메뉴 건너뛰기




Volumn 290, Issue 48, 2015, Pages 28822-28833

Dysregulation of plasmalogen homeostasis impairs cholesterol biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; PHOSPHOLIPIDS; PHYSIOLOGY; SYNTHESIS (CHEMICAL);

EID: 84948469149     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.656983     Document Type: Article
Times cited : (51)

References (75)
  • 2
    • 84864046701 scopus 로고    scopus 로고
    • Functions of plasmalogen lipids in health and disease
    • Braverman, N. E., and Moser, A. B. (2012) Functions of plasmalogen lipids in health and disease. Biochim. Biophys. Acta 1822, 1442-1452
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 1442-1452
    • Braverman, N.E.1    Moser, A.B.2
  • 3
    • 0037244159 scopus 로고    scopus 로고
    • Deficiency in ethanolamine plasmalogen leads to altered cholesterol transport
    • Munn, N. J., Arnio, E., Liu, D., Zoeller, R. A., and Liscum, L. (2003) Deficiency in ethanolamine plasmalogen leads to altered cholesterol transport. J. Lipid Res. 44, 182-192
    • (2003) J. Lipid Res. , vol.44 , pp. 182-192
    • Munn, N.J.1    Arnio, E.2    Liu, D.3    Zoeller, R.A.4    Liscum, L.5
  • 4
    • 65549163117 scopus 로고    scopus 로고
    • Defects in myelination, paranode organization and Purkinje cell innervation in the ether lipid-deficient mouse cerebellum
    • Teigler, A., Komljenovic, D., Draguhn, A., Gorgas, K., and Just, W. W. (2009) Defects in myelination, paranode organization and Purkinje cell innervation in the ether lipid-deficient mouse cerebellum. Hum. Mol. Genet. 18, 1897-1908
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 1897-1908
    • Teigler, A.1    Komljenovic, D.2    Draguhn, A.3    Gorgas, K.4    Just, W.W.5
  • 5
    • 4444258170 scopus 로고    scopus 로고
    • Mammalian wax biosynthesis. I. Identification of two fatty acyl-coenzyme a reductases with different substrate specificities and tissue distributions
    • Cheng, J. B., and Russell, D. W. (2004) Mammalian wax biosynthesis. I. identification of two fatty acyl-coenzyme a reductases with different substrate specificities and tissue distributions. J. Biol. Chem. 279, 37789-37797
    • (2004) J. Biol. Chem. , vol.279 , pp. 37789-37797
    • Cheng, J.B.1    Russell, D.W.2
  • 6
    • 77950551803 scopus 로고    scopus 로고
    • Posttranslational regulation of fatty acyl-CoA reductase 1, Far1, controls ether glycerophospholipid synthesis
    • Honsho, M., Asaoku, S., and Fujiki, Y. (2010) Posttranslational regulation of fatty acyl-CoA reductase 1, Far1, controls ether glycerophospholipid synthesis. J. Biol. Chem. 285, 8537-8542
    • (2010) J. Biol. Chem. , vol.285 , pp. 8537-8542
    • Honsho, M.1    Asaoku, S.2    Fujiki, Y.3
  • 7
    • 84889072644 scopus 로고    scopus 로고
    • Topogenesis and homeostasis of fatty acyl-CoA reductase 1
    • Honsho, M., Asaoku, S., Fukumoto, K., and Fujiki, Y. (2013) Topogenesis and homeostasis of fatty acyl-CoA reductase 1. J. Biol. Chem. 288, 34588-34598
    • (2013) J. Biol. Chem. , vol.288 , pp. 34588-34598
    • Honsho, M.1    Asaoku, S.2    Fukumoto, K.3    Fujiki, Y.4
  • 9
    • 79961118496 scopus 로고    scopus 로고
    • Regulation ofHMG-CoAreductase in mammals and yeast
    • Burg, J. S., and Espenshade, P. J. (2011) Regulation ofHMG-CoAreductase in mammals and yeast. Prog. Lipid Res. 50, 403-410
    • (2011) Prog. Lipid Res. , vol.50 , pp. 403-410
    • Burg, J.S.1    Espenshade, P.J.2
  • 10
    • 0025651856 scopus 로고
    • Regulation of squalene epoxidase in HepG2 cells
    • Hidaka, Y., Satoh, T., and Kamei, T. (1990) Regulation of squalene epoxidase in HepG2 cells. J. Lipid Res. 31, 2087-2094
    • (1990) J. Lipid Res. , vol.31 , pp. 2087-2094
    • Hidaka, Y.1    Satoh, T.2    Kamei, T.3
  • 11
    • 0018670881 scopus 로고
    • Two major regulatory steps in cholesterol synthesis by human renal cancer cells
    • Gonzalez, R., Carlson, J. P., and Dempsey, M. E. (1979) Two major regulatory steps in cholesterol synthesis by human renal cancer cells. Arch. Biochem. Biophys. 196, 574-580
    • (1979) Arch. Biochem. Biophys. , vol.196 , pp. 574-580
    • Gonzalez, R.1    Carlson, J.P.2    Dempsey, M.E.3
  • 12
    • 79952174597 scopus 로고    scopus 로고
    • Cholesterol-dependent degradation of squalene monooxygenase, a control point in cholesterol synthesis beyond HMG-CoA reductase
    • Gill, S., Stevenson, J., Kristiana, I., and Brown, A. J. (2011) Cholesterol-dependent degradation of squalene monooxygenase, a control point in cholesterol synthesis beyond HMG-CoA reductase. Cell Metab. 13, 260-273
    • (2011) Cell Metab. , vol.13 , pp. 260-273
    • Gill, S.1    Stevenson, J.2    Kristiana, I.3    Brown, A.J.4
  • 13
    • 50849121067 scopus 로고    scopus 로고
    • Isolation and characterization of mutant animal cell line defective in alkyl-dihydroxyacetonephosphate synthase: Localization and transport of plasmalogens to post-Golgi compartments
    • Honsho, M., Yagita, Y., Kinoshita, N., and Fujiki, Y. (2008) Isolation and characterization of mutant animal cell line defective in alkyl-dihydroxyacetonephosphate synthase: Localization and transport of plasmalogens to post-Golgi compartments. Biochim. Biophys. Acta 1783, 1857-1865
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1857-1865
    • Honsho, M.1    Yagita, Y.2    Kinoshita, N.3    Fujiki, Y.4
  • 14
    • 0031586033 scopus 로고    scopus 로고
    • Isolation and characterization of peroxisome-deficient Chinese hamster ovary cell mutants representing human complementation group III
    • Okumoto, K., Bogaki, A., Tateishi, K., Tsukamoto, T., Osumi, T., Shimozawa, N., Suzuki, Y., Orii, T., and Fujiki, Y. (1997) Isolation and characterization of peroxisome-deficient Chinese hamster ovary cell mutants representing human complementation group III. Exp. Cell Res. 233, 11-20
    • (1997) Exp. Cell Res. , vol.233 , pp. 11-20
    • Okumoto, K.1    Bogaki, A.2    Tateishi, K.3    Tsukamoto, T.4    Osumi, T.5    Shimozawa, N.6    Suzuki, Y.7    Orii, T.8    Fujiki, Y.9
  • 15
    • 0028812541 scopus 로고
    • Alteration of the myometrial plasma membrane cholesterol content with -cyclodextrin modulates the binding affinity of the oxytocin receptor
    • Klein, U., Gimpl, G., and Fahrenholz, F. (1995) Alteration of the myometrial plasma membrane cholesterol content with -cyclodextrin modulates the binding affinity of the oxytocin receptor. Biochemistry 34, 13784-13793
    • (1995) Biochemistry , vol.34 , pp. 13784-13793
    • Klein, U.1    Gimpl, G.2    Fahrenholz, F.3
  • 16
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G., and Dyer, W. J. (1959) A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37, 911-917
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 17
    • 84896899993 scopus 로고    scopus 로고
    • Very-long-chain polyunsaturated fatty acids accumulate in phosphatidylcholine of fibroblasts from patients with Zellweger syndrome and acyl-CoA oxidase1 deficiency
    • Abe, Y., Honsho, M., Nakanishi, H., Taguchi, R., and Fujiki, Y. (2014) Very-long-chain polyunsaturated fatty acids accumulate in phosphatidylcholine of fibroblasts from patients with Zellweger syndrome and acyl-CoA oxidase1 deficiency. Biochim. Biophys. Acta 1841, 610-619
    • (2014) Biochim. Biophys. Acta , vol.1841 , pp. 610-619
    • Abe, Y.1    Honsho, M.2    Nakanishi, H.3    Taguchi, R.4    Fujiki, Y.5
  • 18
  • 19
    • 0033804750 scopus 로고    scopus 로고
    • PEX3 is the causal gene responsible for peroxisome membrane assembly defective Zellweger syndrome of complementation group G
    • Ghaedi, K., Honsho, M., Shimozawa, N., Suzuki, Y., Kondo, N., and Fujiki, Y. (2000) PEX3 is the causal gene responsible for peroxisome membrane assembly defective Zellweger syndrome of complementation group G. Am. J. Hum. Genet. 67, 976-981
    • (2000) Am. J. Hum. Genet. , vol.67 , pp. 976-981
    • Ghaedi, K.1    Honsho, M.2    Shimozawa, N.3    Suzuki, Y.4    Kondo, N.5    Fujiki, Y.6
  • 20
    • 28544451220 scopus 로고    scopus 로고
    • Shuttling mechanism of peroxisome targeting signal type 1 receptor Pex5: ATP-independent import and ATP-dependent export
    • Miyata, N., and Fujiki, Y. (2005) Shuttling mechanism of peroxisome targeting signal type 1 receptor Pex5: ATP-independent import and ATP-dependent export. Mol. Cell. Biol. 25, 10822-10832
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10822-10832
    • Miyata, N.1    Fujiki, Y.2
  • 21
    • 0032471611 scopus 로고    scopus 로고
    • Mutation in PEX16 is causal in the peroxisome-deficient Zellweger syndrome of complementation group D
    • Honsho, M., Tamura, S., Shimozawa, N., Suzuki, Y., Kondo, N., and Fujiki, Y. (1998) Mutation in PEX16 is causal in the peroxisome-deficient Zellweger syndrome of complementation group D. Am. J. Hum. Genet. 63, 1622-1630
    • (1998) Am. J. Hum. Genet. , vol.63 , pp. 1622-1630
    • Honsho, M.1    Tamura, S.2    Shimozawa, N.3    Suzuki, Y.4    Kondo, N.5    Fujiki, Y.6
  • 22
    • 0031656796 scopus 로고    scopus 로고
    • Mutation in PEX10 is the cause of Zellweger peroxisome deficiency syndrome of complementation group B
    • Okumoto, K., Itoh, R., Shimozawa, N., Suzuki, Y., Tamura, S., Kondo, N., and Fujiki, Y. (1998) Mutation in PEX10 is the cause of Zellweger peroxisome deficiency syndrome of complementation group B. Hum. Mol. Genet. 7, 1399-1405
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1399-1405
    • Okumoto, K.1    Itoh, R.2    Shimozawa, N.3    Suzuki, Y.4    Tamura, S.5    Kondo, N.6    Fujiki, Y.7
  • 23
    • 33845748205 scopus 로고    scopus 로고
    • SREBP-2 positively regulates transcription of the cholesterol efflux gene, ABCA1, by generating oxysterol ligands for LXR
    • Wong, J., Quinn, C. M., and Brown, A. J. (2006) SREBP-2 positively regulates transcription of the cholesterol efflux gene, ABCA1, by generating oxysterol ligands for LXR. Biochem. J. 400, 485-491
    • (2006) Biochem. J. , vol.400 , pp. 485-491
    • Wong, J.1    Quinn, C.M.2    Brown, A.J.3
  • 24
    • 80053083941 scopus 로고    scopus 로고
    • The mammalian target of rapamycin regulates cholesterol biosynthetic gene expression and exhibits a rapamycin-resistant transcriptional profile
    • Wang, B. T., Ducker, G. S., Barczak, A. J., Barbeau, R., Erle, D. J., and Shokat, K. M. (2011) The mammalian target of rapamycin regulates cholesterol biosynthetic gene expression and exhibits a rapamycin-resistant transcriptional profile. Proc. Natl. Acad. Sci. U.S.A. 108, 15201-15206
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 15201-15206
    • Wang, B.T.1    Ducker, G.S.2    Barczak, A.J.3    Barbeau, R.4    Erle, D.J.5    Shokat, K.M.6
  • 25
    • 33744732467 scopus 로고    scopus 로고
    • Involvement of Akt in ER-to-Golgi transport of SCAP/SREBP: A link between a key cell proliferative pathway and membrane synthesis
    • Du, X., Kristiana, I., Wong, J., and Brown, A. J. (2006) Involvement of Akt in ER-to-Golgi transport of SCAP/SREBP: a link between a key cell proliferative pathway and membrane synthesis. Mol. Biol. Cell 17, 2735-2745
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2735-2745
    • Du, X.1    Kristiana, I.2    Wong, J.3    Brown, A.J.4
  • 27
    • 0026731811 scopus 로고
    • Rab GTP-binding proteins with three different carboxyl-terminal cysteine motifs are modified in vivo by 20-carbon isoprenoids
    • Kinsella, B. T., and Maltese, W. A. (1992) rab GTP-binding proteins with three different carboxyl-terminal cysteine motifs are modified in vivo by 20-carbon isoprenoids. J. Biol. Chem. 267, 3940-3945
    • (1992) J. Biol. Chem. , vol.267 , pp. 3940-3945
    • Kinsella, B.T.1    Maltese, W.A.2
  • 28
    • 34848835187 scopus 로고    scopus 로고
    • Statins reduce amyloid- production through inhibition of protein isoprenylation
    • Ostrowski, S. M., Wilkinson, B. L., Golde, T. E., and Landreth, G. (2007) Statins reduce amyloid- production through inhibition of protein isoprenylation. J. Biol. Chem. 282, 26832-26844
    • (2007) J. Biol. Chem. , vol.282 , pp. 26832-26844
    • Ostrowski, S.M.1    Wilkinson, B.L.2    Golde, T.E.3    Landreth, G.4
  • 29
    • 53149118574 scopus 로고    scopus 로고
    • Sterol regulators of cholesterol homeostasis and beyond: The oxysterol hypothesis revisited and revised
    • Gill, S., Chow, R., and Brown, A. J. (2008) Sterol regulators of cholesterol homeostasis and beyond: the oxysterol hypothesis revisited and revised. Prog. Lipid Res. 47, 391-404
    • (2008) Prog. Lipid Res. , vol.47 , pp. 391-404
    • Gill, S.1    Chow, R.2    Brown, A.J.3
  • 30
    • 0030615072 scopus 로고    scopus 로고
    • Ro 48-8071, a new 2,3-oxidosqualene: Lanosterol cyclase inhibitor lowering plasma cholesterol in hamsters, squirrel monkeys, and minipigs: Comparison to simvastatin
    • Morand, O. H., Aebi, J. D., Dehmlow, H., Ji, Y. H., Gains, N., Lengsfeld, H., and Himber, J. (1997) Ro 48-8071, a new 2,3-oxidosqualene: lanosterol cyclase inhibitor lowering plasma cholesterol in hamsters, squirrel monkeys, and minipigs: comparison to simvastatin. J. Lipid Res. 38, 373-390
    • (1997) J. Lipid Res. , vol.38 , pp. 373-390
    • Morand, O.H.1    Aebi, J.D.2    Dehmlow, H.3    Ji, Y.H.4    Gains, N.5    Lengsfeld, H.6    Himber, J.7
  • 31
    • 65249180182 scopus 로고    scopus 로고
    • Suppression of 2,3-oxidosqualene cyclase by high fat diet contributes to liver X receptor - Mediated improvement of hepatic lipid profile
    • Dang, H., Liu, Y., Pang, W., Li, C., Wang, N., Shyy, J. Y., and Zhu, Y. (2009) Suppression of 2,3-oxidosqualene cyclase by high fat diet contributes to liver X receptor-mediated improvement of hepatic lipid profile. J. Biol. Chem. 284, 6218-6226
    • (2009) J. Biol. Chem. , vol.284 , pp. 6218-6226
    • Dang, H.1    Liu, Y.2    Pang, W.3    Li, C.4    Wang, N.5    Shyy, J.Y.6    Zhu, Y.7
  • 32
    • 84895820661 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase MARCH6 degrades squalene monooxygenase and affects 3-hydroxy-3-methyl-glutaryl coenzyme A reductase and the cholesterol synthesis pathway
    • Zelcer, N., Sharpe, L. J., Loregger, A., Kristiana, I., Cook, E. C. L., Phan, L., Stevenson, J., and Brown, A. J. (2014) The E3 ubiquitin ligase MARCH6 degrades squalene monooxygenase and affects 3-hydroxy-3-methyl-glutaryl coenzyme A reductase and the cholesterol synthesis pathway. Mol. Cell. Biol. 34, 1262-1270
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 1262-1270
    • Zelcer, N.1    Sharpe, L.J.2    Loregger, A.3    Kristiana, I.4    Cook, E.C.L.5    Phan, L.6    Stevenson, J.7    Brown, A.J.8
  • 33
    • 84880707873 scopus 로고    scopus 로고
    • Sterol homeostasis requires regulated degradation of squalene monooxygenase by the ubiquitin ligase Doa10/Teb4
    • Foresti, O., Ruggiano, A., Hannibal-Bach, H. K., Ejsing, C. S., and Carvalho, P. (2013) Sterol homeostasis requires regulated degradation of squalene monooxygenase by the ubiquitin ligase Doa10/Teb4. eLife 2, e00953
    • (2013) ELife , vol.2
    • Foresti, O.1    Ruggiano, A.2    Hannibal-Bach, H.K.3    Ejsing, C.S.4    Carvalho, P.5
  • 35
    • 34247381583 scopus 로고    scopus 로고
    • Synthesis of the oxysterol, 24(S), 25-epoxycholesterol, parallels cholesterol production and may protect against cellular accumulation of newly-synthesized cholesterol
    • Wong, J., Quinn, C. M., and Brown, A. J. (2007) Synthesis of the oxysterol, 24(S), 25-epoxycholesterol, parallels cholesterol production and may protect against cellular accumulation of newly-synthesized cholesterol. Lipids Health Dis. 6, 10
    • (2007) Lipids Health Dis. , vol.6 , pp. 10
    • Wong, J.1    Quinn, C.M.2    Brown, A.J.3
  • 36
    • 84879588228 scopus 로고    scopus 로고
    • Controlling cholesterol synthesis beyond 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR)
    • Sharpe, L. J., and Brown, A. J. (2013) Controlling cholesterol synthesis beyond 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR). J. Biol. Chem. 288, 18707-18715
    • (2013) J. Biol. Chem. , vol.288 , pp. 18707-18715
    • Sharpe, L.J.1    Brown, A.J.2
  • 37
    • 0027321760 scopus 로고
    • Fatty alcohol accumulation in the autosomal recessive form of rhizomelic chondrodysplasia punctata
    • Rizzo, W. B., Craft, D. A., Judd, L. L., Moser, H. W., and Moser, A. B. (1993) Fatty alcohol accumulation in the autosomal recessive form of rhizomelic chondrodysplasia punctata. Biochem. Med. Metab. Biol. 50, 93-102
    • (1993) Biochem. Med. Metab. Biol. , vol.50 , pp. 93-102
    • Rizzo, W.B.1    Craft, D.A.2    Judd, L.L.3    Moser, H.W.4    Moser, A.B.5
  • 38
    • 84864522297 scopus 로고    scopus 로고
    • Sterols regulate 3-hydroxysterol -24-reductase (DHCR24) via dual sterol regulatory elements: Cooperative induction of key enzymes in lipid synthesis by sterol regulatory element binding proteins
    • Zerenturk, E. J., Sharpe, L. J., and Brown, A. J. (2012) Sterols regulate 3-hydroxysterol -24-reductase (DHCR24) via dual sterol regulatory elements: cooperative induction of key enzymes in lipid synthesis by sterol regulatory element binding proteins. Biochim. Biophys. Acta 1821, 1350-1360
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 1350-1360
    • Zerenturk, E.J.1    Sharpe, L.J.2    Brown, A.J.3
  • 39
    • 30344473341 scopus 로고    scopus 로고
    • Protein sensors for membrane sterols
    • Goldstein, J. L., DeBose-Boyd, R. A., and Brown, M. S. (2006) Protein sensors for membrane sterols. Cell 124, 35-46
    • (2006) Cell , vol.124 , pp. 35-46
    • Goldstein, J.L.1    DeBose-Boyd, R.A.2    Brown, M.S.3
  • 40
    • 77956176288 scopus 로고    scopus 로고
    • Sterol metabolism and SREBP activation
    • Sato, R. (2010) Sterol metabolism and SREBP activation. Arch. Biochem. Biophys. 501, 177-181
    • (2010) Arch. Biochem. Biophys. , vol.501 , pp. 177-181
    • Sato, R.1
  • 41
    • 0032574043 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes: IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro
    • Nagase, T., Ishikawa, K., Miyajima, N., Tanaka, A., Kotani, H., Nomura, N., and Ohara, O. (1998) Prediction of the coding sequences of unidentified human genes: IX. the complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 5, 31-39
    • (1998) DNA Res. , vol.5 , pp. 31-39
    • Nagase, T.1    Ishikawa, K.2    Miyajima, N.3    Tanaka, A.4    Kotani, H.5    Nomura, N.6    Ohara, O.7
  • 45
    • 0023447484 scopus 로고
    • Biosynthesis and biotransformation of ether lipids
    • Mangold, H. K., and Weber, N. (1987) Biosynthesis and biotransformation of ether lipids. Lipids 22, 789-799
    • (1987) Lipids , vol.22 , pp. 789-799
    • Mangold, H.K.1    Weber, N.2
  • 47
    • 0029099882 scopus 로고
    • Purification and characterization of recombinant squalene epoxidase
    • Nagumo, A., Kamei, T., Sakakibara, J., and Ono, T. (1995) Purification and characterization of recombinant squalene epoxidase. J. Lipid Res. 36, 1489-1497
    • (1995) J. Lipid Res. , vol.36 , pp. 1489-1497
    • Nagumo, A.1    Kamei, T.2    Sakakibara, J.3    Ono, T.4
  • 48
    • 0025900025 scopus 로고
    • Effect of a novel squalene epoxidase inhibitor, NB-598, on the regulation of cholesterol metabolism in HepG2 cells
    • Hidaka, Y., Hotta, H., Nagata, Y., Iwasawa, Y., Horie, M., and Kamei, T. (1991) Effect of a novel squalene epoxidase inhibitor, NB-598, on the regulation of cholesterol metabolism in HepG2 cells. J. Biol. Chem. 266, 13171-13177
    • (1991) J. Biol. Chem. , vol.266 , pp. 13171-13177
    • Hidaka, Y.1    Hotta, H.2    Nagata, Y.3    Iwasawa, Y.4    Horie, M.5    Kamei, T.6
  • 50
    • 0029947979 scopus 로고    scopus 로고
    • Effectiveness and safety of low-dose pravastatin and squalene, alone and in combination, in elderly patients with hypercholesterolemia
    • Chan, P., Tomlinson, B., Lee, C. B., and Lee, Y. S. (1996) Effectiveness and safety of low-dose pravastatin and squalene, alone and in combination, in elderly patients with hypercholesterolemia. J. Clin. Pharmacol. 36, 422-427
    • (1996) J. Clin. Pharmacol. , vol.36 , pp. 422-427
    • Chan, P.1    Tomlinson, B.2    Lee, C.B.3    Lee, Y.S.4
  • 51
    • 0242613116 scopus 로고
    • Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in human fibroblasts by lipoproteins
    • Brown, M. S., Dana, S. E., and Goldstein, J. L. (1973) Regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in human fibroblasts by lipoproteins. Proc. Natl. Acad. Sci. U.S.A. 70, 2162-2166
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 2162-2166
    • Brown, M.S.1    Dana, S.E.2    Goldstein, J.L.3
  • 54
    • 65449182422 scopus 로고    scopus 로고
    • Peroxisome deficiency causes a complex phenotype because of hepatic SREBP/Insig dysregulation associated with endoplasmic reticulum stress
    • Kovacs, W. J., Tape, K. N., Shackelford, J. E., Wikander, T. M., Richards, M. J., Fliesler, S. J., Krisans, S. K., and Faust, P. L. (2009) Peroxisome deficiency causes a complex phenotype because of hepatic SREBP/Insig dysregulation associated with endoplasmic reticulum stress. J. Biol. Chem. 284, 7232-7245
    • (2009) J. Biol. Chem. , vol.284 , pp. 7232-7245
    • Kovacs, W.J.1    Tape, K.N.2    Shackelford, J.E.3    Wikander, T.M.4    Richards, M.J.5    Fliesler, S.J.6    Krisans, S.K.7    Faust, P.L.8
  • 55
    • 84895182182 scopus 로고    scopus 로고
    • Cholesterol biosynthesis and ER stress in peroxisome deficiency
    • Faust, P. L., and Kovacs, W. J. (2014) Cholesterol biosynthesis and ER stress in peroxisome deficiency. Biochimie 98, 75-85
    • (2014) Biochimie , vol.98 , pp. 75-85
    • Faust, P.L.1    Kovacs, W.J.2
  • 56
    • 0035978394 scopus 로고    scopus 로고
    • Isoprenoid biosynthesis is not compromised in a Zellweger syndrome mouse model
    • Vanhorebeek, I., Baes, M., and Declercq, P. E. (2001) Isoprenoid biosynthesis is not compromised in a Zellweger syndrome mouse model. Biochim. Biophys. Acta 1532, 28-36
    • (2001) Biochim. Biophys. Acta , vol.1532 , pp. 28-36
    • Vanhorebeek, I.1    Baes, M.2    Declercq, P.E.3
  • 57
    • 0142027805 scopus 로고    scopus 로고
    • Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes
    • Horton, J. D., Shah, N. A., Warrington, J. A., Anderson, N. N., Park, S. W., Brown, M. S., and Goldstein, J. L. (2003) Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes. Proc. Natl. Acad. Sci. U.S.A. 100, 12027-12032
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 12027-12032
    • Horton, J.D.1    Shah, N.A.2    Warrington, J.A.3    Anderson, N.N.4    Park, S.W.5    Brown, M.S.6    Goldstein, J.L.7
  • 58
    • 0017351118 scopus 로고
    • Squalene epoxidase and oxidosqualene lanosterol-cyclase activities in cholesterogenic and non-cholesterogenic tissues
    • Astruc, M., Tabacik, C., Descomps, B., and de Paulet, A. C. (1977) Squalene epoxidase and oxidosqualene lanosterol-cyclase activities in cholesterogenic and non-cholesterogenic tissues. Biochim. Biophys. Acta 487, 204-211
    • (1977) Biochim. Biophys. Acta , vol.487 , pp. 204-211
    • Astruc, M.1    Tabacik, C.2    Descomps, B.3    De Paulet, A.C.4
  • 59
    • 79960121018 scopus 로고    scopus 로고
    • Purification, identification, and cloning of lysoplasmalogenase, the enzyme that catalyzes hydrolysis of the vinyl ether bond of lysoplasmalogen
    • Wu, L. C., Pfeiffer, D. R., Calhoon, E. A., Madiai, F., Marcucci, G., Liu, S., and Jurkowitz, M. S. (2011) Purification, identification, and cloning of lysoplasmalogenase, the enzyme that catalyzes hydrolysis of the vinyl ether bond of lysoplasmalogen. J. Biol. Chem. 286, 24916-24930
    • (2011) J. Biol. Chem. , vol.286 , pp. 24916-24930
    • Wu, L.C.1    Pfeiffer, D.R.2    Calhoon, E.A.3    Madiai, F.4    Marcucci, G.5    Liu, S.6    Jurkowitz, M.S.7
  • 60
    • 84863983024 scopus 로고    scopus 로고
    • The endogenous regulator 24(S),25-epoxycholesterol inhibits cholesterol synthesis at DHCR24 (Seladin-1)
    • Zerenturk, E. J., Kristiana, I., Gill, S., and Brown, A. J. (2012) The endogenous regulator 24(S),25-epoxycholesterol inhibits cholesterol synthesis at DHCR24 (Seladin-1). Biochim. Biophys. Acta 1821, 1269-1277
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 1269-1277
    • Zerenturk, E.J.1    Kristiana, I.2    Gill, S.3    Brown, A.J.4
  • 61
    • 59649086858 scopus 로고    scopus 로고
    • 24(S),25-Epoxycholesterol: A messenger for cholesterol homeostasis
    • Brown, A. J. (2009) 24(S),25-Epoxycholesterol: a messenger for cholesterol homeostasis. Int. J. Biochem. Cell Biol. 41, 744-747
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 744-747
    • Brown, A.J.1
  • 63
    • 10644229420 scopus 로고    scopus 로고
    • Statins inhibit synthesis of an oxysterol ligand for the liver X receptor in human macrophages with consequences for cholesterol flux
    • Wong, J., Quinn, C. M., and Brown, A. J. (2004) Statins inhibit synthesis of an oxysterol ligand for the liver X receptor in human macrophages with consequences for cholesterol flux. Arterioscler. Thromb. Vasc. Biol. 24, 2365-2371
    • (2004) Arterioscler. Thromb. Vasc. Biol. , vol.24 , pp. 2365-2371
    • Wong, J.1    Quinn, C.M.2    Brown, A.J.3
  • 64
    • 84901937811 scopus 로고    scopus 로고
    • Liver X receptors in lipid metabolism: Opportunities for drug discovery
    • Hong, C., and Tontonoz, P. (2014) Liver X receptors in lipid metabolism: opportunities for drug discovery. Nat. Rev. Drug Discov. 13, 433-444
    • (2014) Nat. Rev. Drug Discov. , vol.13 , pp. 433-444
    • Hong, C.1    Tontonoz, P.2
  • 65
    • 33845587711 scopus 로고    scopus 로고
    • Enzymatic reduction of oxysterols impairs LXR signaling in cultured cells and the livers of mice
    • Chen, W., Chen, G., Head, D. L., Mangelsdorf, D. J., and Russell, D. W. (2007) Enzymatic reduction of oxysterols impairs LXR signaling in cultured cells and the livers of mice. Cell Metab. 5, 73-79
    • (2007) Cell Metab. , vol.5 , pp. 73-79
    • Chen, W.1    Chen, G.2    Head, D.L.3    Mangelsdorf, D.J.4    Russell, D.W.5
  • 66
    • 67650092919 scopus 로고    scopus 로고
    • LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor
    • Zelcer, N., Hong, C., Boyadjian, R., and Tontonoz, P. (2009) LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor. Science 325, 100-104
    • (2009) Science , vol.325 , pp. 100-104
    • Zelcer, N.1    Hong, C.2    Boyadjian, R.3    Tontonoz, P.4
  • 67
    • 0032544519 scopus 로고    scopus 로고
    • Plasmalogen phospholipids are involved in HDL-mediated cholesterol efflux: Insights from investigations with plasmalogen-deficient cells
    • Mandel, H., Sharf, R., Berant, M., Wanders, R. J. A., Vreken, P., and Aviram, M. (1998) Plasmalogen phospholipids are involved in HDL-mediated cholesterol efflux: insights from investigations with plasmalogen-deficient cells. Biochem. Biophys. Res. Commun. 250, 369-373
    • (1998) Biochem. Biophys. Res. Commun. , vol.250 , pp. 369-373
    • Mandel, H.1    Sharf, R.2    Berant, M.3    Wanders, R.J.A.4    Vreken, P.5    Aviram, M.6
  • 70
    • 33746366462 scopus 로고    scopus 로고
    • Biochemistry of mammalian peroxisomes revisited
    • Wanders, R. J. A., and Waterham, H. R. (2006) Biochemistry of mammalian peroxisomes revisited. Annu. Rev. Biochem. 75, 295-332
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 295-332
    • Wanders, R.J.A.1    Waterham, H.R.2
  • 71
    • 0005876095 scopus 로고
    • The distribution of phosphorus-containing lipid compounds in the human brain
    • Balakrishnan, S., Goodwin, H., and Cumings, J. N. (1961) The distribution of phosphorus-containing lipid compounds in the human brain. J. Neurochem. 8, 276-284
    • (1961) J. Neurochem. , vol.8 , pp. 276-284
    • Balakrishnan, S.1    Goodwin, H.2    Cumings, J.N.3
  • 72
    • 0035023152 scopus 로고    scopus 로고
    • Plasmalogen deficiency in early Alzheimer's disease subjects and in animal models: Molecular characterization using electrospray ionization mass spectrometry
    • Han, X., Holtzman, D. M., and McKeel, D. W., Jr. (2001) Plasmalogen deficiency in early Alzheimer's disease subjects and in animal models: molecular characterization using electrospray ionization mass spectrometry. J. Neurochem. 77, 1168-1180
    • (2001) J. Neurochem. , vol.77 , pp. 1168-1180
    • Han, X.1    Holtzman, D.M.2    McKeel, D.W.3
  • 73
    • 79953769393 scopus 로고    scopus 로고
    • Lipid metabolism and glial lipoproteins in the central nervous system
    • Hayashi, H. (2011) Lipid metabolism and glial lipoproteins in the central nervous system. Biol. Pharm. Bull. 34, 453-461
    • (2011) Biol. Pharm. Bull. , vol.34 , pp. 453-461
    • Hayashi, H.1
  • 74
    • 61849180931 scopus 로고    scopus 로고
    • Marked differences in cholesterol synthesis between neurons and glial cells from postnatal rats
    • Nieweg, K., Schaller, H., and Pfrieger, F. W. (2009) Marked differences in cholesterol synthesis between neurons and glial cells from postnatal rats. J. Neurochem. 109, 125-134
    • (2009) J. Neurochem. , vol.109 , pp. 125-134
    • Nieweg, K.1    Schaller, H.2    Pfrieger, F.W.3
  • 75
    • 0028839090 scopus 로고
    • Molecular cloning and expression of rat squalene epoxidase
    • Sakakibara, J., Watanabe, R., Kanai, Y., and Ono, T. (1995) Molecular cloning and expression of rat squalene epoxidase. J. Biol. Chem. 270, 17-20
    • (1995) J. Biol. Chem. , vol.270 , pp. 17-20
    • Sakakibara, J.1    Watanabe, R.2    Kanai, Y.3    Ono, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.