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Cited by 156Lipid metabolism and biosynthesisCancer, Lipids, and MetabolismAdipose Tissue and Metabolism

Localization of adipocyte long-chain fatty acyl-CoA synthetase at the plasma membrane

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Gargiulo, Christina E., Stuhlsatz-Krouper, Sarah M., Schaffer, Jean E.·1999·Journal of Lipid Research
DOI 10.1016/s0022-2275(20)32123-4
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Abstract

Long-chain fatty acyl-CoA synthetase (FACS) catalyzes esterification of long-chain fatty acids (LCFAs) with coenzyme A (CoA), the first step in fatty acid metabolism. FACS has been shown to play a role in LCFA import into bacteria and implicated to function in mammalian cell LCFA import. In the present study, we demonstrate that FACS overexpression in fibroblasts increases LCFA uptake, and overexpression of both FACS and the fatty acid transport protein (FATP) have synergistic effects on LCFA uptake. To explore how FACS contributes to LCFA import, we examined the subcellular location of this enzyme in 3T3-L1 adipocytes which natively express this protein and which efficiently take up LCFAs. We demonstrate for the first time that FACS is an integral membrane protein. Subcellular fractionation of adipocytes by differential density centrifugation reveals immunoreactive and enzymatically active FACS in several membrane fractions, including the plasma membrane. Immunofluorescence studies on adipocyte plasma membrane lawns confirm that FACS resides at the plasma membrane of adipocytes, where it co-distributes with FATP. Taken together, our data support a model in which imported LCFAs are immediately esterified at the plasma membrane upon uptake, and in which FATP and FACS function coordinately to facilitate LCFA movement across the plasma membrane of mammalian cells.

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  • CD36 has an important role in long-chain fatty acid uptake into skeletal muscle in rodents and humans, and its concentration and activity increase after exercise.

    “There is abundant evidence which indicates that CD36 plays an important role in LCFA uptake into skeletal muscle in rodents and human and its concentration and activity are increased following exercise [89–96].”

    From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [89]

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Authors
Gargiulo, C. E., Stuhlsatz-Krouper, S. M., & Schaffer, J. E.
Affiliations
Washington University in St. Louis (US)
Corresponding author
Schaffer, Jean E.
ORCID
Schaffer, Jean E.
Venue
Journal of Lipid Research
Publisher
Elsevier BV
Published
1999-05
Volume
40
Issue
5
Pages
881-892
ISSN
0022-2275 (ISSN-L)
DOI
10.1016/s0022-2275(20)32123-4
OpenAlex
W2148427109
Cited by
156
References
73
Citations by year
2025: 2 · 2024: 3 · 2023: 1 · 2022: 3 · 2021: 4 · 2020: 2 · 2019: 5 · 2018: 2 · 2017: 4 · 2016: 2 · 2015: 4 · 2014: 5 · 2013: 2 · 2012: 5
FWCI
5.21
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Lipid Research (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK054268, DK54268)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
  • Health Sciences › Medicine › Physiology › Adipose Tissue and Metabolism
Keywords
fatty acid esterification, long-chain fatty acid uptake, fatty acid transporters, plasma membrane localization, adipocytes, membrane proteins, fatty acid metabolism, 3T3-L1 adipocytes, fatty acid import
MeSH terms
Long-Chain-Fatty-Acid-CoA Ligase, Animals, Biological Transport, Active, Carrier Proteins, Cell Membrane, Coenzyme A Ligases, Fatty Acids, Membrane Proteins, Microscopy, Fluorescence, Models, Biological, Repressor Proteins, 3T3 Cells, Adipocytes, Membrane Transport Proteins, Saccharomyces cerevisiae Proteins, Fatty Acid Transport Proteins, Mice

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