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Volumn 7, Issue 11, 2012, Pages

The Activities of Lysyl Hydroxylase 3 (LH3) Regulate the Amount and Oligomerization Status of Adiponectin

Author keywords

[No Author keywords available]

Indexed keywords

ADIPONECTIN; CHOLESTEROL; FATTY ACID; GLUCOSE; HIGH DENSITY LIPOPROTEIN; INSULIN; LONG CHAIN ACYL COENZYME A DEHYDROGENASE; LOW DENSITY LIPOPROTEIN; LOW DENSITY LIPOPROTEIN CHOLESTEROL; LYSINE; LYSYL HYDROXYLASE 3; OLIGOMER; PROCOLLAGEN GLUCOSYLTRANSFERASE; PROCOLLAGEN LYSINE 2 OXOGLUTARATE 5 DIOXYGENASE; RECOMBINANT PROTEIN; TRIACYLGLYCEROL; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 84870545020     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0050045     Document Type: Article
Times cited : (17)

References (45)
  • 1
    • 0034680898 scopus 로고    scopus 로고
    • Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity
    • Heikkinen J, Risteli M, Wang C, Latvala J, Rossi M, et al. (2000) Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity. J Biol Chem 275 (46) (): 36158-36163.
    • (2000) J Biol Chem , vol.275 , Issue.46 , pp. 36158-36163
    • Heikkinen, J.1    Risteli, M.2    Wang, C.3    Latvala, J.4    Rossi, M.5
  • 2
    • 0036861267 scopus 로고    scopus 로고
    • The third activity for lysyl hydroxylase 3: Galactosylation of hydroxylysyl residues in collagens in vitro
    • Wang C, Luosujärvi H, Heikkinen J, Risteli M, Uitto L, et al. (2002) The third activity for lysyl hydroxylase 3: Galactosylation of hydroxylysyl residues in collagens in vitro. Matrix Biol 21 (7) (): 559-566.
    • (2002) Matrix Biol , vol.21 , Issue.7 , pp. 559-566
    • Wang, C.1    Luosujärvi, H.2    Heikkinen, J.3    Risteli, M.4    Uitto, L.5
  • 3
    • 34347382592 scopus 로고    scopus 로고
    • Expanding the lysyl hydroxylase toolbox: New insights into the localization and activities of lysyl hydroxylase 3 (LH3)
    • Myllylä R, Wang C, Heikkinen J, Juffer A, Lampela O, et al. (2007) Expanding the lysyl hydroxylase toolbox: New insights into the localization and activities of lysyl hydroxylase 3 (LH3). J Cell Physiol 212 (2) (): 323-329.
    • (2007) J Cell Physiol , vol.212 , Issue.2 , pp. 323-329
    • Myllylä, R.1    Wang, C.2    Heikkinen, J.3    Juffer, A.4    Lampela, O.5
  • 4
    • 0242710145 scopus 로고    scopus 로고
    • Collagens-structure, function, and biosynthesis
    • Gelse K, Pöschl E, Aigner T, (2003) Collagens-structure, function, and biosynthesis. Adv Drug Deliv Rev (55) pp. 1531.
    • (2003) Adv Drug Deliv Rev , Issue.55 , pp. 1531
    • Gelse, K.1    Pöschl, E.2    Aigner, T.3
  • 5
    • 33646384584 scopus 로고    scopus 로고
    • Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling
    • Salo AM, Wang C, Sipilä L, Sormunen R, Vapola M, et al. (2006) Lysyl hydroxylase 3 (LH3) modifies proteins in the extracellular space, a novel mechanism for matrix remodeling. J Cell Physiol 207 (3) (): 644-653.
    • (2006) J Cell Physiol , vol.207 , Issue.3 , pp. 644-653
    • Salo, A.M.1    Wang, C.2    Sipilä, L.3    Sormunen, R.4    Vapola, M.5
  • 6
    • 33750976345 scopus 로고    scopus 로고
    • The lysyl hydroxylase isoforms are widely expressed during mouse embryogenesis, but obtain tissue- and cell-specific patterns in the adult
    • Salo AM, Sipilä L, Sormunen R, Ruotsalainen H, Vainio S, et al. (2006) The lysyl hydroxylase isoforms are widely expressed during mouse embryogenesis, but obtain tissue- and cell-specific patterns in the adult. Matrix Biol 25 (8) (): 475-483.
    • (2006) Matrix Biol , vol.25 , Issue.8 , pp. 475-483
    • Salo, A.M.1    Sipilä, L.2    Sormunen, R.3    Ruotsalainen, H.4    Vainio, S.5
  • 7
    • 63049133431 scopus 로고    scopus 로고
    • The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability
    • Wang C, Kovanen V, Raudasoja P, Eskelinen S, Pospiech H, et al. (2009) The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability. J Cell Mol Med 13 (3) (): 508-521.
    • (2009) J Cell Mol Med , vol.13 , Issue.3 , pp. 508-521
    • Wang, C.1    Kovanen, V.2    Raudasoja, P.3    Eskelinen, S.4    Pospiech, H.5
  • 8
    • 33645049315 scopus 로고    scopus 로고
    • Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes
    • Ruotsalainen H, Sipilä L, Vapola M, Sormunen R, Salo AM, et al. (2006) Glycosylation catalyzed by lysyl hydroxylase 3 is essential for basement membranes. J Cell Sci 119 (Pt 4) (): 625-635.
    • (2006) J Cell Sci , vol.119 , Issue.Pt 4 , pp. 625-635
    • Ruotsalainen, H.1    Sipilä, L.2    Vapola, M.3    Sormunen, R.4    Salo, A.M.5
  • 9
    • 36349032945 scopus 로고    scopus 로고
    • Secretion and assembly of type IV and VI collagens depend on glycosylation of hydroxylysines
    • Sipilä L, Ruotsalainen H, Sormunen R, Baker NL, Lamande SR, et al. (2007) Secretion and assembly of type IV and VI collagens depend on glycosylation of hydroxylysines. J Biol Chem 282 (46) (): 33381-33388.
    • (2007) J Biol Chem , vol.282 , Issue.46 , pp. 33381-33388
    • Sipilä, L.1    Ruotsalainen, H.2    Sormunen, R.3    Baker, N.L.4    Lamande, S.R.5
  • 10
    • 53049110420 scopus 로고    scopus 로고
    • A connective tissue disorder caused by mutations of the lysyl hydroxylase 3 gene
    • Salo AM, Cox H, Farndon P, Moss C, Grindulis H, et al. (2008) A connective tissue disorder caused by mutations of the lysyl hydroxylase 3 gene. Am J Hum Genet 83 (4) (): 495-503.
    • (2008) Am J Hum Genet , vol.83 , Issue.4 , pp. 495-503
    • Salo, A.M.1    Cox, H.2    Farndon, P.3    Moss, C.4    Grindulis, H.5
  • 11
    • 70350502101 scopus 로고    scopus 로고
    • Reduction of lysyl hydroxylase 3 causes deleterious changes in the deposition and organization of extracellular matrix
    • Risteli M, Ruotsalainen H, Salo AM, Sormunen R, Sipilä L, et al. (2009) Reduction of lysyl hydroxylase 3 causes deleterious changes in the deposition and organization of extracellular matrix. J Biol Chem 284 (41) (): 28204-28211.
    • (2009) J Biol Chem , vol.284 , Issue.41 , pp. 28204-28211
    • Risteli, M.1    Ruotsalainen, H.2    Salo, A.M.3    Sormunen, R.4    Sipilä, L.5
  • 12
    • 33748992313 scopus 로고    scopus 로고
    • Adipocytokines: Mediators linking adipose tissue, inflammation and immunity
    • Tilg H, Moschen AR, (2006) Adipocytokines: Mediators linking adipose tissue, inflammation and immunity. Nat Rev Immunol 6 (10) (): 772-783.
    • (2006) Nat Rev Immunol , vol.6 , Issue.10 , pp. 772-783
    • Tilg, H.1    Moschen, A.R.2
  • 13
    • 65649131589 scopus 로고    scopus 로고
    • Serum adiponectin as a useful marker for metabolic syndrome in type 2 diabetic patients
    • Yun JE, Sull JW, Lee HY, Park E, Kim S, et al. (2009) Serum adiponectin as a useful marker for metabolic syndrome in type 2 diabetic patients. Diabetes Metab Res Rev 25 (3) (): 259-265.
    • (2009) Diabetes Metab Res Rev , vol.25 , Issue.3 , pp. 259-265
    • Yun, J.E.1    Sull, J.W.2    Lee, H.Y.3    Park, E.4    Kim, S.5
  • 14
    • 77953230769 scopus 로고    scopus 로고
    • Genetic and environmental determinants of total and high-molecular weight adiponectin in families with low HDL-cholesterol and early onset coronary heart disease
    • Kangas-Kontio T, Huotari A, Ruotsalainen H, Herzig KH, Tamminen M, et al. (2010) Genetic and environmental determinants of total and high-molecular weight adiponectin in families with low HDL-cholesterol and early onset coronary heart disease. Atherosclerosis 210 (2) (): 479-485.
    • (2010) Atherosclerosis , vol.210 , Issue.2 , pp. 479-485
    • Kangas-Kontio, T.1    Huotari, A.2    Ruotsalainen, H.3    Herzig, K.H.4    Tamminen, M.5
  • 16
    • 38949125405 scopus 로고    scopus 로고
    • Post-translational modifications of adiponectin: Mechanisms and functional implications
    • Wang Y, Lam KS, Yau MH, Xu A, (2008) Post-translational modifications of adiponectin: Mechanisms and functional implications. Biochem J 409 (3) (): 623-633.
    • (2008) Biochem J , vol.409 , Issue.3 , pp. 623-633
    • Wang, Y.1    Lam, K.S.2    Yau, M.H.3    Xu, A.4
  • 17
    • 0037205414 scopus 로고    scopus 로고
    • Hydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin. potential role in the modulation of its insulin-sensitizing activity
    • Wang Y, Xu A, Knight C, Xu LY, Cooper GJ, (2002) Hydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin. potential role in the modulation of its insulin-sensitizing activity. J Biol Chem 277 (22) (): 19521-19529.
    • (2002) J Biol Chem , vol.277 , Issue.22 , pp. 19521-19529
    • Wang, Y.1    Xu, A.2    Knight, C.3    Xu, L.Y.4    Cooper, G.J.5
  • 18
    • 33745664785 scopus 로고    scopus 로고
    • Adiponectin multimerization is dependent on conserved lysines in the collagenous domain: Evidence for regulation of multimerization by alterations in posttranslational modifications
    • Richards AA, Stephens T, Charlton HK, Jones A, Macdonald GA, et al. (2006) Adiponectin multimerization is dependent on conserved lysines in the collagenous domain: Evidence for regulation of multimerization by alterations in posttranslational modifications. Mol Endocrinol 20 (7) (): 1673-1687.
    • (2006) Mol Endocrinol , vol.20 , Issue.7 , pp. 1673-1687
    • Richards, A.A.1    Stephens, T.2    Charlton, H.K.3    Jones, A.4    Macdonald, G.A.5
  • 19
    • 33745222085 scopus 로고    scopus 로고
    • Post-translational modifications of the four conserved lysine residues within the collagenous domain of adiponectin are required for the formation of its high molecular weight oligomeric complex
    • Wang Y, Lam KS, Chan L, Chan KW, Lam JB, et al. (2006) Post-translational modifications of the four conserved lysine residues within the collagenous domain of adiponectin are required for the formation of its high molecular weight oligomeric complex. J Biol Chem 281 (24) (): 16391-16400.
    • (2006) J Biol Chem , vol.281 , Issue.24 , pp. 16391-16400
    • Wang, Y.1    Lam, K.S.2    Chan, L.3    Chan, K.W.4    Lam, J.B.5
  • 20
    • 0141924849 scopus 로고    scopus 로고
    • Impaired multimerization of human adiponectin mutants associated with diabetes. molecular structure and multimer formation of adiponectin
    • Waki H, Yamauchi T, Kamon J, Ito Y, Uchida S, et al. (2003) Impaired multimerization of human adiponectin mutants associated with diabetes. molecular structure and multimer formation of adiponectin. J Biol Chem 278 (41) (): 40352-40363.
    • (2003) J Biol Chem , vol.278 , Issue.41 , pp. 40352-40363
    • Waki, H.1    Yamauchi, T.2    Kamon, J.3    Ito, Y.4    Uchida, S.5
  • 21
    • 11144355637 scopus 로고    scopus 로고
    • Complex distribution, not absolute amount of adiponectin, correlates with thiazolidinedione-mediated improvement in insulin sensitivity
    • Pajvani UB, Hawkins M, Combs TP, Rajala MW, Doebber T, et al. (2004) Complex distribution, not absolute amount of adiponectin, correlates with thiazolidinedione-mediated improvement in insulin sensitivity. J Biol Chem 279 (13) (): 12152-12162.
    • (2004) J Biol Chem , vol.279 , Issue.13 , pp. 12152-12162
    • Pajvani, U.B.1    Hawkins, M.2    Combs, T.P.3    Rajala, M.W.4    Doebber, T.5
  • 22
    • 42449113834 scopus 로고    scopus 로고
    • Plasma adiponectin complexes have distinct biochemical characteristics
    • Schraw T, Wang ZV, Halberg N, Hawkins M, Scherer PE, (2008) Plasma adiponectin complexes have distinct biochemical characteristics. Endocrinology 149 (5) (): 2270-2282.
    • (2008) Endocrinology , vol.149 , Issue.5 , pp. 2270-2282
    • Schraw, T.1    Wang, Z.V.2    Halberg, N.3    Hawkins, M.4    Scherer, P.E.5
  • 24
    • 24044479055 scopus 로고    scopus 로고
    • Testosterone selectively reduces the high molecular weight form of adiponectin by inhibiting its secretion from adipocytes
    • Xu A, Chan KW, Hoo RL, Wang Y, Tan KC, et al. (2005) Testosterone selectively reduces the high molecular weight form of adiponectin by inhibiting its secretion from adipocytes. J Biol Chem 280 (18) (): 18073-18080.
    • (2005) J Biol Chem , vol.280 , Issue.18 , pp. 18073-18080
    • Xu, A.1    Chan, K.W.2    Hoo, R.L.3    Wang, Y.4    Tan, K.C.5
  • 25
    • 68249131913 scopus 로고    scopus 로고
    • Mitochondrial 2,4-dienoyl-CoA reductase deficiency in mice results in severe hypoglycemia with stress intolerance and unimpaired ketogenesis
    • Miinalainen IJ, Schmitz W, Huotari A, Autio KJ, Soininen R, et al. (2009) Mitochondrial 2,4-dienoyl-CoA reductase deficiency in mice results in severe hypoglycemia with stress intolerance and unimpaired ketogenesis. PLoS Genet 5 (7) (): e1000543.
    • (2009) PLoS Genet , vol.5 , Issue.7
    • Miinalainen, I.J.1    Schmitz, W.2    Huotari, A.3    Autio, K.J.4    Soininen, R.5
  • 26
    • 0019885893 scopus 로고
    • Specificity of trypsin and carboxypeptidase B for hydroxylysine residues in denatured collagens
    • Wu GY, Pereyra B, Seifter S, (1981) Specificity of trypsin and carboxypeptidase B for hydroxylysine residues in denatured collagens. Biochemistry 20 (15) (): 4321-4324.
    • (1981) Biochemistry , vol.20 , Issue.15 , pp. 4321-4324
    • Wu, G.Y.1    Pereyra, B.2    Seifter, S.3
  • 27
    • 0037317488 scopus 로고    scopus 로고
    • Sexual differentiation, pregnancy, calorie restriction, and aging affect the adipocyte-specific secretory protein adiponectin
    • Combs TP, Berg AH, Rajala MW, Klebanov S, Iyengar P, et al. (2003) Sexual differentiation, pregnancy, calorie restriction, and aging affect the adipocyte-specific secretory protein adiponectin. Diabetes 52 (2) (): 268-276.
    • (2003) Diabetes , vol.52 , Issue.2 , pp. 268-276
    • Combs, T.P.1    Berg, A.H.2    Rajala, M.W.3    Klebanov, S.4    Iyengar, P.5
  • 28
    • 0036724336 scopus 로고    scopus 로고
    • Androgens decrease plasma adiponectin, an insulin-sensitizing adipocyte-derived protein
    • Nishizawa H, Shimomura I, Kishida K, Maeda N, Kuriyama H, et al. (2002) Androgens decrease plasma adiponectin, an insulin-sensitizing adipocyte-derived protein. Diabetes 51 (9) (): 2734-2741.
    • (2002) Diabetes , vol.51 , Issue.9 , pp. 2734-2741
    • Nishizawa, H.1    Shimomura, I.2    Kishida, K.3    Maeda, N.4    Kuriyama, H.5
  • 29
    • 70350162530 scopus 로고    scopus 로고
    • The influence of sex, body composition, and nonesterified fatty acids on serum adipokine concentrations
    • Plaisance EP, Grandjean PW, Judd RL, Jones KW, Taylor JK, (2009) The influence of sex, body composition, and nonesterified fatty acids on serum adipokine concentrations. Metabolism 58 (11) (): 1557-1563.
    • (2009) Metabolism , vol.58 , Issue.11 , pp. 1557-1563
    • Plaisance, E.P.1    Grandjean, P.W.2    Judd, R.L.3    Jones, K.W.4    Taylor, J.K.5
  • 30
    • 0028787490 scopus 로고
    • A novel serum protein similar to C1q, produced exclusively in adipocytes
    • Scherer PE, Williams S, Fogliano M, Baldini G, Lodish HF, (1995) A novel serum protein similar to C1q, produced exclusively in adipocytes. J Biol Chem 270 (45) (): 26746-26749.
    • (1995) J Biol Chem , vol.270 , Issue.45 , pp. 26746-26749
    • Scherer, P.E.1    Williams, S.2    Fogliano, M.3    Baldini, G.4    Lodish, H.F.5
  • 31
    • 34248350766 scopus 로고    scopus 로고
    • Adiponectin and the metabolic syndrome: Mechanisms mediating risk for metabolic and cardiovascular disease
    • Lara-Castro C, Fu Y, Chung BH, Garvey WT, (2007) Adiponectin and the metabolic syndrome: Mechanisms mediating risk for metabolic and cardiovascular disease. Curr Opin Lipidol 18 (3) (): 263-270.
    • (2007) Curr Opin Lipidol , vol.18 , Issue.3 , pp. 263-270
    • Lara-Castro, C.1    Fu, Y.2    Chung, B.H.3    Garvey, W.T.4
  • 32
    • 0036063777 scopus 로고    scopus 로고
    • Diet-induced insulin resistance in mice lacking adiponectin/ACRP30
    • Maeda N, Shimomura I, Kishida K, Nishizawa H, Matsuda M, et al. (2002) Diet-induced insulin resistance in mice lacking adiponectin/ACRP30. Nat Med 8 (7) (): 731-737.
    • (2002) Nat Med , vol.8 , Issue.7 , pp. 731-737
    • Maeda, N.1    Shimomura, I.2    Kishida, K.3    Nishizawa, H.4    Matsuda, M.5
  • 33
    • 33646346627 scopus 로고    scopus 로고
    • Mice lacking adiponectin show decreased hepatic insulin sensitivity and reduced responsiveness to peroxisome proliferator-activated receptor gamma agonists
    • Nawrocki AR, Rajala MW, Tomas E, Pajvani UB, Saha AK, et al. (2006) Mice lacking adiponectin show decreased hepatic insulin sensitivity and reduced responsiveness to peroxisome proliferator-activated receptor gamma agonists. J Biol Chem 281 (5) (): 2654-2660.
    • (2006) J Biol Chem , vol.281 , Issue.5 , pp. 2654-2660
    • Nawrocki, A.R.1    Rajala, M.W.2    Tomas, E.3    Pajvani, U.B.4    Saha, A.K.5
  • 34
    • 72449141637 scopus 로고    scopus 로고
    • Transcriptional and post-translational regulation of adiponectin
    • Liu M, Liu F, (2010) Transcriptional and post-translational regulation of adiponectin. Biochem J 425 (1) (): 41-52.
    • (2010) Biochem J , vol.425 , Issue.1 , pp. 41-52
    • Liu, M.1    Liu, F.2
  • 35
    • 79953225159 scopus 로고    scopus 로고
    • Lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture
    • Sricholpech M, Perdivara I, Nagaoka H, Yokoyama M, Tomer KB, et al. (2011) Lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture. J Biol Chem 286 (11) (): 8846-8856.
    • (2011) J Biol Chem , vol.286 , Issue.11 , pp. 8846-8856
    • Sricholpech, M.1    Perdivara, I.2    Nagaoka, H.3    Yokoyama, M.4    Tomer, K.B.5
  • 36
    • 4444245754 scopus 로고    scopus 로고
    • Characterization of collagenous peptides bound to lysyl hydroxylase isoforms
    • Risteli M, Niemitalo O, Lankinen H, Juffer AH, Myllyla R, (2004) Characterization of collagenous peptides bound to lysyl hydroxylase isoforms. J Biol Chem 279 (36) (): 37535-37543.
    • (2004) J Biol Chem , vol.279 , Issue.36 , pp. 37535-37543
    • Risteli, M.1    Niemitalo, O.2    Lankinen, H.3    Juffer, A.H.4    Myllyla, R.5
  • 37
    • 59449103217 scopus 로고    scopus 로고
    • Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases
    • Schegg B, Hulsmeier AJ, Rutschmann C, Maag C, Hennet T, (2009) Core glycosylation of collagen is initiated by two beta(1-O)galactosyltransferases. Mol Cell Biol 29 (4) (): 943-952.
    • (2009) Mol Cell Biol , vol.29 , Issue.4 , pp. 943-952
    • Schegg, B.1    Hulsmeier, A.J.2    Rutschmann, C.3    Maag, C.4    Hennet, T.5
  • 38
    • 0035218501 scopus 로고    scopus 로고
    • The fibril structure of type V collagen triple-helical domain
    • Mizuno K, Adachi E, Imamura Y, Katsumata O, Hayashi T, (2001) The fibril structure of type V collagen triple-helical domain. Micron 32 (3) (): 317-323.
    • (2001) Micron , vol.32 , Issue.3 , pp. 317-323
    • Mizuno, K.1    Adachi, E.2    Imamura, Y.3    Katsumata, O.4    Hayashi, T.5
  • 39
    • 33745834319 scopus 로고    scopus 로고
    • Adiponectin and adiponectin receptors in insulin resistance, diabetes, and the metabolic syndrome
    • Kadowaki T, Yamauchi T, Kubota N, Hara K, Ueki K, et al. (2006) Adiponectin and adiponectin receptors in insulin resistance, diabetes, and the metabolic syndrome. J Clin Invest 116 (7) (): 1784-1792.
    • (2006) J Clin Invest , vol.116 , Issue.7 , pp. 1784-1792
    • Kadowaki, T.1    Yamauchi, T.2    Kubota, N.3    Hara, K.4    Ueki, K.5
  • 40
    • 44949237971 scopus 로고    scopus 로고
    • Adiponectin and its association with insulin resistance and type 2 diabetes
    • Sheng T, Yang K, (2008) Adiponectin and its association with insulin resistance and type 2 diabetes. J Genet Genomics 35 (6) (): 321-326.
    • (2008) J Genet Genomics , vol.35 , Issue.6 , pp. 321-326
    • Sheng, T.1    Yang, K.2
  • 41
    • 0037135523 scopus 로고    scopus 로고
    • Disruption of adiponectin causes insulin resistance and neointimal formation
    • Kubota N, Terauchi Y, Yamauchi T, Kubota T, Moroi M, et al. (2002) Disruption of adiponectin causes insulin resistance and neointimal formation. J Biol Chem 277 (29) (): 25863-25866.
    • (2002) J Biol Chem , vol.277 , Issue.29 , pp. 25863-25866
    • Kubota, N.1    Terauchi, Y.2    Yamauchi, T.3    Kubota, T.4    Moroi, M.5
  • 42
    • 48249117609 scopus 로고    scopus 로고
    • Adiponectin reduces plasma triglyceride by increasing VLDL triglyceride catabolism
    • Qiao L, Zou C, van der Westhuyzen DR, Shao J, (2008) Adiponectin reduces plasma triglyceride by increasing VLDL triglyceride catabolism. Diabetes 57 (7) (): 1824-1833.
    • (2008) Diabetes , vol.57 , Issue.7 , pp. 1824-1833
    • Qiao, L.1    Zou, C.2    van der Westhuyzen, D.R.3    Shao, J.4
  • 43
    • 58249117645 scopus 로고    scopus 로고
    • Identification and characterization of CTRP9, a novel secreted glycoprotein, from adipose tissue that reduces serum glucose in mice and forms heterotrimers with adiponectin
    • Wong GW, Krawczyk SA, Kitidis-Mitrokostas C, Ge G, Spooner E, et al. (2009) Identification and characterization of CTRP9, a novel secreted glycoprotein, from adipose tissue that reduces serum glucose in mice and forms heterotrimers with adiponectin. FASEB J 23 (1) (): 241-258.
    • (2009) FASEB J , vol.23 , Issue.1 , pp. 241-258
    • Wong, G.W.1    Krawczyk, S.A.2    Kitidis-Mitrokostas, C.3    Ge, G.4    Spooner, E.5
  • 44
    • 3142668924 scopus 로고    scopus 로고
    • A family of Acrp30/adiponectin structural and functional paralogs
    • Wong GW, Wang J, Hug C, Tsao TS, Lodish HF, (2004) A family of Acrp30/adiponectin structural and functional paralogs. Proc Natl Acad Sci U S A 101 (28) (): 10302-10307.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.28 , pp. 10302-10307
    • Wong, G.W.1    Wang, J.2    Hug, C.3    Tsao, T.S.4    Lodish, H.F.5
  • 45
    • 58149315989 scopus 로고    scopus 로고
    • Molecular, biochemical and functional characterizations of C1q/TNF family members: Adipose-tissue-selective expression patterns, regulation by PPAR-gamma agonist, cysteine-mediated oligomerizations, combinatorial associations and metabolic functions
    • Wong GW, Krawczyk SA, Kitidis-Mitrokostas C, Revett T, Gimeno R, et al. (2008) Molecular, biochemical and functional characterizations of C1q/TNF family members: Adipose-tissue-selective expression patterns, regulation by PPAR-gamma agonist, cysteine-mediated oligomerizations, combinatorial associations and metabolic functions. Biochem J 416 (2) (): 161-177.
    • (2008) Biochem J , vol.416 , Issue.2 , pp. 161-177
    • Wong, G.W.1    Krawczyk, S.A.2    Kitidis-Mitrokostas, C.3    Revett, T.4    Gimeno, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.