메뉴 건너뛰기




Volumn 287, Issue 21, 2012, Pages 17483-17492

Cellular pregnenolone esterification by Acyl-CoA:cholesterol acyltransferase

Author keywords

[No Author keywords available]

Indexed keywords

ACYL-COA:CHOLESTEROL ACYLTRANSFERASE; BINDING AFFINITIES; CELL TYPES; PREGNENOLONE; SIDE-CHAINS; SMALL MOLECULES; STERYL ESTERS;

EID: 84861214063     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.331306     Document Type: Article
Times cited : (21)

References (27)
  • 1
    • 48949093381 scopus 로고    scopus 로고
    • Steroidogenic enzymes
    • Miller, W. L. (2008) Steroidogenic enzymes. Endocr. Dev. 13, 1-18
    • (2008) Endocr. Dev. , vol.13 , pp. 1-18
    • Miller, W.L.1
  • 2
    • 77952800717 scopus 로고    scopus 로고
    • Cellular cholesterol delivery, intracellular processing and utilization for biosynthesis of steroid hormones
    • Hu, J., Zhang, Z., Shen, W. J., and Azhar, S. (2010) Cellular cholesterol delivery, intracellular processing and utilization for biosynthesis of steroid hormones. Nutr. Metab. 7, 47-73
    • (2010) Nutr. Metab. , vol.7 , pp. 47-73
    • Hu, J.1    Zhang, Z.2    Shen, W.J.3    Azhar, S.4
  • 3
    • 0018611739 scopus 로고
    • Characterization of the lipoidal derivatives of pregnenolone prepared by incubation of the steroid with adrenal mitochondria
    • Mellon-Nussbaum, S., Ponticorvo, L., and Lieberman, S. (1979) Characterization of the lipoidal derivatives of pregnenolone prepared by incubation of the steroid with adrenal mitochondria. J. Biol. Chem. 254, 12500-12505 (Pubitemid 10138176)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.24 , pp. 12500-12505
    • Mellon-Nussbaum, S.1    Ponticorvo, L.2    Lieberman, S.3
  • 4
    • 0020399484 scopus 로고
    • GLC/MS identification of new pregnenolone metabolites in confluent embryonic rat fibroblast cultures
    • DOI 10.1016/0022-4731(82)90034-6
    • Damon, M., and Chavis, C. (1982) GLC/MS identification of new pregnenolone metabolites in confluent embryonic rat fibroblast cultures. J. Steroid. Biochem. 16, 771-778 (Pubitemid 13228091)
    • (1982) Journal of Steroid Biochemistry , vol.16 , Issue.6 , pp. 771-778
    • Damon, M.1    Chavis, C.2
  • 5
    • 0025609473 scopus 로고
    • Steroid fatty acid esters in adrenals and plasma: Effects of ACTH
    • Bélanger, B., Caron, S., Bélanger, A., and Dupont, A. (1990) Steroid fatty acid esters in adrenals and plasma: effects of ACTH. J. Endocrinol. 127, 505-511
    • (1990) J. Endocrinol. , vol.127 , pp. 505-511
    • Bélanger, B.1    Caron, S.2    Bélanger, A.3    Dupont, A.4
  • 6
    • 0030020791 scopus 로고    scopus 로고
    • Formation of pregnenolone- and dehydroepiandrosterone-fatty acid esters by lecithin-cholesterol acyltransferase in human plasma high density lipoproteins
    • Lavallée, B., Provost, P. R., and Belanger, A. (1996) Formation of pregnenolone- and dehydroepiandrosterone-fatty acid esters by lecithin-cholesterol acyltransferase in human plasma high density lipoproteins. Biochim. Biophys. Acta 1299, 306-312
    • (1996) Biochim. Biophys. Acta , vol.1299 , pp. 306-312
    • Lavallée, B.1    Provost, P.R.2    Belanger, A.3
  • 9
    • 27844475676 scopus 로고    scopus 로고
    • The active site His-460 of human acyl-coenzyme A:cholesterol acyltransferase 1 resides in a hitherto undisclosed transmembrane domain
    • DOI 10.1074/jbc.M508384200
    • Guo, Z. Y., Lin, S., Heinen, J. A., Chang, C. C., and Chang, T. Y. (2005) The active site His-460 of human acyl-coenzyme A:cholesterol acyltransferase 1 resides in a hitherto undisclosed transmembrane domain. J. Biol. Chem. 280, 37814-37826 (Pubitemid 41642392)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.45 , pp. 37814-37826
    • Guo, Z.-Y.1    Lin, S.2    Heinen, J.A.3    Chang, C.C.Y.4    Chang, T.-Y.5
  • 10
    • 84861212469 scopus 로고    scopus 로고
    • Membrane bound O-acyltransferases (MBOAT)
    • Chang, C. C., Sun, J., and Chang, T. Y. (2011) Membrane bound O-acyltransferases (MBOAT). Front. Biol. 6, 177-182
    • (2011) Front. Biol. , vol.6 , pp. 177-182
    • Chang, C.C.1    Sun, J.2    Chang, T.Y.3
  • 11
    • 0038175518 scopus 로고    scopus 로고
    • Cholesterol is superior to 7-ketocholesterol or 7alpha-hydroxycholesterol as an allosteric activator for acyl-coenzyme A:Cholesterol acyltransferase 1
    • DOI 10.1074/jbc.M211559200
    • Zhang, Y., Yu, C., Liu, J., Spencer, T. A., Chang, C. C., and Chang, T. Y. (2003) Cholesterol is superior to 7-ketocholesterol or 7 alpha- hydroxycholesterol as an allosteric activator for acyl-coenzyme A:cholesterol acyltransferase 1. J. Biol. Chem. 278, 11642-11647 (Pubitemid 36792726)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.13 , pp. 11642-11647
    • Zhang, Y.1    Yu, C.2    Liu, J.3    Spencer, T.A.4    Chang, C.C.Y.5    Chang, T.-Y.6
  • 12
    • 27444431715 scopus 로고    scopus 로고
    • Investigating the allosterism of acyl-CoA:cholesterol acyltransferase (ACAT) by using various sterols: In vitro and intact cell studies
    • DOI 10.1042/BJ20050428
    • Liu, J., Chang, C. C., Westover, E. J., Covey, D. F., and Chang, T. Y. (2005) Investigating the allosterism of acyl-CoA:cholesterol acyltransferase (ACAT) by using various sterols: in vitro and intact cell studies. Biochem. J. 391, 389-397 (Pubitemid 41532437)
    • (2005) Biochemical Journal , vol.391 , Issue.2 , pp. 389-397
    • Liu, J.1    Chang, C.C.Y.2    Westover, E.J.3    Covey, D.F.4    Chang, T.-Y.5
  • 13
    • 0019051169 scopus 로고
    • A method for the chemical synthesis of 14C-labeled fatty acyl coenzyme A's of high specific activity
    • Bishop, J. E., and Hajra, A. K. (1980) A method for the chemical synthesis of 14C-labeled fatty acyl coenzyme A's of high specific activity. Anal. Biochem. 106, 344-350
    • (1980) Anal. Biochem. , vol.106 , pp. 344-350
    • Bishop, J.E.1    Hajra, A.K.2
  • 15
    • 0033579429 scopus 로고    scopus 로고
    • Human acyl-CoA:cholesterol acyltransferase-1 is a homotetrameric enzyme in intact cells and in vitro
    • Yu, C., Chen, J., Lin, S., Liu, J., Chang, C. C., and Chang, T. Y. (1999) Human acyl-CoA:cholesterol acyltransferase-1 is a homotetrameric enzyme in intact cells and in vitro. J. Biol. Chem. 274, 36139-36145
    • (1999) J. Biol. Chem. , vol.274 , pp. 36139-36145
    • Yu, C.1    Chen, J.2    Lin, S.3    Liu, J.4    Chang, C.C.5    Chang, T.Y.6
  • 16
    • 78649278881 scopus 로고    scopus 로고
    • Purification of recombinant acyl-coenzyme A:cholesterol acyltransferase 1 (ACAT1) from H293 cells and binding studies between the enzyme and substrates using difference intrinsic fluorescence spectroscopy
    • Chang, C. C., Miyazaki, A., Dong, R., Kheirollah, A., Yu, C., Geng, Y., Higgs, H. N., and Chang, T. Y. (2010) Purification of recombinant acyl-coenzyme A:cholesterol acyltransferase 1 (ACAT1) from H293 cells and binding studies between the enzyme and substrates using difference intrinsic fluorescence spectroscopy. Biochemistry 49, 9957-9963
    • (2010) Biochemistry , vol.49 , pp. 9957-9963
    • Chang, C.C.1    Miyazaki, A.2    Dong, R.3    Kheirollah, A.4    Yu, C.5    Geng, Y.6    Higgs, H.N.7    Chang, T.Y.8
  • 18
    • 10044255546 scopus 로고    scopus 로고
    • Novel lipoidal derivatives of pregnenolone and dehydroepiandrosterone and absence of their sulfated counterparts in rodent brain
    • DOI 10.1194/jlr.M400244-JLR200
    • Liere, P., Pianos, A., Eychenne, B., Cambourg, A., Liu, S., Griffiths, W., Schumacher, M., Sjövall, J., and Baulieu, E. E. (2004) Novel lipoidal derivatives of pregnenolone and dehydroepiandrosterone and absence of their sulfated counterparts in rodent brain. J. Lipid Res. 45, 2287-2302 (Pubitemid 39602976)
    • (2004) Journal of Lipid Research , vol.45 , Issue.12 , pp. 2287-2302
    • Liere, P.1    Pianos, A.2    Eychenne, B.3    Cambourg, A.4    Liu, S.5    Griffiths, W.6    Schumacher, M.7    Sjovall, J.8    Baulieu, E.-E.9
  • 19
    • 33746615977 scopus 로고    scopus 로고
    • Development and performance evaluation of a tandem mass spectrometry assay for 4 adrenal steroids
    • DOI 10.1373/clinchem.2006.068445
    • Kushnir, M. M., Rockwood, A. L., Roberts, W. L., Pattison, E. G., Owen, W. E., Bunker, A. M., and Meikle, A. W. (2006) Development and performance evaluation of a tandem mass spectrometry assay for 4 adrenal steroids. Clin. Chem. 52, 1559-1567 (Pubitemid 44148319)
    • (2006) Clinical Chemistry , vol.52 , Issue.8 , pp. 1559-1567
    • Kushnir, M.M.1    Rockwood, A.L.2    Roberts, W.L.3    Pattison, E.G.4    Owen, W.E.5    Bunker, A.M.6    Meikle, A.W.7
  • 22
    • 0036133869 scopus 로고    scopus 로고
    • Neurosteroids: Biochemistry and clinical significance
    • DOI 10.1016/S1043-2760(01)00503-3, PII S1043276001005033
    • Mellon, S. H., and Griffin, L. D. (2002) Neurosteroids: biochemistry and clinical significance. Trends Endocrinol. Metab. 13, 35-43 (Pubitemid 36734014)
    • (2002) Trends in Endocrinology and Metabolism , vol.13 , Issue.1 , pp. 35-43
    • Mellon, S.H.1    Griffin, L.D.2
  • 23
    • 0028982924 scopus 로고
    • Pregneolone-from Selye to Alzheimer and a model of the pregnenolone sulfate binding site on the GABAA receptor
    • Roberts, E. (1995) Pregneolone-from Selye to Alzheimer and a model of the pregnenolone sulfate binding site on the GABAA receptor. Biochem. Pharmacol. 49, 1-16
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 1-16
    • Roberts, E.1
  • 25
    • 0037133501 scopus 로고    scopus 로고
    • Role of the N-terminal hydrophilic domain of acyl-coenzyme A:cholesterol acyltransferase 1 on the enzyme's quaternary structure and catalytic efficiency
    • DOI 10.1021/bi0120188
    • Yu, C., Zhang, Y., Lu, X., Chen, J., Chang, C. C., and Chang, T. Y. (2002) Role of the N-terminal hydrophilic domain of acyl-coenzyme A:cholesterol acyltransferase 1 on the enzyme's quaternary structure and catalytic efficiency. Biochemistry 41, 3762-3769 (Pubitemid 34224690)
    • (2002) Biochemistry , vol.41 , Issue.11 , pp. 3762-3769
    • Yu, C.1    Zhang, Y.2    Lu, X.3    Chen, J.4    Chang, C.C.Y.5    Chang, T.-Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.