메뉴 건너뛰기




Volumn 65, Issue 8, 2013, Pages 675-684

The role of signalling in cellular cholesterol homeostasis

Author keywords

ABCA1; cholesterol; efflux; kinase; phosphorylation; signalling

Indexed keywords

ABC TRANSPORTER A1; CASEIN KINASE II; CHOLESTEROL; CYCLIC AMP; JANUS KINASE 2; LIPID; LOW DENSITY LIPOPROTEIN RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATASE; PHOSPHOTRANSFERASE; PROTEIN KINASE C; STEROL REGULATORY ELEMENT BINDING PROTEIN 2; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR LXR; TRANSCRIPTION FACTOR SREBP 2; UNCLASSIFIED DRUG;

EID: 84890699334     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.1182     Document Type: Review
Times cited : (45)

References (62)
  • 3
  • 4
    • 79960624651 scopus 로고    scopus 로고
    • The complex interplay between cholesterol and prostate malignancy
    • Solomon, K. R., and, Freeman, M. R., (2011) The complex interplay between cholesterol and prostate malignancy. Urol. Clin. N Am. 38, 243-259.
    • (2011) Urol. Clin. N Am. , vol.38 , pp. 243-259
    • Solomon, K.R.1    Freeman, M.R.2
  • 5
    • 84873716248 scopus 로고    scopus 로고
    • Cholesterol accumulation in prostate cancer: A classic observation from a modern perspective
    • Krycer, J. R., and, Brown, A. J., (2013) Cholesterol accumulation in prostate cancer: a classic observation from a modern perspective. Biochim. Biophys. Acta 1835, 219-229.
    • (2013) Biochim. Biophys. Acta , vol.1835 , pp. 219-229
    • Krycer, J.R.1    Brown, A.J.2
  • 6
    • 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
    • DOI 10.1091/mbc.E05-11-1094
    • 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. (Pubitemid 43825509)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.6 , pp. 2735-2745
    • Du, X.1    Kristiana, I.2    Wong, J.3    Brown, A.J.4
  • 7
    • 84855808743 scopus 로고    scopus 로고
    • Akt acutely activates the cholesterogenic transcription factor SREBP-2
    • Luu, W., Sharpe, L. J., Stevenson, J., and, Brown, A. J., (2012) Akt acutely activates the cholesterogenic transcription factor SREBP-2. Biochim. Biophys. Acta 1823, 458-464.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 458-464
    • Luu, W.1    Sharpe, L.J.2    Stevenson, J.3    Brown, A.J.4
  • 8
    • 48949115069 scopus 로고    scopus 로고
    • Rapamycin down-regulates LDL-receptor expression independently of SREBP-2. Biochem
    • Sharpe, L. J., and, Brown, A. J., (2008) Rapamycin down-regulates LDL-receptor expression independently of SREBP-2. Biochem. Biophys. Res. Commun. 373, 670-674.
    • (2008) Biophys. Res. Commun. , vol.373 , pp. 670-674
    • Sharpe, L.J.1    Brown, A.J.2
  • 9
    • 50049116472 scopus 로고    scopus 로고
    • SREBP activity is regulated by mTORC1 and contributes to Akt-dependent cell growth
    • Porstmann, T., Santos, C. R., Griffiths, B., Cully, M., Wu, M., et al. (2008) SREBP activity is regulated by mTORC1 and contributes to Akt-dependent cell growth. Cell Metab. 8, 224-236.
    • (2008) Cell Metab. , vol.8 , pp. 224-236
    • Porstmann, T.1    Santos, C.R.2    Griffiths, B.3    Cully, M.4    Wu, M.5
  • 11
    • 65549140251 scopus 로고    scopus 로고
    • A phosphorylation cascade controls the degradation of active SREBP1
    • Bengoechea-Alonso, M. T., and, Ericsson, J., (2009) A phosphorylation cascade controls the degradation of active SREBP1. J. Biol. Chem. 284, 5885-5895.
    • (2009) J. Biol. Chem. , vol.284 , pp. 5885-5895
    • Bengoechea-Alonso, M.T.1    Ericsson, J.2
  • 12
    • 2542418816 scopus 로고    scopus 로고
    • Insulin-activated Erk-mitogen-activated protein kinases phosphorylate sterol regulatory element-binding protein-2 at serine residues 432 and 455 in vivo
    • DOI 10.1074/jbc.M401198200
    • Kotzka, J., Lehr, S., Roth, G., Avci, H., Knebel, B., et al. (2004) Insulin-activated Erk-mitogen-activated protein kinases phosphorylate sterol regulatory element-binding Protein-2 at serine residues 432 and 455 in vivo. J. Biol. Chem. 279, 22404-22411. (Pubitemid 38679438)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.21 , pp. 22404-22411
    • Kotzka, J.1    Lehr, S.2    Roth, G.3    Avci, H.4    Knebel, B.5    Muller-Wieland, D.6
  • 13
    • 47249140920 scopus 로고    scopus 로고
    • Growth factor-induced phosphorylation of sterol regulatory element-binding proteins inhibits sumoylation, thereby stimulating the expression of their target genes, low density lipoprotein uptake, and lipid synthesis
    • Arito, M., Horiba, T., Hachimura, S., Inoue, J., and, Sato, R., (2008) Growth factor-induced phosphorylation of sterol regulatory element-binding proteins inhibits sumoylation, thereby stimulating the expression of their target genes, low density lipoprotein uptake, and lipid synthesis. J. Biol. Chem. 283, 15224-15231.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15224-15231
    • Arito, M.1    Horiba, T.2    Hachimura, S.3    Inoue, J.4    Sato, R.5
  • 14
    • 33747867030 scopus 로고    scopus 로고
    • Phosphorylation of the liver X receptors
    • DOI 10.1016/j.febslet.2006.07.074, PII S0014579306009306
    • Chen, M., Bradley, M. N., Beaven, S. W., and, Tontonoz, P., (2006) Phosphorylation of the liver X receptors. FEBS Lett. 580, 4835-4841. (Pubitemid 44286840)
    • (2006) FEBS Letters , vol.580 , Issue.20 , pp. 4835-4841
    • Chen, M.1    Bradley, M.N.2    Beaven, S.W.3    Tontonoz, P.4
  • 16
    • 79957576579 scopus 로고    scopus 로고
    • Control of nuclear receptor activities in metabolism by post-translational modifications
    • Berrabah, W., Aumercier, P., Lefebvre, P., and, Staels, B., (2011) Control of nuclear receptor activities in metabolism by post-translational modifications. FEBS Lett. 585, 1640-1650.
    • (2011) FEBS Lett. , vol.585 , pp. 1640-1650
    • Berrabah, W.1    Aumercier, P.2    Lefebvre, P.3    Staels, B.4
  • 17
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • Hornbeck, P. V., Kornhauser, J. M., Tkachev, S., Zhang, B., Skrzypek, E., et al. (2012) PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res. 40, D261-D270.
    • (2012) Nucleic Acids Res. , vol.40
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4    Skrzypek, E.5
  • 18
    • 0015864346 scopus 로고
    • Modulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity with cAMP and wth protein fractions of rat liver cytosol
    • Beg, Z. H., Allmann, D. W., and, Gibson, D. M., (1973) Modulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity with cAMP and wth protein fractions of rat liver cytosol. Biochem. Biophys. Res. Commun. 54, 1362-1369.
    • (1973) Biochem. Biophys. Res. Commun. , vol.54 , pp. 1362-1369
    • Beg, Z.H.1    Allmann, D.W.2    Gibson, D.M.3
  • 19
    • 84857687439 scopus 로고    scopus 로고
    • AMPK functions as an adenylate charge-regulated protein kinase
    • Oakhill, J. S., Scott, J. W., and, Kemp, B. E., (2012) AMPK functions as an adenylate charge-regulated protein kinase. Trends Endocrinol. Metab. 23, 125-132.
    • (2012) Trends Endocrinol. Metab. , vol.23 , pp. 125-132
    • Oakhill, J.S.1    Scott, J.W.2    Kemp, B.E.3
  • 20
    • 0025310576 scopus 로고
    • Regulation of HMG-CoA reductase: Identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver
    • Clarke, P. R., and, Hardie, D. G., (1990) Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver. EMBO J. 9, 2439-2446.
    • (1990) EMBO J. , vol.9 , pp. 2439-2446
    • Clarke, P.R.1    Hardie, D.G.2
  • 21
    • 79961118496 scopus 로고    scopus 로고
    • Regulation of HMG-CoA reductase in mammals and yeast
    • Burg, J. S., and, Espenshade, P. J,. (2011) Regulation of HMG-CoA reductase 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
  • 22
    • 0027428833 scopus 로고
    • Replacement of serine-871 of hamster 3-hydroxy-3-methylglutaryl-CoA reductase prevents phosphorylation by AMP-activated kinase and blocks inhibition of sterol synthesis induced by ATP depletion
    • DOI 10.1073/pnas.90.20.9261
    • Sato, R., Goldstein, J. L., and, Brown, M. S., (1993) Replacement of serine-871 of hamster 3-hydroxy-3-methylglutaryl-CoA reductase prevents phosphorylation by AMP-activated kinase and blocks inhibition of sterol synthesis induced by ATP depletion. Proc. Natl. Acad. Sci. USA 90, 9261-9265. (Pubitemid 23315763)
    • (1993) Proceedings of the National Academy of Sciences of the United States of America , vol.90 , Issue.20 , pp. 9261-9265
    • Sato, R.1    Goldstein, J.L.2    Brown, M.S.3
  • 23
    • 44849131929 scopus 로고    scopus 로고
    • Feedback regulation of cholesterol synthesis: Sterol-accelerated ubiquitination and degradation of HMG CoA reductase
    • DeBose-Boyd, R. A., (2008) Feedback regulation of cholesterol synthesis: sterol-accelerated ubiquitination and degradation of HMG CoA reductase. Cell Res. 18, 609-621.
    • (2008) Cell Res. , vol.18 , pp. 609-621
    • Debose-Boyd, R.A.1
  • 24
    • 84869021501 scopus 로고    scopus 로고
    • AMP-activated protein kinase: An emerging drug target to regulate imbalances in lipid and carbohydrate metabolism to treat cardio-metabolic diseases
    • Srivastava, R. A., Pinkosky, S. L., Filippov, S., Hanselman, J. C., Cramer, C. T., et al. (2012) AMP-activated protein kinase: an emerging drug target to regulate imbalances in lipid and carbohydrate metabolism to treat cardio-metabolic diseases. J. Lipid Res. 53, 2490-2514.
    • (2012) J. Lipid Res. , vol.53 , pp. 2490-2514
    • Srivastava, R.A.1    Pinkosky, S.L.2    Filippov, S.3    Hanselman, J.C.4    Cramer, C.T.5
  • 25
    • 84860469242 scopus 로고    scopus 로고
    • Increased hepatic synthesis and dysregulation of cholesterol metabolism is associated with the severity of nonalcoholic fatty liver disease
    • Min, H. K., Kapoor, A., Fuchs, M., Mirshahi, F., Zhou, H., et al. (2012) Increased hepatic synthesis and dysregulation of cholesterol metabolism is associated with the severity of nonalcoholic fatty liver disease. Cell Metab. 15, 665-674.
    • (2012) Cell Metab. , vol.15 , pp. 665-674
    • Min, H.K.1    Kapoor, A.2    Fuchs, M.3    Mirshahi, F.4    Zhou, H.5
  • 26
    • 0023149125 scopus 로고
    • Phosphorylation of serine 833 in cytoplasmic domain of low density lipoprotein receptor by a high molecular weight enzyme resembling casein kinase II
    • Kishimoto, A., Brown, M. S., Slaughter, C. A., and, Goldstein, J. L., (1987) Phosphorylation of serine 833 in cytoplasmic domain of low density lipoprotein receptor by a high molecular weight enzyme resembling casein kinase II. J. Biol. Chem. 262, 1344-1351. (Pubitemid 17028456)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.3 , pp. 1344-1351
    • Kishimoto, A.1    Brown, M.S.2    Slaughter, C.A.3    Goldstein, J.L.4
  • 27
    • 79953214429 scopus 로고    scopus 로고
    • Janus kinase activation by cytokine oncostatin M decreases PCSK9 expression in liver cells
    • Cao, A., Wu, M., Li, H., and, Liu, J., (2011) Janus kinase activation by cytokine oncostatin M decreases PCSK9 expression in liver cells. J. Lipid Res. 52, 518-530.
    • (2011) J. Lipid Res. , vol.52 , pp. 518-530
    • Cao, A.1    Wu, M.2    Li, H.3    Liu, J.4
  • 28
    • 44949241428 scopus 로고    scopus 로고
    • PCSK9 is phosphorylated by a Golgi casein kinase-like kinase ex vivo and circulates as a phosphoprotein in humans
    • DOI 10.1111/j.1742-4658.2008.06495.x
    • Dewpura, T., Raymond, A., Hamelin, J., Seidah, N. G., Mbikay, M., et al. (2008) PCSK9 is phosphorylated by a Golgi casein kinase-like kinase ex vivo and circulates as a phosphoprotein in humans. FEBS J. 275, 3480-3493. (Pubitemid 351813558)
    • (2008) FEBS Journal , vol.275 , Issue.13 , pp. 3480-3493
    • Dewpura, T.1    Raymond, A.2    Hamelin, J.3    Seidah, N.G.4    Mbikay, M.5    Chretien, M.6    Mayne, J.7
  • 30
    • 84857636796 scopus 로고    scopus 로고
    • Regulation of ABCA1 functions by signaling pathways
    • Liu, Y., and, Tang, C., (2012) Regulation of ABCA1 functions by signaling pathways. Biochim. Biophys. Acta 1821, 522-529.
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 522-529
    • Liu, Y.1    Tang, C.2
  • 31
    • 84856411164 scopus 로고    scopus 로고
    • Signal transduction pathways provide opportunities to enhance HDL and apoAI-dependent reverse cholesterol transport
    • Mulay, V., Wood, P., Rentero, C., Enrich, C., and, Grewal, T., (2012) Signal transduction pathways provide opportunities to enhance HDL and apoAI-dependent reverse cholesterol transport. Curr. Pharm. Biotechnol. 13, 352-364.
    • (2012) Curr. Pharm. Biotechnol. , vol.13 , pp. 352-364
    • Mulay, V.1    Wood, P.2    Rentero, C.3    Enrich, C.4    Grewal, T.5
  • 32
    • 0029804198 scopus 로고    scopus 로고
    • Cyclic AMP induces apolipoprotein E binding activity and promotes cholesterol efflux from a macrophage cell line to apolipoprotein acceptors
    • DOI 10.1074/jbc.271.48.30647
    • Smith, J. D., Miyata, M., Ginsberg, M., Grigaux, C., Shmookler, E., et al. (1996) Cyclic AMP induces apolipoprotein E binding activity and promotes cholesterol efflux from a macrophage cell line to apolipoprotein acceptors. J. Biol. Chem. 271, 30647-30655. (Pubitemid 26404080)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.48 , pp. 30647-30655
    • Smith, J.D.1    Miyata, M.2    Ginsberg, M.3    Grigaux, C.4    Shmookler, E.5    Plump, A.S.6
  • 33
    • 0034666311 scopus 로고    scopus 로고
    • The correlation of ATP-binding cassette 1 mRNA levels with cholesterol efflux from various cell lines
    • Bortnick, A. E., Rothblat, G. H., Stoudt, G., Hoppe, K. L., Royer, L. J., et al. (2000) The correlation of ATP-binding cassette 1 mRNA levels with cholesterol efflux from various cell lines. J. Biol. Chem. 275, 28634-28640.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28634-28640
    • Bortnick, A.E.1    Rothblat, G.H.2    Stoudt, G.3    Hoppe, K.L.4    Royer, L.J.5
  • 34
    • 0034602387 scopus 로고    scopus 로고
    • ABCA1 is the cAMP-inducible apolipoprotein receptor that mediates cholesterol secretion from macrophages
    • Oram, J. F., Lawn, R. M., Garvin, M. R., and, Wade, D. P., (2000) ABCA1 is the cAMP-inducible apolipoprotein receptor that mediates cholesterol secretion from macrophages. J. Biol. Chem. 275, 34508-34511.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34508-34511
    • Oram, J.F.1    Lawn, R.M.2    Garvin, M.R.3    Wade, D.P.4
  • 35
    • 24344446896 scopus 로고    scopus 로고
    • Lipid efflux in human and mouse macrophagic cells: Evidence for differential regulation of phospholipid and cholesterol efflux
    • DOI 10.1194/jlr.M400482-JLR200
    • Kiss, R. S., Maric, J., and, Marcel, Y. L., (2005) Lipid efflux in human and mouse macrophagic cells: evidence for differential regulation of phospholipid and cholesterol efflux. J. Lipid Res. 46, 1877-1887. (Pubitemid 41248484)
    • (2005) Journal of Lipid Research , vol.46 , Issue.9 , pp. 1877-1887
    • Kiss, R.S.1    Maric, J.2    Marcel, Y.L.3
  • 36
    • 0036906470 scopus 로고    scopus 로고
    • CAMP induces ABCA1 phosphorylation activity and promotes cholesterol efflux from fibroblasts
    • DOI 10.1194/jlr.M200235-JLR200
    • Haidar, B., Denis, M., Krimbou, L., Marcil, M., and, Genest, J., Jr., (2002) cAMP induces ABCA1 phosphorylation activity and promotes cholesterol efflux from fibroblasts. J. Lipid Res. 43, 2087-2094. (Pubitemid 35471076)
    • (2002) Journal of Lipid Research , vol.43 , Issue.12 , pp. 2087-2094
    • Haidar, B.1    Denis, M.2    Krimbou, L.3    Marcil, M.4    Genest Jr., J.5
  • 38
    • 1642300417 scopus 로고    scopus 로고
    • Apolipoprotein A-I activates cellular cAMP signaling through the ABCA1 transporter
    • DOI 10.1074/jbc.M313487200
    • Haidar, B., Denis, M., Marcil, M., Krimbou, L., and, Genest, J., Jr., (2004) Apolipoprotein A-I activates cellular cAMP signaling through the ABCA1 transporter. J. Biol. Chem. 279, 9963-9969. (Pubitemid 38372598)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.11 , pp. 9963-9969
    • Haidar, B.1    Denis, M.2    Marcil, M.3    Krimbou, L.4    Genest Jr., J.5
  • 39
    • 1542320076 scopus 로고    scopus 로고
    • Janus kinase 2 modulates the apolipoprotein interactions with abca1 required for removing cellular cholesterol
    • DOI 10.1074/jbc.M312571200
    • Tang, C., Vaughan, A. M., and Oram, J. F., (2004) Janus kinase 2 modulates the apolipoprotein interactions with ABCA1 required for removing cellular cholesterol. J. Biol. Chem. 279, 7622-7628. (Pubitemid 38294642)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7622-7628
    • Tang, C.1    Vaughan, A.M.2    Oram, J.F.3
  • 40
    • 73449097086 scopus 로고    scopus 로고
    • Expression and stability of two isoforms of ABCG1 in human vascular cells
    • Gelissen, I. C., Cartland, S., Brown, A. J., Sandoval, C., Kim, M., et al. (2010) Expression and stability of two isoforms of ABCG1 in human vascular cells. Atherosclerosis 208, 75-82.
    • (2010) Atherosclerosis , vol.208 , pp. 75-82
    • Gelissen, I.C.1    Cartland, S.2    Brown, A.J.3    Sandoval, C.4    Kim, M.5
  • 41
    • 84866152233 scopus 로고    scopus 로고
    • Protein kinase A modulates the activity of a major human isoform of ABCG1
    • Gelissen, I. C., Sharpe, L. J., Sandoval, C., Rao, G., Kockx, M., et al. (2012) Protein kinase A modulates the activity of a major human isoform of ABCG1. J. Lipid Res. 53, 2133-2140.
    • (2012) J. Lipid Res. , vol.53 , pp. 2133-2140
    • Gelissen, I.C.1    Sharpe, L.J.2    Sandoval, C.3    Rao, G.4    Kockx, M.5
  • 42
    • 84872390119 scopus 로고    scopus 로고
    • Species variation in ABCG1 isoform expression: Implications for the use of animal models in elucidating ABCG1 function
    • Burns, V., Sharpe, L. J., Gelissen, I. C., and, Brown, A. J., (2013) Species variation in ABCG1 isoform expression: implications for the use of animal models in elucidating ABCG1 function. Atherosclerosis 226, 408-411.
    • (2013) Atherosclerosis , vol.226 , pp. 408-411
    • Burns, V.1    Sharpe, L.J.2    Gelissen, I.C.3    Brown, A.J.4
  • 43
    • 34250902930 scopus 로고    scopus 로고
    • Targeting the protein kinase C family: Are we there yet?
    • DOI 10.1038/nrc2168, PII NRC2168
    • Mackay, H. J., and, Twelves, C. J., (2007) Targeting the protein kinase C family: are we there yet? Nat. Rev. Cancer 7, 554-562. (Pubitemid 46985395)
    • (2007) Nature Reviews Cancer , vol.7 , Issue.7 , pp. 554-562
    • Mackay, H.J.1    Twelves, C.J.2
  • 44
    • 0025553492 scopus 로고
    • Cholesterol efflux from adipose cells is coupled to diacylglycerol production and protein kinase C activation
    • Theret, N., Delbart, C., Aguie, G., Fruchart, J. C., Vassaux, G., et al. (1990) Cholesterol efflux from adipose cells is coupled to diacylglycerol production and protein kinase C activation. Biochem. Biophys. Res. Commun. 173, 1361-1368.
    • (1990) Biochem. Biophys. Res. Commun. , vol.173 , pp. 1361-1368
    • Theret, N.1    Delbart, C.2    Aguie, G.3    Fruchart, J.C.4    Vassaux, G.5
  • 45
    • 0025779078 scopus 로고
    • Protein kinase C as a mediator of high density lipoprotein receptor-dependent efflux of intracellular cholesterol
    • Mendez, A. J., Oram, J. F., and Bierman, E. L., (1991) Protein kinase C as a mediator of high density lipoprotein receptor-dependent efflux of intracellular cholesterol. J. Biol. Chem. 266, 10104-10111. (Pubitemid 21906774)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.16 , pp. 10104-10111
    • Mendez, A.J.1    Oram, J.F.2    Bierman, E.L.3
  • 46
    • 0030783089 scopus 로고    scopus 로고
    • Selective down-regulation by protein kinase C inhibitors of apolipoprotein-mediated cellular cholesterol efflux in macrophages
    • DOI 10.1021/bi970079t
    • Li, Q., Tsujita, M., and, Yokoyama, S., (1997) Selective down-regulation by protein kinase C inhibitors of apolipoprotein-mediated cellular cholesterol efflux in macrophages. Biochemistry 36, 12045-12052. (Pubitemid 27440942)
    • (1997) Biochemistry , vol.36 , Issue.40 , pp. 12045-12052
    • Li, Q.1    Tsujita, M.2    Yokoyama, S.3
  • 47
    • 0347918856 scopus 로고    scopus 로고
    • Apolipoprotein A-I Activates Protein Kinase Cα Signaling to Phosphorylate and Stabilize ATP Binding Cassette Transporter A1 for the High Density Lipoprotein Assembly
    • DOI 10.1074/jbc.M306258200
    • Yamauchi, Y., Hayashi, M., Abe-Dohmae, S., and, Yokoyama, S., (2003) Apolipoprotein A-I activates protein kinase C alpha signaling to phosphorylate and stabilize ATP binding cassette transporter A1 for the high density lipoprotein assembly. J. Biol. Chem. 278, 47890-47897. (Pubitemid 37523237)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.48 , pp. 47890-47897
    • Yamauchi, Y.1    Hayashi, M.2    Abe-Dohmae, S.3    Yokoyama, S.4
  • 48
    • 27744455987 scopus 로고    scopus 로고
    • Unsaturated fatty acids phosphorylate and destabilize ABCA1 through a phospholipase D2 pathway
    • DOI 10.1074/jbc.M506210200
    • Wang, Y., and, Oram, J. F., (2005) Unsaturated fatty acids phosphorylate and destabilize ABCA1 through a phospholipase D2 pathway. J. Biol. Chem. 280, 35896-35903. (Pubitemid 41633857)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.43 , pp. 35896-35903
    • Wang, Y.1    Oram, J.F.2
  • 49
    • 34248145949 scopus 로고    scopus 로고
    • Unsaturated fatty acids phosphorylate and destabilize ABCA1 through a protein kinase C δ pathway
    • DOI 10.1194/jlr.M600437-JLR200
    • Wang, Y., and, Oram, J. F., (2007) Unsaturated fatty acids phosphorylate and destabilize ABCA1 through a protein kinase C delta pathway. J. Lipid Res. 48, 1062-1068. (Pubitemid 46708673)
    • (2007) Journal of Lipid Research , vol.48 , Issue.5 , pp. 1062-1068
    • Wang, Y.1    Oram, J.F.2
  • 50
    • 77949887017 scopus 로고    scopus 로고
    • Inhibition of ERK1/2 and activation of liver X receptor synergistically induce macrophage ABCA1 expression and cholesterol efflux
    • Zhou, X., Yin, Z., Guo, X., Hajjar, D. P., and, Han, J., (2010) Inhibition of ERK1/2 and activation of liver X receptor synergistically induce macrophage ABCA1 expression and cholesterol efflux. J. Biol. Chem. 285, 6316-6326.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6316-6326
    • Zhou, X.1    Yin, Z.2    Guo, X.3    Hajjar, D.P.4    Han, J.5
  • 52
    • 84858201901 scopus 로고    scopus 로고
    • The interaction of ApoA-I and ABCA1 triggers signal transduction pathways to mediate efflux of cellular lipids
    • Zhao, G. J., Yin, K., Fu, Y. C., and, Tang, C. K., (2012) The interaction of ApoA-I and ABCA1 triggers signal transduction pathways to mediate efflux of cellular lipids. Mol. Med. 18, 149-158.
    • (2012) Mol. Med. , vol.18 , pp. 149-158
    • Zhao, G.J.1    Yin, K.2    Fu, Y.C.3    Tang, C.K.4
  • 53
    • 0141844589 scopus 로고    scopus 로고
    • Phosphorylation of a pest sequence in ABCA1 promotes calpain degradation and is reversed by ApoA-I
    • DOI 10.1074/jbc.M307161200
    • Martinez, L. O., Agerholm-Larsen, B., Wang, N., Chen, W., and, Tall, A. R., (2003) Phosphorylation of a pest sequence in ABCA1 promotes calpain degradation and is reversed by ApoA-I. J. Biol. Chem. 278, 37368-37374. (Pubitemid 37175255)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37368-37374
    • Martinez, L.O.1    Agerholm-Larsen, B.2    Wang, N.3    Chen, W.4    Tall, A.R.5
  • 56
    • 8344222640 scopus 로고    scopus 로고
    • Cyclosporin A traps ABCA1 at the plasma membrane and inhibits ABCA1-mediated lipid efflux to apolipoprotein A-I
    • DOI 10.1161/01.ATV.0000144811.94581.52
    • Le Goff, W., Peng, D. Q., Settle, M., Brubaker, G., Morton, R. E., et al. (2004) Cyclosporin A traps ABCA1 at the plasma membrane and inhibits ABCA1-mediated lipid efflux to apolipoprotein A-I. Arterioscler. Thromb. Vasc. Biol. 24, 2155-2161. (Pubitemid 39482445)
    • (2004) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.24 , Issue.11 , pp. 2155-2161
    • Le Goff, W.1    Peng, D.-Q.2    Settle, M.3    Brubaker, G.4    Morton, R.E.5    Smith, J.D.6
  • 57
    • 0026575932 scopus 로고
    • The mechanism of action of cyclosporin A and FK506
    • Schreiber, S. L., and, Crabtree, G. R., (1992) The mechanism of action of cyclosporin A and FK506. Immunol. Today 13, 136-142.
    • (1992) Immunol. Today , vol.13 , pp. 136-142
    • Schreiber, S.L.1    Crabtree, G.R.2
  • 58
    • 77951070514 scopus 로고    scopus 로고
    • Cholesterol efflux to apoA-I in ABCA1-expressing cells is regulated by Ca2+-dependent calcineurin signaling
    • Karwatsky, J., Ma, L., Dong, F., and, Zha, X., (2010) Cholesterol efflux to apoA-I in ABCA1-expressing cells is regulated by Ca2+-dependent calcineurin signaling. J. Lipid Res. 51, 1144-1156.
    • (2010) J. Lipid Res. , vol.51 , pp. 1144-1156
    • Karwatsky, J.1    Ma, L.2    Dong, F.3    Zha, X.4
  • 59
    • 84890645468 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase inhibition down-regulates ligand-induced ABCA1 expression
    • in press.
    • Luu, W., Sharpe, L. J., and, Brown, A. J., Protein tyrosine phosphatase inhibition down-regulates ligand-induced ABCA1 expression. Atherosclerosis, in press.
    • Atherosclerosis
    • Luu, W.1    Sharpe, L.J.2    Brown, A.J.3
  • 60
    • 72449192809 scopus 로고    scopus 로고
    • Guidelines for the effective use of chemical inhibitors of protein function to understand their roles in cell regulation
    • Cohen P., (2010) Guidelines for the effective use of chemical inhibitors of protein function to understand their roles in cell regulation. Biochem. J. 425, 53-54.
    • (2010) Biochem. J. , vol.425 , pp. 53-54
    • Cohen, P.1
  • 62
    • 34548511124 scopus 로고    scopus 로고
    • Rottlerin: An inappropriate and ineffective inhibitor of PKC
    • DOI 10.1016/j.tips.2007.07.003, PII S016561470700185X
    • Soltoff, S. P., (2007) Rottlerin: an inappropriate and ineffective inhibitor of PKCdelta. Trends Pharmacol. Sci. 28, 453-458. (Pubitemid 47371266)
    • (2007) Trends in Pharmacological Sciences , vol.28 , Issue.9 , pp. 453-458
    • Soltoff, S.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.