The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
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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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
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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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