus 로고
    • Role of local contractile activity and muscle fiber type on LPL regulation during exercise
    • M.T. Hamilton, J. Etienne, W.C. McClure, B.S. Pavey, and A.K. Holloway Role of local contractile activity and muscle fiber type on LPL regulation during exercise Am. J. Physiol. 275 1998 E1016 E1022
    • (1998) Am. J. Physiol. , vol.275
    • Hamilton, M.T.1    Etienne, J.2    McClure, W.C.3    Pavey, B.S.4    Holloway, A.K.5
  • 165
    • 0026713988 scopus 로고
    • Exercise training has a heparin-like effect on lipoprotein lipase activity in muscle
    • L.B. Oscai, R.W. Tsika, and D.A. Essig Exercise training has a heparin-like effect on lipoprotein lipase activity in muscle Can. J. Physiol. Pharmacol. 70 1992 905 909
    • (1992) Can. J. Physiol. Pharmacol. , vol.70 , pp. 905-909
    • Oscai, L.B.1    Tsika, R.W.2    Essig, D.A.3
  • 166
    • 0020556664 scopus 로고
    • The influence of starvation and refeeding on the lipoprotein lipase activity of skeletal muscle and adipose tissue of lean and obese Zucker rats
    • D.W. Quig, D.K. Layman, P.J. Bechtel, and L.R. Hackler The influence of starvation and refeeding on the lipoprotein lipase activity of skeletal muscle and adipose tissue of lean and obese Zucker rats J. Nutr. 113 1983 1150 1156 (Pubitemid 13037849)
    • (1983) Journal of Nutrition , vol.113 , Issue.6 , pp. 1150-1156
    • Quig, D.W.1    Layman, D.K.2    Bechtel, P.J.3    Hackler, L.R.4
  • 167
    • 0036811465 scopus 로고    scopus 로고
    • Skeletal muscle heterogeneity in fasting-induced upregulation of genes encoding UCP2, UCP3, PPARγ and key enzymes of lipid oxidation
    • DOI 10.1007/s00424-002-0879-9
    • S. Samec, J. Seydoux, A.P. Russell, J.P. Montani, and A.G. Dulloo Skeletal muscle heterogeneity in fasting-induced upregulation of genes encoding UCP2, UCP3, PPARgamma and key enzymes of lipid oxidation Pflugers Arch. - Eur. J. Physiol. 445 2002 80 86 (Pubitemid 35370418)
    • (2002) Pflugers Archiv European Journal of Physiology , vol.445 , Issue.1 , pp. 80-86
    • Samec, S.1    Seydoux, J.2    Russell, A.P.3    Montani, J.P.4    Dulloo, A.G.5
  • 169
    • 0037341240 scopus 로고    scopus 로고
    • Effect of short-term fasting and refeeding on transcriptional regulation of metabolic genes in human skeletal muscle
    • DOI 10.2337/diabetes.52.3.657
    • H. Pilegaard, B. Saltin, and P.D. Neufer Effect of short-term fasting and refeeding on transcriptional regulation of metabolic genes in human skeletal muscle Diabetes 52 2003 657 662 (Pubitemid 36323571)
    • (2003) Diabetes , vol.52 , Issue.3 , pp. 657-662
    • Pilegaard, H.1    Saltin, B.2    Neufer, P.D.3
  • 170
    • 0033921984 scopus 로고    scopus 로고
    • Exercise attenuates the fasting-induced transcriptional activation of metabolic genes in skeletal muscle
    • A.L. Hildebrandt, and P.D. Neufer Exercise attenuates the fasting-induced transcriptional activation of metabolic genes in skeletal muscle Am. J. Physiol. Endocrinol. Metab. 278 2000 E1078 E1086
    • (2000) Am. J. Physiol. Endocrinol. Metab. , vol.278
    • Hildebrandt, A.L.1    Neufer, P.D.2
  • 171
    • 0037432191 scopus 로고    scopus 로고
    • A forkhead transcription factor FKHR up-regulates lipoprotein lipase expression in skeletal muscle
    • DOI 10.1016/S0014-5793(03)00062-0
    • Y. Kamei, J. Mizukami, S. Miura, M. Suzuki, N. Takahashi, T. Kawada, T. Taniguchi, and O. Ezaki A forkhead transcription factor FKHR up-regulates lipoprotein lipase expression in skeletal muscle FEBS Lett. 536 2003 232 236 (Pubitemid 36206437)
    • (2003) FEBS Letters , vol.536 , Issue.1-3 , pp. 232-236
    • Kamei, Y.1    Mizukami, J.2    Miura, S.3    Suzuki, M.4    Takahashi, N.5    Kawada, T.6    Taniguchi, T.7    Ezaki, O.8
  • 174
    • 0033928070 scopus 로고    scopus 로고
    • Exercise induces lipoprotein lipase and GLUT-4 protein in muscle independent of adrenergic-receptor signaling
    • J.S. Greiwe, J.O. Holloszy, and C.F. Semenkovich Exercise induces lipoprotein lipase and GLUT-4 protein in muscle independent of adrenergic-receptor signaling J. Appl. Physiol. 89 2000 176 181 (Pubitemid 30482578)
    • (2000) Journal of Applied Physiology , vol.89 , Issue.1 , pp. 176-181
    • Greiwe, J.S.1    Holloszy, J.O.2    Semenkovich, C.F.3
  • 176
    • 0037095899 scopus 로고    scopus 로고
    • Influence of pre-exercise muscle glycogen content on exercise-induced transcriptional regulation of metabolic genes
    • DOI 10.1113/jphysiol.2002.016832
    • H. Pilegaard, C. Keller, A. Steensberg, J.W. Helge, B.K. Pedersen, B. Saltin, and P.D. Neufer Influence of pre-exercise muscle glycogen content on exercise-induced transcriptional regulation of metabolic genes J. Physiol. 541 2002 261 271 (Pubitemid 35190197)
    • (2002) Journal of Physiology , vol.541 , Issue.1 , pp. 261-271
    • Pilegaard, H.1    Keller, C.2    Steensberg, A.3    Helge, J.W.4    Pedersen, B.K.5    Saltin, B.6    Darrell Neufer, P.7
  • 178
    • 0030956572 scopus 로고    scopus 로고
    • Induction of human skeletal muscle lipoprotein lipase gene expression by short-term exercise is transient
    • R.L. Seip, K. Mair, T.G. Cole, and C.F. Semenkovich Induction of human skeletal muscle lipoprotein lipase gene expression by short-term exercise is transient Am. J. Physiol. 272 1997 E255 E261
    • (1997) Am. J. Physiol. , vol.272
    • Seip, R.L.1    Mair, K.2    Cole, T.G.3    Semenkovich, C.F.4
  • 179
    • 11244311656 scopus 로고    scopus 로고
    • Are exercise-induced genes induced by exercise?
    • DOI 10.1096/fj.04-2084fje
    • K. Vissing, J.L. Andersen, and P. Schjerling Are exercise-induced genes induced by exercise? FASEB J. 19 2005 94 96 (Pubitemid 40069929)
    • (2005) FASEB Journal , vol.19 , Issue.1 , pp. 94-96
    • Vissing, K.1    Andersen, J.L.2    Schjerling, P.3
  • 181
    • 0027498235 scopus 로고
    • Tissue-specific alterations in lipoprotein lipase activity in rat after chronic infusion of isoproterenol
    • Y. Deshaies, A. Geloen, A. Paulin, A. Marette, and L.J. Bukowiecki Tissue-specific alterations in lipoprotein lipase activity in the rat after chronic infusion of isoproterenol Horm. Metab. Res. Hormon- und Stoffwechselforschung = Hormones et metabolisme 25 1993 13 16 (Pubitemid 23035812)
    • (1993) Hormone and Metabolic Research , vol.25 , Issue.1 , pp. 13-16
    • Deshaies, Y.1    Geloen, A.2    Paulin, A.3    Marette, A.4    Bukowiecki, L.J.5
  • 182
    • 75849163636 scopus 로고    scopus 로고
    • Independent and combined effects of aerobic exercise and pharmacological strategies on serum triglyceride concentrations: A qualitative review
    • E.P. Plaisance, P.W. Grandjean, and A.J. Mahurin Independent and combined effects of aerobic exercise and pharmacological strategies on serum triglyceride concentrations: a qualitative review Phys. Sportsmed. 37 2009 11 19
    • (2009) Phys. Sportsmed. , vol.37 , pp. 11-19
    • Plaisance, E.P.1    Grandjean, P.W.2    Mahurin, A.J.3
  • 183
    • 0029550543 scopus 로고
    • Effects of exercise training and feeding on lipoprotein lipase gene expression in adipose tissue, heart, and skeletal muscle of the rat
    • DOI 10.1016/0026-0495(95)90081-0
    • J.M. Ong, R.B. Simsolo, M. Saghizadeh, J.W. Goers, and P.A. Kern Effects of exercise training and feeding on lipoprotein lipase gene expression in adipose tissue, heart, and skeletal muscle of the rat Metabolism 44 1995 1596 1605 (Pubitemid 26102600)
    • (1995) Metabolism: Clinical and Experimental , vol.44 , Issue.12 , pp. 1596-1605
    • Ong, J.M.1    Simsolo, R.B.2    Saghizadeh, M.3    Goers, J.W.F.4    Kern, P.A.5
  • 184
    • 0018602501 scopus 로고
    • Changes in lipoprotein-lipase activity and lipid stores in human skeletal muscle with prolonged heavy exercise
    • H. Lithell, J. Orlander, R. Schele, B. Sjodin, and J. Karlsson Changes in lipoprotein-lipase activity and lipid stores in human skeletal muscle with prolonged heavy exercise Acta Physiol. Scand. 107 1979 257 261 (Pubitemid 10172575)
    • (1979) Acta Physiologica Scandinavica , vol.107 , Issue.3 , pp. 257-261
    • Lithell, H.1    Orlander, J.2    Schele, R.3
  • 185
    • 0018163729 scopus 로고
    • Lipoprotein lipase activity in adipose tissue and skeletal muscle of runners: Relation to serum lipoproteins
    • E.A. Nikkila, M.R. Taskinen, S. Rehunen, and M. Harkonen Lipoprotein lipase activity in adipose tissue and skeletal muscle of runners: relation to serum lipoproteins Metabolism 27 1978 1661 1667
    • (1978) Metabolism , vol.27 , pp. 1661-1667
    • Nikkila, E.A.1    Taskinen, M.R.2    Rehunen, S.3    Harkonen, M.4
  • 186
    • 0018971223 scopus 로고
    • Effect of acute vigorous exercise on lipoprotein lipase activity of adipose tissue and skeletal muscle in physically active men
    • M.R. Taskinen, and E.A. Nikkila Effect of acute vigorous exercise on lipoprotein lipase activity of adipose tissue and skeletal muscle in physically active men Artery 6 1980 471 483 (Pubitemid 10040865)
    • (1980) Artery , vol.6 , Issue.6 , pp. 471-483
    • Taskinen, M.R.1    Nikkila, E.A.2    Rehunen, S.3    Gordin, A.4
  • 187
    • 0141746249 scopus 로고    scopus 로고
    • Suppression of skeletal muscle lipoprotein lipase activity during physical inactivity: A molecular reason to maintain daily low-intensity activity
    • DOI 10.1113/jphysiol.2003.045591
    • L. Bey, and M.T. Hamilton Suppression of skeletal muscle lipoprotein lipase activity during physical inactivity: a molecular reason to maintain daily low-intensity activity J. Physiol. 551 2003 673 682 (Pubitemid 37121722)
    • (2003) Journal of Physiology , vol.551 , Issue.2 , pp. 673-682
    • Bey, L.1    Hamilton, M.T.2
  • 188
    • 0027365334 scopus 로고
    • The regulation of adipose tissue and muscle lipoprotein lipase in runners by detraining
    • R.B. Simsolo, J.M. Ong, and P.A. Kern The regulation of adipose tissue and muscle lipoprotein lipase in runners by detraining J. Clin. Invest. 92 1993 2124 2130 (Pubitemid 23333515)
    • (1993) Journal of Clinical Investigation , vol.92 , Issue.5 , pp. 2124-2130
    • Simsolo, R.B.1    Ong, J.M.2    Kern, P.A.3
  • 189
    • 33747872227 scopus 로고    scopus 로고
    • Modification of myocardial substrate use as a therapy for heart failure
    • DOI 10.1038/ncpcardio0583, PII NCPCARDIO0583
    • K. Abozguia, K. Clarke, L. Lee, and M. Frenneaux Modification of myocardial substrate use as a therapy for heart failure Nat. Clin. Pract. Cardiovasc. Med. 3 2006 490 498 (Pubitemid 44288462)
    • (2006) Nature Clinical Practice Cardiovascular Medicine , vol.3 , Issue.9 , pp. 490-498
    • Abozguia, K.1    Clarke, K.2    Lee, L.3    Frenneaux, M.4
  • 190
    • 21244492310 scopus 로고    scopus 로고
    • Myocardial substrate metabolism in the normal and failing heart
    • DOI 10.1152/physrev.00006.2004
    • W.C. Stanley, F.A. Recchia, and G.D. Lopaschuk Myocardial substrate metabolism in the normal and failing heart Physiol. Rev. 85 2005 1093 1129 (Pubitemid 40894649)
    • (2005) Physiological Reviews , vol.85 , Issue.3 , pp. 1093-1129
    • Stanley, W.C.1    Recchia, F.A.2    Lopaschuk, G.D.3
  • 191
    • 34248370974 scopus 로고    scopus 로고
    • Lipids in the heart: A source of fuel and a source of toxins
    • DOI 10.1097/MOL.0b013e32814a57db, PII 0004143320070600000009
    • T.S. Park, H. Yamashita, W.S. Blaner, and I.J. Goldberg Lipids in the heart: a source of fuel and a source of toxins Curr. Opin. Lipidol. 18 2007 277 282 (Pubitemid 46743051)
    • (2007) Current Opinion in Lipidology , vol.18 , Issue.3 , pp. 277-282
    • Park, T.-S.1    Yamashita, H.2    Blaner, W.S.3    Goldberg, I.J.4
  • 193
    • 0014752306 scopus 로고
    • The effect of fasting on the utilization of chylomicron triglyceride fatty acids in relation to clearing factor lipase (lipoprotein lipase) releasable by heparin in the perfused rat heart
    • J. Borensztajn, and D.S. Robinson The effect of fasting on the utilization of chylomicron triglyceride fatty acids in relation to clearing factor lipase (lipoprotein lipase) releasable by heparin in the perfused rat heart J. Lipid Res. 11 1970 111 117
    • (1970) J. Lipid Res. , vol.11 , pp. 111-117
    • Borensztajn, J.1    Robinson, D.S.2
  • 194
    • 34250671272 scopus 로고
    • The effect of fasting on the lipoprotein lipase activity of rat heart and diaphragm
    • C.H. Hollenberg The effect of fasting on the lipoprotein lipase activity of rat heart and diaphragm J. Clin. Invest. 39 1960 1282 1287
    • (1960) J. Clin. Invest. , vol.39 , pp. 1282-1287
    • Hollenberg, C.H.1
  • 195
    • 0023892975 scopus 로고
    • Regulation of lipoprotein lipase in different rat tissues
    • M. Kuwajima, D.W. Foster, and J.D. McGarry Regulation of lipoprotein lipase in different rat tissues Metabolism 37 1988 597 601
    • (1988) Metabolism , vol.37 , pp. 597-601
    • Kuwajima, M.1    Foster, D.W.2    McGarry, J.D.3
  • 200
    • 0026665146 scopus 로고
    • Synthesis and transport of lipoprotein lipase in perfused guinea pig hearts
    • G. Liu, and T. Olivecrona Synthesis and transport of lipoprotein lipase in perfused guinea pig hearts Am. J. Physiol. 263 1992 H438 H446
    • (1992) Am. J. Physiol. , vol.263
    • Liu, G.1    Olivecrona, T.2
  • 201
    • 35148829469 scopus 로고    scopus 로고
    • A transcription-dependent mechanism, akin to that in adipose tissue, modulates lipoprotein lipase activity in rat heart
    • G. Wu, L. Zhang, J. Gupta, G. Olivecrona, and T. Olivecrona A transcription-dependent mechanism, akin to that in adipose tissue, modulates lipoprotein lipase activity in rat heart Am. J. Physiol. Endocrinol. Metab. 293 2007 E908 E915
    • (2007) Am. J. Physiol. Endocrinol. Metab. , vol.293
    • Wu, G.1    Zhang, L.2    Gupta, J.3    Olivecrona, G.4    Olivecrona, T.5
  • 202
    • 0034890019 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-alpha ligands inhibit cardiac lipoprotein lipase activity
    • R. Carroll, and D.L. Severson Peroxisome proliferator-activated receptor-alpha ligands inhibit cardiac lipoprotein lipase activity Am. J. Physiol. Heart Circ. Physiol. 281 2001 H888 H894
    • (2001) Am. J. Physiol. Heart Circ. Physiol. , vol.281
    • Carroll, R.1    Severson, D.L.2
  • 203
    • 78649909203 scopus 로고    scopus 로고
    • Does long-term metformin treatment increase cardiac lipoprotein lipase?
    • D. Hauton Does long-term metformin treatment increase cardiac lipoprotein lipase? Metabolism 60 2011 32 42
    • (2011) Metabolism , vol.60 , pp. 32-42
    • Hauton, D.1
  • 204
    • 0016062804 scopus 로고
    • Effects of cold exposure on heart clearing factor lipase and triglyceride utilization in the rat
    • M.P. Rogers, and D.S. Robinson Effects of cold exposure on heart clearing factor lipase and triglyceride utilization in the rat J. Lipid Res. 15 1974 263 272
    • (1974) J. Lipid Res. , vol.15 , pp. 263-272
    • Rogers, M.P.1    Robinson, D.S.2
  • 205
    • 52049127012 scopus 로고    scopus 로고
    • Cold acclimation induces physiological cardiac hypertrophy and increases assimilation of triacylglycerol metabolism through lipoprotein lipase
    • Y. Cheng, and D. Hauton Cold acclimation induces physiological cardiac hypertrophy and increases assimilation of triacylglycerol metabolism through lipoprotein lipase Biochim. Biophys. Acta 1781 2008 618 626
    • (2008) Biochim. Biophys. Acta , vol.1781 , pp. 618-626
    • Cheng, Y.1    Hauton, D.2
  • 206
    • 0347989317 scopus 로고    scopus 로고
    • Brown Adipose Tissue: Function and Physiological Significance
    • DOI 10.1152/physrev.00015.2003
    • B. Cannon, and J. Nedergaard Brown adipose tissue: function and physiological significance Physiol. Rev. 84 2004 277 359 (Pubitemid 38054374)
    • (2004) Physiological Reviews , vol.84 , Issue.1 , pp. 277-359
    • Cannon, B.1    Nedergaard, J.2
  • 213
    • 0021821435 scopus 로고
    • Effect of temperature on lipoprotein lipase and lipogenic enzyme activities in brown adipose tissue of hypophysectomized rats
    • M. Goubern, M.C. Laury, L. Zizine, and R. Portet Effect of temperature on lipoprotein lipase and lipogenic enzyme activities in brown adipose tissue of hypophysectomized rats Horm. Metab. Res. Hormon- und Stoffwechselforschung = Hormones et metabolisme 17 1985 176 180 (Pubitemid 15062940)
    • (1985) Hormone and Metabolic Research , vol.17 , Issue.4 , pp. 176-180
    • Goubern, M.1    Laury, M.C.2    Zizine, L.3    Portet, R.4
  • 214
    • 0031744430 scopus 로고    scopus 로고
    • Beta-adrenergic modulation of triglyceridemia under increased energy expenditure
    • L. Mantha, and Y. Deshaies Beta-adrenergic modulation of triglyceridemia under increased energy expenditure Am. J. Physiol. 274 1998 R1769 R1776
    • (1998) Am. J. Physiol. , vol.274
    • Mantha, L.1    Deshaies, Y.2
  • 216
    • 0021952845 scopus 로고
    • Effects of cold acclimation on the activity of lipoprotein lipase in adipose tissues of genetically obese Zucker rats
    • R. Bertin, M. Triconnet, and R. Portet Effects of cold acclimation on the activity of lipoprotein lipase in adipose tissues of genetically obese Zucker rats Comp. Biochem. Physiol. B 81 1985 797 801
    • (1985) Comp. Biochem. Physiol. B , vol.81 , pp. 797-801
    • Bertin, R.1    Triconnet, M.2    Portet, R.3
  • 217
    • 0011246116 scopus 로고
    • Beta-adrenergic stimulation of lipoprotein lipase in rat brown adipose tissue during acclimation to cold
    • C. Carneheim, J. Nedergaard, and B. Cannon Beta-adrenergic stimulation of lipoprotein lipase in rat brown adipose tissue during acclimation to cold Am. J. Physiol. 246 1984 E327 E333
    • (1984) Am. J. Physiol. , vol.246
    • Carneheim, C.1    Nedergaard, J.2    Cannon, B.3
  • 218
    • 0015082039 scopus 로고
    • Response of lipoprotein lipase in various tissues to cold exposure
    • M.W. Radomski, and T. Orme Response of lipoprotein lipase in various tissues to cold exposure Am. J. Physiol. 220 1971 1852 1856
    • (1971) Am. J. Physiol. , vol.220 , pp. 1852-1856
    • Radomski, M.W.1    Orme, T.2
  • 219
    • 0023837744 scopus 로고
    • Cold-induced beta-adrenergic recruitment of lipoprotein lipase in brown fat is due to increased transcription
    • C. Carneheim, J. Nedergaard, and B. Cannon Cold-induced beta-adrenergic recruitment of lipoprotein lipase in brown fat is due to increased transcription Am. J. Physiol. 254 1988 E155 E161
    • (1988) Am. J. Physiol. , vol.254
    • Carneheim, C.1    Nedergaard, J.2    Cannon, B.3
  • 221
  • 222
    • 0031045726 scopus 로고    scopus 로고
    • 1-adrenergic receptors
    • P. Kuusela, S. Rehnmark, A. Jacobsson, B. Cannon, and J. Nedergaard Adrenergic stimulation of lipoprotein lipase gene expression in rat brown adipocytes differentiated in culture: mediation via beta3- and alpha1-adrenergic receptors Biochem. J. 321 Pt 3 1997 759 767 (Pubitemid 27084886)
    • (1997) Biochemical Journal , vol.321 , Issue.3 , pp. 759-767
    • Kuusela, P.1    Rehnmark, S.2    Jacobsson, A.3    Cannon, B.4    Nedergaard, J.5
  • 223
    • 0024332102 scopus 로고
    • Short photoperiod and cold activate brown fat lipoprotein lipase in the Djungarian hamster
    • M. Klingenspor, S. Klaus, H. Wiesinger, and G. Heldmaier Short photoperiod and cold activate brown fat lipoprotein lipase in the Djungarian hamster Am. J. Physiol. 257 1989 R1123 R1127
    • (1989) Am. J. Physiol. , vol.257
    • Klingenspor, M.1    Klaus, S.2    Wiesinger, H.3    Heldmaier, G.4
  • 224
    • 0025325668 scopus 로고
    • Inhibition of 5'-deiodination of thyroxine suppresses the cold-induced increase in brown adipose tissue messenger ribonucleic acid for mitochondrial uncoupling protein without influencing lipoprotein lipase activity
    • R.J. Reiter, S. Klaus, C. Ebbinghaus, G. Heldmaier, U. Redlin, D. Ricquier, M.K. Vaughan, and S. Steinlechner Inhibition of 5′-deiodination of thyroxine suppresses the cold-induced increase in brown adipose tissue messenger ribonucleic acid for mitochondrial uncoupling protein without influencing lipoprotein lipase activity Endocrinology 126 1990 2550 2554 (Pubitemid 20173046)
    • (1990) Endocrinology , vol.126 , Issue.5 , pp. 2550-2554
    • Reiter, R.J.1    Klaus, S.2    Ebbinghaus, C.3    Heldmaier, G.4    Redlin, U.5    Ricquier, D.6    Vaughan, M.K.7    Steinlechner, S.8
  • 225
    • 0024457064 scopus 로고
    • Effects of norepinephrine and denervation on brown adipose tissue in Syrian hamsters
    • J.M. Hamilton, T.J. Bartness, and G.N. Wade Effects of norepinephrine and denervation on brown adipose tissue in Syrian hamsters Am. J. Physiol. 257 1989 R396 R404
    • (1989) Am. J. Physiol. , vol.257
    • Hamilton, J.M.1    Bartness, T.J.2    Wade, G.N.3
  • 226
    • 0037312845 scopus 로고    scopus 로고
    • PPAR-γ activation mediates adipose depot-specific effects on gene expression and lipoprotein lipase activity: Mechanisms for modulation of postprandial lipemia and differential adipose accretion
    • DOI 10.2337/diabetes.52.2.291
    • M. Laplante, H. Sell, K.L. MacNaul, D. Richard, J.P. Berger, and Y. Deshaies PPAR-gamma activation mediates adipose depot-specific effects on gene expression and lipoprotein lipase activity: mechanisms for modulation of postprandial lipemia and differential adipose accretion Diabetes 52 2003 291 299 (Pubitemid 36173181)
    • (2003) Diabetes , vol.52 , Issue.2 , pp. 291-299
    • Laplante, M.1    Sell, H.2    MacNaul, K.L.3    Richard, D.4    Berger, J.P.5    Deshaies, Y.6
  • 229
    • 21344449736 scopus 로고    scopus 로고
    • Rosiglitazone up-regulates lipoprotein lipase, hormone-sensitive lipase and uncoupling protein-1, and down-regulates insulin-induced fatty acid synthase gene expression in brown adipocytes of Wistar rats
    • DOI 10.1007/s00125-005-1744-0
    • T. Teruel, R. Hernandez, E. Rial, A. Martin-Hidalgo, and M. Lorenzo Rosiglitazone up-regulates lipoprotein lipase, hormone-sensitive lipase and uncoupling protein-1, and down-regulates insulin-induced fatty acid synthase gene expression in brown adipocytes of Wistar rats Diabetologia 48 2005 1180 1188 (Pubitemid 40909655)
    • (2005) Diabetologia , vol.48 , Issue.6 , pp. 1180-1188
    • Teruel, T.1    Hernandez, R.2    Rial, E.3    Martin-Hidalgo, A.4    Lorenzo, M.5
  • 230
    • 0020635463 scopus 로고
    • Novel regulation of lipoprotein lipase activity in rat brown adipose tissue: Effects of fasting and caloric restriction during refeeding
    • S.K. Fried, J.O. Hill, M. Nickel, and M. DiGirolamo Novel regulation of lipoprotein lipase activity in rat brown adipose tissue: effects of fasting and caloric restriction during refeeding J. Nutr. 113 1983 1870 1874 (Pubitemid 13024438)
    • (1983) Journal of Nutrition , vol.113 , Issue.9 , pp. 1870-1874
    • Fried, S.K.1    Hill, J.O.2    Nickel, M.3    DiGirolamo, M.4
  • 231
    • 0019415124 scopus 로고
    • Circadian rhythm and hormonal sensitivity of lipoprotein lipase activity in cold acclimated rats
    • M. Goubern, and R. Portet Circadian rhythm and hormonal sensitivity of lipoprotein lipase activity in cold acclimated rats Horm. Metab. Res. Hormon- und Stoffwechselforschung = Hormones et metabolisme 13 1981 73 77 (Pubitemid 11139760)
    • (1981) Hormone and Metabolic Research , vol.13 , Issue.2 , pp. 73-77
    • Goubern, M.1    Portet, R.2
  • 232
    • 0020040736 scopus 로고
    • Lipoprotein lipase secretion by human monocyte-derived macrophages
    • A. Chait, P.H. Iverius, and J.D. Brunzell Lipoprotein lipase secretion by human monocyte-derived macrophages J. Clin. Invest. 69 1982 490 493 (Pubitemid 12177628)
    • (1982) Journal of Clinical Investigation , vol.69 , Issue.2 , pp. 490-493
    • Chait, A.1    Iverius, P.H.2    Brunzell, J.D.3
  • 233
    • 72849178877 scopus 로고
    • 14C-labelled unesterified fatty acids by macrophages in vitro and the effect of clearing factor
    • 14C-labelled unesterified fatty acids by macrophages in vitro and the effect of clearing factor Q. J. Exp. Physiol. Cogn. Med. Sci. 45 1960 220 228
    • (1960) Q. J. Exp. Physiol. Cogn. Med. Sci. , vol.45 , pp. 220-228
    • Day, A.J.1
  • 236
    • 0027194102 scopus 로고
    • Evidence that cholesteryl ester and triglyceride accumulation in J774 macrophages induced by very low density lipoprotein subfractions occurs by different mechanisms
    • A.J. Evans, C.G. Sawyez, B.M. Wolfe, P.W. Connelly, G.F. Maguire, and M.W. Huff Evidence that cholesteryl ester and triglyceride accumulation in J774 macrophages induced by very low density lipoprotein subfractions occurs by different mechanisms J. Lipid Res. 34 1993 703 717 (Pubitemid 23152919)
    • (1993) Journal of Lipid Research , vol.34 , Issue.5 , pp. 703-717
    • Evans, A.J.1    Sawyez, C.G.2    Wolfe, B.M.3    Connelly, P.W.4    Maguire, G.F.5    Huff, M.W.6
  • 238
    • 0026751376 scopus 로고
    • Lipoprotein lipase is synthesized by macrophage-derived foam cells in human coronary atherosclerotic plaques
    • K.D. O'Brien, D. Gordon, S. Deeb, M. Ferguson, and A. Chait Lipoprotein lipase is synthesized by macrophage-derived foam cells in human coronary atherosclerotic plaques J. Clin. Invest. 89 1992 1544 1550
    • (1992) J. Clin. Invest. , vol.89 , pp. 1544-1550
    • O'Brien, K.D.1    Gordon, D.2    Deeb, S.3    Ferguson, M.4    Chait, A.5
  • 239
    • 0029991139 scopus 로고    scopus 로고
    • Lipoprotein lipase stimulates the binding and uptake of moderately oxidized low-density lipoprotein by J774 macrophages
    • W.L. Hendriks, H. van der Boom, L.C. van Vark, and L.M. Havekes Lipoprotein lipase stimulates the binding and uptake of moderately oxidized low-density lipoprotein by J774 macrophages Biochem. J. 314 Pt 2 1996 563 568 (Pubitemid 26074771)
    • (1996) Biochemical Journal , vol.314 , Issue.2 , pp. 563-568
    • Hendriks, W.L.1    Van Der Boom, H.2    Van Vark, L.C.3    Havekes, L.M.4
  • 240
    • 0027479260 scopus 로고
    • Absence of triglyceride accumulation in lipoprotein lipase-deficient human monocyte-macrophages incubated with human very low density lipoprotein
    • DOI 10.1210/jc.76.3.793
    • S.I. Skarlatos, H.L. Dichek, S.S. Fojo, H.B. Brewer, and H.S. Kruth Absence of triglyceride accumulation in lipoprotein lipase-deficient human monocyte-macrophages incubated with human very low density lipoprotein J. Clin. Endocrinol. Metab. 76 1993 793 796 (Pubitemid 23086507)
    • (1993) Journal of Clinical Endocrinology and Metabolism , vol.76 , Issue.3 , pp. 793-796
    • Skarlatos, S.I.1    Dichek, H.L.2    Fojo, S.S.3    Brewer, H.B.4    Kruth, H.S.5
  • 242
    • 0034714215 scopus 로고    scopus 로고
    • Macrophage lipoprotein lipase promotes foam cell formation and atherosclerosis in low density lipoprotein receptor-deficient mice
    • V.R. Babaev, M.B. Patel, C.F. Semenkovich, S. Fazio, and M.F. Linton Macrophage lipoprotein lipase promotes foam cell formation and atherosclerosis in low density lipoprotein receptor-deficient mice J. Biol. Chem. 275 2000 26293 26299
    • (2000) J. Biol. Chem. , vol.275 , pp. 26293-26299
    • Babaev, V.R.1    Patel, M.B.2    Semenkovich, C.F.3    Fazio, S.4    Linton, M.F.5
  • 244
    • 0035571614 scopus 로고    scopus 로고
    • Macrophage-specific expression of human lipoprotein lipase accelerates atherosclerosis in transgenic apolipoprotein E knockout mice but not in C57BL/6 mice
    • K. Wilson, G.L. Fry, D.A. Chappell, C.D. Sigmund, and J.D. Medh Macrophage-specific expression of human lipoprotein lipase accelerates atherosclerosis in transgenic apolipoprotein e knockout mice but not in C57BL/6 mice Arterioscler. Thromb. Vasc. Biol. 21 2001 1809 1815 (Pubitemid 34219785)
    • (2001) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.21 , Issue.11 , pp. 1809-1815
    • Wilson, K.1    Fry, G.L.2    Chappell, D.A.3    Sigmund, C.D.4    Medh, J.D.5
  • 249
    • 0022448108 scopus 로고
    • Effects of activation on lipoprotein lipase secretion by macrophages. Evidence for autoregulation
    • S.R. Behr, and F.B. Kraemer Effects of activation on lipoprotein lipase secretion by macrophages. Evidence for autoregulation J. Exp. Med. 164 1986 1362 1367 (Pubitemid 16031631)
    • (1986) Journal of Experimental Medicine , vol.164 , Issue.4 , pp. 1362-1367
    • Behr, S.R.1    Kraemer, F.B.2
  • 250
    • 0023134060 scopus 로고
    • Regulation of lipoprotein lipase secretion by mouse peritoneal macrophages
    • DOI 10.1016/0006-291X(87)90443-8
    • D.I. Goldberg, and J.C. Khoo Regulation of lipoprotein lipase secretion by mouse peritoneal macrophages Biochem. Biophys. Res. Commun. 142 1987 1 6 (Pubitemid 17000749)
    • (1987) Biochemical and Biophysical Research Communications , vol.142 , Issue.1 , pp. 1-6
    • Goldberg, D.I.1    Khoo, J.C.2
  • 252
    • 0023267440 scopus 로고
    • Bacterial lipopolysaccharide suppresses the expression of lipoprotein lipase in murine macrophages: A process independent of tumor necrosis factor or interleukin 1
    • DOI 10.1016/0165-2478(87)90034-4
    • O. Sopher, and R. Goldman Bacterial lipopolysaccharide suppresses the expression of lipoprotein lipase in murine macrophages: a process independent of tumor necrosis factor or interleukin 1 Immunol. Lett. 15 1987 261 265 (Pubitemid 17103672)
    • (1987) Immunology Letters , vol.15 , Issue.3 , pp. 261-265
    • Sopher, O.1    Goldman, R.2
  • 253
    • 0023761804 scopus 로고
    • Bacterial lipopolysaccharide reduces macrophage lipoprotein lipase levels: An effect that is independent of tumor necrosis factor
    • J.R. White, A. Chait, S.J. Klebanoff, S. Deeb, and J.D. Brunzell Bacterial lipopolysaccharide reduces macrophage lipoprotein lipase levels: an effect that is independent of tumor necrosis factor J. Lipid Res. 29 1988 1379 1385 (Pubitemid 18261060)
    • (1988) Journal of Lipid Research , vol.29 , Issue.10 , pp. 1379-1385
    • White, J.R.1    Chait, A.2    Klebanoff, S.J.3    Deeb, S.4    Brunzell, J.D.5
  • 254
    • 0030198984 scopus 로고    scopus 로고
    • Differential regulation of lipoprotein lipase in the macrophage J774.2 cell line by cytokines
    • DOI 10.1006/cyto.1996.0071
    • T.S. Tengku-Muhammad, T.R. Hughes, A. Cryer, and D.P. Ramji Differential regulation of lipoprotein lipase in the macrophage J774.2 cell line by cytokines Cytokine 8 1996 525 533 (Pubitemid 26294542)
    • (1996) Cytokine , vol.8 , Issue.7 , pp. 525-533
    • Tengku-Muhammad, T.S.1    Hughes, T.R.2    Cryer, A.3    Ramji, D.P.4
  • 256
    • 55049123960 scopus 로고    scopus 로고
    • The interferon-gamma-mediated inhibition of lipoprotein lipase gene transcription in macrophages involves casein kinase 2- and phosphoinositide-3- kinase-mediated regulation of transcription factors Sp1 and Sp3
    • S.M. Harris, E.J. Harvey, T.R. Hughes, and D.P. Ramji The interferon-gamma-mediated inhibition of lipoprotein lipase gene transcription in macrophages involves casein kinase 2- and phosphoinositide-3-kinase-mediated regulation of transcription factors Sp1 and Sp3 Cell. Signal. 20 2008 2296 2301
    • (2008) Cell. Signal. , vol.20 , pp. 2296-2301
    • Harris, S.M.1    Harvey, E.J.2    Hughes, T.R.3    Ramji, D.P.4
  • 258
    • 14844367135 scopus 로고    scopus 로고
    • A critical role for the Sp1-binding sites in the transforming growth factor-β-mediated inhibition of lipoprotein lipase gene expression in macrophages
    • DOI 10.1093/nar/gki280
    • S.A. Irvine, P. Foka, S.A. Rogers, J.R. Mead, and D.P. Ramji A critical role for the Sp1-binding sites in the transforming growth factor-beta-mediated inhibition of lipoprotein lipase gene expression in macrophages Nucleic Acids Res. 33 2005 1423 1434 (Pubitemid 41418372)
    • (2005) Nucleic Acids Research , vol.33 , Issue.5 , pp. 1423-1434
    • Irvine, S.A.1    Foka, P.2    Rogers, S.A.3    Mead, J.R.4    Ramji, D.P.5
  • 260
    • 53149131360 scopus 로고    scopus 로고
    • C-reactive protein enhances macrophage lipoprotein lipase expression
    • F. Maingrette, L. Li, and G. Renier C-reactive protein enhances macrophage lipoprotein lipase expression J. Lipid Res. 49 2008 1926 1935
    • (2008) J. Lipid Res. , vol.49 , pp. 1926-1935
    • Maingrette, F.1    Li, L.2    Renier, G.3
  • 262
    • 0029874894 scopus 로고    scopus 로고
    • Role of oxidant injury on macrophage lipoprotein lipase (LPL) production and sensitivity to LPL
    • G. Renier, A.C. Desfaits, A. Lambert, and R. Mikhail Role of oxidant injury on macrophage lipoprotein lipase (LPL) production and sensitivity to LPL J. Lipid Res. 37 1996 799 809 (Pubitemid 26140816)
    • (1996) Journal of Lipid Research , vol.37 , Issue.4 , pp. 799-809
    • Renier, G.1    Desfaits, A.-C.2    Lambert, A.3    Mikhail, R.4
  • 263
    • 0022831848 scopus 로고
    • Regulation of the secretion of lipoprotein lipase by mouse macrophages
    • DOI 10.1016/0167-4889(86)90197-7
    • S.R. Behr, and F.B. Kraemer Regulation of the secretion of lipoprotein lipase by mouse macrophages Biochim. Biophys. Acta 889 1986 346 354 (Pubitemid 17229828)
    • (1986) Biochimica et Biophysica Acta - Molecular Cell Research , vol.889 , Issue.3 , pp. 346-354
    • Behr, S.R.1    Kraemer, F.B.2
  • 264
    • 0025015070 scopus 로고
    • Control of lipoprotein lipase secretion by macrophages: Effect of macrophage differentiation agents
    • R. Goldman Control of lipoprotein lipase secretion by macrophages: effect of macrophage differentiation agents J. Leukoc. Biol. 47 1990 79 86 (Pubitemid 20015320)
    • (1990) Journal of Leukocyte Biology , vol.47 , Issue.1 , pp. 79-86
    • Goldman, R.1
  • 265
    • 0023039087 scopus 로고
    • Lipoprotein lipase in mouse peritoneal macrophages: The effects of insulin and dexamethasone
    • M. Kawakami, T. Murase, S. Ishibashi, N. Mori, and F. Takaku Lipoprotein lipase in mouse peritoneal macrophages: the effects of insulin and dexamethasone J. Biochem. 100 1986 1373 1378 (Pubitemid 17198438)
    • (1986) Journal of Biochemistry , vol.100 , Issue.5 , pp. 1373-1378
    • Kawakami, M.1    Murase, T.2    Ishibashi, S.3
  • 266
    • 0025882529 scopus 로고
    • Transcriptional activation of the lipoprotein lipase gene in macrophages by dexamethasone
    • W.S. Domin, A. Chait, and S.S. Deeb Transcriptional activation of the lipoprotein lipase gene in macrophages by dexamethasone Biochemistry 30 1991 2570 2574
    • (1991) Biochemistry , vol.30 , pp. 2570-2574
    • Domin, W.S.1    Chait, A.2    Deeb, S.S.3
  • 267
    • 18244381063 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor (PPAR) agonists decrease lipoprotein lipase secretion and glycated LDL uptake by human macrophages
    • DOI 10.1016/S0014-5793(02)02223-8, PII S0014579302022238
    • F.G. Gbaguidi, G. Chinetti, D. Milosavljevic, E. Teissier, J. Chapman, G. Olivecrona, J.C. Fruchart, S. Griglio, J. Fruchart-Najib, and B. Staels Peroxisome proliferator-activated receptor (PPAR) agonists decrease lipoprotein lipase secretion and glycated LDL uptake by human macrophages FEBS Lett. 512 2002 85 90 (Pubitemid 34164456)
    • (2002) FEBS Letters , vol.512 , Issue.1-3 , pp. 85-90
    • Gbaguidi, F.G.1    Chinetti, G.2    Milosavljevic, D.3    Teissier, E.4    Chapman, J.5    Olivecrona, G.6    Fruchart, J.C.7    Griglio, S.8    Fruchart-Najib, J.9    Staels, B.10
  • 268
    • 0036839889 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor α and γ agonists upregulate human macrophage lipoprotein lipase expression
    • DOI 10.1016/S0021-9150(02)00203-4, PII S0021915002002034
    • L. Li, M.C. Beauchamp, and G. Renier Peroxisome proliferator-activated receptor alpha and gamma agonists upregulate human macrophage lipoprotein lipase expression Atherosclerosis 165 2002 101 110 (Pubitemid 35223171)
    • (2002) Atherosclerosis , vol.165 , Issue.1 , pp. 101-110
    • Li, L.1    Beauchamp, M.-C.2    Renier, G.3
  • 269
    • 84870067162 scopus 로고    scopus 로고
    • Activation of peroxisome proliferator-activated receptor delta inhibits human macrophage foam cell formation and the inflammatory response induced by very low-density lipoprotein
    • L.A. Bojic, C.G. Sawyez, D.E. Telford, J.Y. Edwards, R.A. Hegele, and M.W. Huff Activation of peroxisome proliferator-activated receptor delta inhibits human macrophage foam cell formation and the inflammatory response induced by very low-density lipoprotein Arterioscler. Thromb. Vasc. Biol. 32 2012 2919 2928
    • (2012) Arterioscler. Thromb. Vasc. Biol. , vol.32 , pp. 2919-2928
    • Bojic, L.A.1    Sawyez, C.G.2    Telford, D.E.3    Edwards, J.Y.4    Hegele, R.A.5    Huff, M.W.6
  • 270
  • 271
    • 0026468372 scopus 로고
    • Regulation of lipoprotein lipase secretion in murine macrophages during foam cell formation in vitro. Effect of triglyceride-rich lipoproteins
    • O. Sofer, M. Fainaru, Z. Schafer, and R. Goldman Regulation of lipoprotein lipase secretion in murine macrophages during foam cell formation in vitro. Effect of triglyceride-rich lipoproteins Arterioscler. Thromb. 12 1992 1458 1466
    • (1992) Arterioscler. Thromb. , vol.12 , pp. 1458-1466
    • Sofer, O.1    Fainaru, M.2    Schafer, Z.3    Goldman, R.4
  • 272
    • 0035900749 scopus 로고    scopus 로고
    • Regulation of lipoprotein lipase by the oxysterol receptors, LXRalpha and LXRbeta
    • Y. Zhang, J.J. Repa, K. Gauthier, and D.J. Mangelsdorf Regulation of lipoprotein lipase by the oxysterol receptors, LXRalpha and LXRbeta J. Biol. Chem. 276 2001 43018 43024
    • (2001) J. Biol. Chem. , vol.276 , pp. 43018-43024
    • Zhang, Y.1    Repa, J.J.2    Gauthier, K.3    Mangelsdorf, D.J.4
  • 273
    • 0030060474 scopus 로고    scopus 로고
    • Oxysterols present in atherosclerotic tissue decrease the expression of lipoprotein lipase messenger RNA in human monocyte-derived macrophages
    • L.M. Hulten, H. Lindmark, U. Diczfalusy, I. Bjorkhem, M. Ottosson, Y. Liu, G. Bondjers, and O. Wiklund Oxysterols present in atherosclerotic tissue decrease the expression of lipoprotein lipase messenger RNA in human monocyte-derived macrophages J. Clin. Invest. 97 1996 461 468
    • (1996) J. Clin. Invest. , vol.97 , pp. 461-468
    • Hulten, L.M.1    Lindmark, H.2    Diczfalusy, U.3    Bjorkhem, I.4    Ottosson, M.5    Liu, Y.6    Bondjers, G.7    Wiklund, O.8
  • 275
    • 0023609842 scopus 로고
    • Effect of dibutyryl cyclic AMP and theophylline on lipoprotein lipase secretion by human monocyte-derived macrophages
    • DOI 10.1016/0014-5793(87)81153-5
    • J. Gardette, D. Margelin, J.C. Maziere, J. Bertrand, and J. Picard Effect of dibutyryl cyclic AMP and theophylline on lipoprotein lipase secretion by human monocyte-derived macrophages FEBS Lett. 225 1987 178 182 (Pubitemid 18021842)
    • (1987) FEBS Letters , vol.225 , Issue.1-2 , pp. 178-182
    • Gardette, J.1    Margelin, D.2    Maziere, J.C.3    Bertrand, J.4    Picard, J.5
  • 276
    • 0020702104 scopus 로고
    • 2 and its increase in variants deficient in adenylate cyclase and cyclic AMP-dependent protein kinase
    • R.N. Melmed, G. Friedman, T. Chajek-Shaul, O. Stein, and Y. Stein Lipoprotein lipase activity in cultured macrophage cell line J774(2) and its increase in variants deficient in adenylate cyclase and cyclic AMP-dependent protein kinase Biochim. Biophys. Acta 762 1983 58 66 (Pubitemid 13154062)
    • (1983) Biochimica et Biophysica Acta , vol.762 , Issue.1 , pp. 58-66
    • Melmed, R.N.1    Friedman, G.2    Chajek Shaul, T.3
  • 277
    • 0031892402 scopus 로고    scopus 로고
    • Stimulatory effect of glucose on macrophage lipoprotein lipase expression and production
    • DOI 10.2337/diabetes.47.3.431
    • M.R. Sartippour, A. Lambert, M. Laframboise, P. St-Jacques, and G. Renier Stimulatory effect of glucose on macrophage lipoprotein lipase expression and production Diabetes 47 1998 431 438 (Pubitemid 28104206)
    • (1998) Diabetes , vol.47 , Issue.3 , pp. 431-438
    • Sartippour, M.R.1    Lambert, A.2    Laframboise, M.3    St-Jacques, P.4    Renier, G.5
  • 278
    • 0024239899 scopus 로고
    • Insulin deficiency decreases lipoprotein lipase secretion by murine macrophages
    • S.R. Behr, and F.B. Kraemer Insulin deficiency decreases lipoprotein lipase secretion by murine macrophages Diabetes 37 1988 1076 1081 (Pubitemid 19033589)
    • (1988) Diabetes , vol.37 , Issue.8 , pp. 1076-1081
    • Behr, S.R.1    Kraemer, F.B.2
  • 279
    • 84881558068 scopus 로고    scopus 로고
    • Lipoprotein lipase in non-small cell lung cancer tissue is highly expressed in a subpopulation of tumor-associated macrophages
    • H. Podgornik, M. Sok, I. Kern, J. Marc, and D. Cerne Lipoprotein lipase in non-small cell lung cancer tissue is highly expressed in a subpopulation of tumor-associated macrophages Pathol. Res. Pract. 209 2013 516 520
    • (2013) Pathol. Res. Pract. , vol.209 , pp. 516-520
    • Podgornik, H.1    Sok, M.2    Kern, I.3    Marc, J.4    Cerne, D.5
  • 280
    • 70349133488 scopus 로고    scopus 로고
    • Increased lipoprotein lipase activity in non-small cell lung cancer tissue predicts shorter patient survival
    • Z. Trost, M. Sok, J. Marc, and D. Cerne Increased lipoprotein lipase activity in non-small cell lung cancer tissue predicts shorter patient survival Arch. Med. Res. 40 2009 364 368
    • (2009) Arch. Med. Res. , vol.40 , pp. 364-368
    • Trost, Z.1    Sok, M.2    Marc, J.3    Cerne, D.4
  • 283
    • 52449122798 scopus 로고    scopus 로고
    • Very-low-density lipoprotein-induced triglyceride accumulation in human mesangial cells is mainly mediated by lipoprotein lipase
    • J. Li, H. Li, Y.B. Wen, and X.W. Li Very-low-density lipoprotein-induced triglyceride accumulation in human mesangial cells is mainly mediated by lipoprotein lipase Nephron. Physiology 110 2008 1 10
    • (2008) Nephron. Physiology , vol.110 , pp. 1-10
    • Li, J.1    Li, H.2    Wen, Y.B.3    Li, X.W.4
  • 286
    • 0032936183 scopus 로고    scopus 로고
    • Insulin-induced up-regulation of lipoprotein lipase messenger ribonucleic acid and activity in mammary gland
    • P. Ramos, A. Martin-Hidalgo, and E. Herrera Insulin-induced up-regulation of lipoprotein lipase messenger ribonucleic acid and activity in mammary gland Endocrinology 140 1999 1089 1093 (Pubitemid 29104207)
    • (1999) Endocrinology , vol.140 , Issue.3 , pp. 1089-1093
    • Ramos, P.1    Martin-Hidalgo, A.2    Herrera, E.3
  • 287
    • 0028295385 scopus 로고
    • Regulation of lipoprotein lipase activity and mRNA in the mammary gland of the lactating mouse
    • D.R. Jensen, S. Gavigan, V. Sawicki, D.L. Witsell, R.H. Eckel, and M.C. Neville Regulation of lipoprotein lipase activity and mRNA in the mammary gland of the lactating mouse Biochem. J. 298 Pt 2 1994 321 327 (Pubitemid 24072472)
    • (1994) Biochemical Journal , vol.298 , Issue.2 , pp. 321-327
    • Jensen, D.R.1    Gavigan, S.2    Sawicki, V.3    Witsell, D.L.4    Eckel, R.H.5    Neville, M.C.6
  • 288
    • 0028608858 scopus 로고
    • Effect of starvation on lipoprotein lipase activity in different tissues during gestation in the rat
    • P. Lopez-Luna, J. Olea, and E. Herrera Effect of starvation on lipoprotein lipase activity in different tissues during gestation in the rat Biochim. Biophys. Acta 1215 1994 275 279
    • (1994) Biochim. Biophys. Acta , vol.1215 , pp. 275-279
    • Lopez-Luna, P.1    Olea, J.2    Herrera, E.3
  • 289
    • 0025003213 scopus 로고
    • A review of the hormone prolactin during lactation
    • K.M. Ostrom A review of the hormone prolactin during lactation Prog. Food Nutr. Sci. 14 1990 1 43
    • (1990) Prog. Food Nutr. Sci. , vol.14 , pp. 1-43
    • Ostrom, K.M.1
  • 290
    • 0031040421 scopus 로고    scopus 로고
    • Prolactin's effects on lipoprotein lipase (LPL) activity and on LPL mRNA levels in cultured mouse mammary gland explants
    • J. Hang, and J.A. Rillema Prolactin's effects on lipoprotein lipase (LPL) activity and on LPL mRNA levels in cultured mouse mammary gland explants Proc. Soc. Exp. Biol. Med. 214 1997 161 166
    • (1997) Proc. Soc. Exp. Biol. Med. , vol.214 , pp. 161-166
    • Hang, J.1    Rillema, J.A.2
  • 291
    • 0028355854 scopus 로고
    • 14C]triolein by insulin and prolactin: Evidence for bihormonal control of lipoprotein lipase activity
    • 14C]triolein by insulin and prolactin: evidence for bihormonal control of lipoprotein lipase activity Biochem. J. 300 Pt 1 1994 257 262 (Pubitemid 24151044)
    • (1994) Biochemical Journal , vol.300 , Issue.1 , pp. 257-262
    • Da Costa, T.H.M.1    Williamson, D.H.2
  • 292
    • 84890987858 scopus 로고    scopus 로고
    • What are lipoproteins doing in the brain?
    • H. Wang, and R.H. Eckel What are lipoproteins doing in the brain? Trends Endocrinol. Metab. 25 2014 8 14
    • (2014) Trends Endocrinol. Metab. , vol.25 , pp. 8-14
    • Wang, H.1    Eckel, R.H.2
  • 297
    • 13844297687 scopus 로고    scopus 로고
    • Beneficial effects of PPAR-γ ligands in ischemia-reperfusion injury, inflammation and shock
    • DOI 10.1016/j.cardiores.2004.12.008
    • M. Abdelrahman, A. Sivarajah, and C. Thiemermann Beneficial effects of PPAR-gamma ligands in ischemia - reperfusion injury, inflammation and shock Cardiovasc. Res. 65 2005 772 781 (Pubitemid 40249723)
    • (2005) Cardiovascular Research , vol.65 , Issue.4 , pp. 772-781
    • Abdelrahman, M.1    Sivarajah, A.2    Thiemermann, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.