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Regulation and immunolocalization of acyl-coenzyme A: cholesterol acyltransferase in mammalian cells as studied with specific antibodies
Open accessAbstract
Acyl-coenzyme A:cholesterol acyltransferase (ACAT) catalyzes the formation of intracellular cholesterol esters in various tissues. We recently reported the cloning and expression of human macrophage ACAT cDNA. In the current study, we report the production of specific polyclonal antibodies against ACAT by immunizing rabbits with the recombinant fusion protein composed of glutathione S-transferase and the first 131 amino acids of ACAT protein. Immunoblot analysis showed that the antibodies cross-reacted with a 50-kDa protein band from a variety of human cell lines. These antibodies immunodepleted more than 90% of detergent-solubilized ACAT activities from six different human cell types, demonstrating that the 50-kDa protein is the major ACAT catalytic component in these cells. In multiple human tissues examined, the antibodies recognized protein bands with various molecular weights. These antibodies also cross-reacted with the ACAT protein in Chinese hamster ovary cells. Immunoblot analysis showed that the ACAT protein contents in human fibroblast cells, HepG2 cells, or Chinese hamster ovary cells were not affected by sterol in the medium, demonstrating that the main mechanism for sterol-dependent regulation of ACAT activity in these cells is not change in ACAT protein content. As revealed by indirect immunofluorescent microscopy, the ACAT protein in tissue culture cells was located in the endoplasmic reticulum. This finding, along with earlier studies, suggests that cholesterol concentration in the endoplasmic reticulum may be the major determinant for regulating ACAT activity in the intact cells.
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Cites
Molecular Cloning: A Laboratory Manual
Sambrook, J., Fritsch, E., & Maniatis, T. (1989) · UCLA - Biblioteca de Ciencias de la Salud · Cited by 133,589
Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684
Antibodies, a laboratory manual
(1989) · Biomedicine & Pharmacotherapy · doi:10.1016/0753-3322(89)90130-3 · Cited by 12,318
Regulation of the mevalonate pathway
Goldstein, J. L., & Brown, M. S. (1990) · Nature · doi:10.1038/343425a0 · Cited by 5,394
The Low-Density Lipoprotein Pathway and its Relation to Atherosclerosis
Goldstein, L. J., & Brown, S. M. (1977) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.46.070177.004341 · Cited by 1,906
Chang, C. C., Huh, H. Y., Cadigan, K. M., & Chang, T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36846-2 · Cited by 389
Self-citationMembrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme
Gil, G., Faust, J. R., Chin, D. J., Goldstein, J. L., & Brown, M. S. (1985) · Cell · doi:10.1016/0092-8674(85)90078-9 · Cited by 386
Localization of endoplasmic reticulum in living and glutaraldehyde-fixed cells with fluorescent dyes
Terasaki, M., Song, J., Wong, J. R., Weiss, M. J., & Chen, L. B. (1984) · Cell · doi:10.1016/0092-8674(84)90530-0 · Cited by 385
Cholesterol ester formation in cultured human fibroblasts. Stimulation by oxygenated sterols.
Brown, M., Dana, S., & Goldstein, J. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41498-1 · Cited by 364
Hep G2 cells as a resource for metabolic studies: lipoprotein, cholesterol, and bile acids
Javitt, N. B. (1990) · The FASEB Journal · doi:10.1096/fasebj.4.2.2153592 · Cited by 357
Regulation of Plasma LDL-Cholesterol Levels by Dietary Cholesterol and Fatty Acids
Spady, D. K., Woollett, L. A., & Dietschy, J. M. (1993) · Annual Review of Nutrition · doi:10.1146/annurev.nu.13.070193.002035 · Cited by 292
Goldstein, J. L., Dana, S. E., & Brown, M. S. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.11.4288 · Cited by 290
Independent regulation of sterol regulatory element-binding proteins 1 and 2 in hamster liver.
Sheng, Z., Otani, H., Brown, M. S., & Goldstein, J. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.4.935 · Cited by 265
Transport of cholesterol from the endoplasmic reticulum to the plasma membrane.
Kaplan, M. R., & Simoni, R. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.2.446 · Cited by 263
Regulation of Plasma LDL-Cholesterol Levels by Dietary Cholesterol and Fatty Acids
Spady, D. K. (1993) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.13.1.355 · Cited by 243
Intracellular Cholesterol Transport and Compartmentation
Liscum, L., & Underwood, K. W. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.26.15443 · Cited by 226
Defective transforming capacity of adenovirus type 5 host-range mutants
Graham, F. L., Harrison, T., & Williams, J. (1978) · Virology · doi:10.1016/0042-6822(78)90003-x · Cited by 212
Intracellular transport of cholesterol to the plasma membrane.
DeGrella, R. F., & Simoni, R. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45374-x · Cited by 204
Roitelman, J., Olender, E. H., Bar‐Nun, S., Dunn, W. A., & Simoni, R. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.117.5.959 · Cited by 185
Cheng, D., Chang, C. C. Y., Qu, X., & Chang, T. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.685 · Cited by 169
Self-citationChang, T., & Limanek, J. S. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43901-x · Cited by 163
Self-citationDaumerie, C. M., Woollett, L. A., & Dietschy, J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.22.10797 · Cited by 147
Subcellular localization of the enzymes of cholesterol biosynthesis and metabolism in rat liver.
Reinhart, M. P., Billheimer, J. T., Faust, J. R., & Gaylor, J. L. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47983-5 · Cited by 134
Sarría, A. J., Panini, S. R., & Evans, R. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41797-8 · Cited by 126
Transfer of cholesterol from its site of synthesis to the plasma membrane.
Lange, Y., & Matthies, H. J. G. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42647-0 · Cited by 120
Havekes, L. M., de Wit, E. C. M., & Princen, H. M. G. (1987) · Biochemical Journal · doi:10.1042/bj2470739 · Cited by 109
Cadigan, K. M., Heider, J. G., & Chang, T. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)57389-6 · Cited by 93
Self-citationInduction of acetyl-LDL receptor activity by phorbol ester in human monocyte cell line THP-1.
Via, D. P., Pons, L., Dennison, D., Fanslow, A. E., & Bernini, F. (1989) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)38230-4 · Cited by 92
Tabas, I. A., Weiland, D. A., & Tall, A. R. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35761-7 · Cited by 78
Fatty acid esterification during differentiation of the human intestinal cell line Caco-2
Trotter, P. J., & Storch, J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82166-4 · Cited by 75
Correll, C. C., & Edwards, P. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42396-9 · Cited by 74
Chang, C. C. Y., Doolittle, G. M., & Chang, T. (1986) · Biochemistry · doi:10.1021/bi00355a038 · Cited by 67
Self-citationField, F. J., Born, E. J., Chen, H., Murthy, S., & Mathur, S. N. (1995) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)39740-6 · Cited by 67
Tissue specific changes in acyl-CoA: cholesterol acyltransferase (ACAT) mRNA levels in rabbits.
Pape, M. E., Schultz, P. A., Rea, T. J., Demattos, R. B., Kieft, K. A., Bisgaier, C. L., Newton, R. S., & Krause, B. R. (1995) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)40066-5 · Cited by 61
Self-citationAcyl-CoA:Cholesterol acyltransferase in chinese hamster ovary cells
Doolittle, G. M., & Chang, T. (1982) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(82)90313-7 · Cited by 60
Self-citationDoolittle, G. M., & Chang, T. Y. (1982) · Biochemistry · doi:10.1021/bi00533a014 · Cited by 58
Self-citationBiology of the A‐431 cell: A useful organism for hormone research
Stoscheck, C. M., & Carpenter, G. F. (1983) · Journal of Cellular Biochemistry · doi:10.1002/jcb.240230116 · Cited by 54
Tabas, I. A., & Boykow, G. C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45333-1 · Cited by 46
Chin, J., & Chang, T. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69163-5 · Cited by 45
Self-citationChang, T., Limanek, J. S., & Chang, C. C. Y. (1981) · Analytical Biochemistry · doi:10.1016/0003-2697(81)90360-2 · Cited by 43
Self-citationCadigan, K. M., & Chang, T. (1988) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)38416-9 · Cited by 33
Self-citationRegulated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in permeabilized cells.
Meigs, T. E., & Simoni, R. D. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42246-6 · Cited by 31
Cadigan, K. M., Chang, C. C. Y., & Chang, T. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.108.6.2201 · Cited by 30
Self-citationChang, T., Chang, C. C. Y., & Cadigan, K. M. (1994) · Trends in Cardiovascular Medicine · doi:10.1016/1050-1738(94)90038-8 · Cited by 27
Self-citationSalter, A. M., EKINS, N., Al‐Seeni, M. N., Brindley, D. N., & Middleton, B. S. (1989) · Biochemical Journal · doi:10.1042/bj2630255 · Cited by 20
Shi, S., Chang, C. C. Y., Gould, G. W., & Chang, T. (1989) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(89)90054-0 · Cited by 8
Self-citation
Research works printed but not linked: 1
- Uelmen, 1995, J. Biol. Chem.
Cited by
Sorted by citations
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Schroepfer, G. J. (2000) · Physiological Reviews · doi:10.1152/physrev.2000.80.1.361 · Cited by 984
The Surface of Lipid Droplets Is a Phospholipid Monolayer with a Unique Fatty Acid Composition
Tauchi-Sato, K., Ozeki, S., Houjou, T., Taguchi, R., & Fujimoto, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207712200 · Cited by 753
Mechanisms of lipid-body formation
Murphy, D. J., & Vance, J. E. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(98)01349-8 · Cited by 577
ACYL-COENZYME A:CHOLESTEROL ACYLTRANSFERASE
Chang, T. Y., Chang, C. C. Y., & Cheng, D. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.613 · Cited by 440
Self-citationAcyl‐coenzyme A:cholesterol acyltransferases
Chang, T.-Y., Li, B.-L., Chang, C. C. Y., & Urano, Y. (2009) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.90926.2008 · Cited by 443
Self-citation
Metadata
- Authors
- Catherine C. Y., C., Chen, J., Thomas, M. A., Cheng, D., Veronica A., D. P., Newton, R. S., Pape, M. E., & Chang, T.-Y.
- Affiliations
- Dartmouth College (US)
- Corresponding author
- Chang, Ta-Yuan
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-12
- Volume
- 270
- Issue
- 49
- Pages
- 29532-29540
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1996953344
- Cited by
- 158
- References
- 45
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2023: 4 · 2022: 3 · 2021: 3 · 2020: 4 · 2019: 3 · 2016: 1 · 2015: 7 · 2014: 6 · 2013: 1 · 2012: 3
- FWCI
- 10.33
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (HL 36709)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Physical Sciences › Chemistry › Organic Chemistry › Steroid Chemistry and Biochemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Keywords
- acyl-CoA:cholesterol acyltransferase, ACAT, polyclonal antibodies, immunolocalization, endoplasmic reticulum, cholesterol esterification, immunodepletion, human cell lines, CHO cells, HepG2 cells, fibroblasts
- MeSH terms
- Animals, Antibodies, Cell Line, Sterol O-Acyltransferase, Endoplasmic Reticulum, Cricetinae, Humans, Molecular Weight, Rabbits, Immunoblotting, CHO Cells
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