Cited by 218Cancer, Lipids, and MetabolismLipid metabolism and biosynthesisPeroxisome Proliferator-Activated Receptors

Characterization of a Heart-specific Fatty Acid Transport Protein

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Gimeno, Ruth E., Ortegon, Angelica M., Patel, Shraddha, Punreddy, Sandhya, Ge, Pei, Sun, Ying, Lodish, Harvey F., Stahl, Andreas·2003·Journal of Biological Chemistry

Abstract

Fatty acids are a major source of energy for cardiac myocytes. Changes in fatty acid metabolism have been implicated as causal in diabetes and cardiac disease. The mechanism by which long chain fatty acids (LCFAs) enter cardiac myocytes is not well understood but appears to occur predominantly by protein-mediated transport. Here we report the cloning, expression pattern, and subcellular localization of a novel member of the fatty acid transport protein (FATP) family termed FATP6. FATP6 is principally expressed in the heart where it is the predominant FATP family member. Similar to other FATPs, transient and stable transfection of FATP6 into 293 cells enhanced uptake of LCFAs. FATP6 mRNA was localized to cardiac myocytes by in situ hybridization. Immunofluorescence microscopy of FATP6 in monkey and murine hearts revealed that the protein is exclusively located on the sarcolemma. FATP6 was restricted in its distribution to areas of the plasma membrane juxtaposed with small blood vessels. In these membrane domains FATP6 also colocalizes with another molecule involved in LCFA uptake, CD36. These findings suggest that FATP6 is involved in heart LCFA uptake, in which it may play a role in the pathogenesis of lipid-related cardiac disorders.

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  1. Hirsch, D., Stahl, A., and Lodish, H. F. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 8625-8629
  2. Slot, J. W., Geuze, H. J., Gigengack, S., James, D. E., and Lienhard, G. E. (1991) Proc. Natl. Acad. Sci. U. S. A. 88, 7815-7819
  3. Strauss, A. W., Powell, C. K., Hale, D. E., Anderson, M. M., Ahuja, A., Brackett, J. C., and Sims, H. F. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 10496 -10500

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Authors
Gimeno, R. E., Ortegon, A. M., Patel, S., Punreddy, S., Ge, P., Sun, Y., Lodish, H. F., & Stahl, A.
Affiliations
  • Palo Alto Medical Foundation (US)
  • Whitehead Institute for Biomedical Research (US)
  • Takeda Oncology (United States) (US)
Corresponding author
Stahl, Andreas
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2003-05
Volume
278
Issue
18
Pages
16039-16044
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1992956691
Cited by
218
References
0
Citations by year
2026: 7 · 2025: 7 · 2024: 5 · 2023: 13 · 2022: 12 · 2021: 5 · 2020: 6 · 2019: 8 · 2018: 5 · 2017: 8 · 2016: 6 · 2015: 8 · 2014: 5 · 2013: 11 · 2012: 10
FWCI
4.42
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • American Heart Association
  • University of Pittsburgh
  • National Institutes of Health
  • Medical Center, University of Pittsburgh
  • National Heart, Lung, and Blood Institute (HL41484, P01HL041484)
  • National Institute of Diabetes and Digestive and Kidney Diseases (DK 47618)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Peroxisome Proliferator-Activated Receptors
Keywords
fatty acid transporters, long-chain fatty acid uptake, cardiomyocytes, sarcolemma, CD36, subcellular localization, gene expression patterns, lipid metabolism, heart disease, diabetes mellitus
MeSH terms
Carrier Proteins, Cell Membrane, Chromosome Mapping, Cloning, Molecular, Fatty Acids, Humans, Membrane Proteins, Myocardium, Membrane Transport Proteins, Myocytes, Cardiac, Fatty Acid Transport Proteins

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