Isolation and partial characterization of plasma membrane fatty acid binding proteins from myocardium and adipose tissue and their relationship to analogous proteins in liver and gut

Potter, BJ; Stump, Decherd; Schwieterman, William D.; Sorrentino, Dario; Ln, Jacobs; Cl, Kiang; Rand, JH; Pd, Berk

doi:10.1016/s0006-291x(87)80283-8

Cited by 55 publications

(30 citation statements)

References 8 publications

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“…In mammalian tissues, FABP pm was originally identified by Stremmel et al in rat liver (416) and jejunal microvilli (414), and later in adipose tissue (336,378) and cardiac myocytes (393,411), all of which are cells with high transmembrane fluxes of fatty acids. FABP pm is peripherally bound at the outer leaflet of the plasma membrane, as FABP pm from rat liver could be isolated by a high-ionic-strength medium (394).…”

Section: A Plasma Membrane Fatty Acid Binding Proteinmentioning

confidence: 99%

Membrane Fatty Acid Transporters as Regulators of Lipid Metabolism: Implications for Metabolic Disease

Glatz

Luiken

Bonen

2010

Physiological Reviews

622

662

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Long-chain fatty acids and lipids serve a wide variety of functions in mammalian homeostasis, particularly in the formation and dynamic properties of biological membranes and as fuels for energy production in tissues such as heart and skeletal muscle. On the other hand, long-chain fatty acid metabolites may exert toxic effects on cellular functions and cause cell injury. Therefore, fatty acid uptake into the cell and intracellular handling need to be carefully controlled. In the last few years, our knowledge of the regulation of cellular fatty acid uptake has dramatically increased. Notably, fatty acid uptake was found to occur by a mechanism that resembles that of cellular glucose uptake. Thus, following an acute stimulus, particularly insulin or muscle contraction, specific fatty acid transporters translocate from intracellular stores to the plasma membrane to facilitate fatty acid uptake, just as these same stimuli recruit glucose transporters to increase glucose uptake. This regulatory mechanism is important to clear lipids from the circulation postprandially and to rapidly facilitate substrate provision when the metabolic demands of heart and muscle are increased by contractile activity. Studies in both humans and animal models have implicated fatty acid transporters in the pathogenesis of diseases such as the progression of obesity to insulin resistance and type 2 diabetes. As a result, membrane fatty acid transporters are now being regarded as a promising therapeutic target to redirect lipid fluxes in the body in an organ-specific fashion.

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Section: A Plasma Membrane Fatty Acid Binding Proteinmentioning

confidence: 99%

Membrane Fatty Acid Transporters as Regulators of Lipid Metabolism: Implications for Metabolic Disease

Glatz

Luiken

Bonen

2010

Physiological Reviews

622

662

View full text Add to dashboard Cite

show abstract

“…A plasma membrane fatty acid binding protein (FABPpm) was purified by oleate-agarose affinity chromatography from hepatocytes, adipocytes, jejunal enterocytes, and cardiac myocytes and was proposed to play a role in fatty acid import (51,60,62). This protein shares amino acid identity with mitochondrial aspartate aminotransferase (mAspAT) (68), a protein synthesized on free polysomes in the cytosol, with an amino-terminal mitochondrial targeting sequence that is clipped after mitochondrial translocation.…”

Section: Proteins That Bind Fatty Acids At the Cell Surface Facilitatmentioning

confidence: 99%

Fatty acid transport: the roads taken

Schaffer

2002

American Journal of Physiology-Endocrinology and Metabolism

151

112

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Efficient uptake and channeling of long-chain fatty acids (LCFAs) are critical cellular functions. Although spontaneous flip-flop of nonionized LCFAs from one leaflet of a bilayer to the other is rapid, evidence is emerging that proteins are important mediators and/or regulators of trafficking of LCFAs into and within cells. Genetic screens have led to the identification of proteins that are required for fatty acid import and utilization in prokaryotic organisms. In addition, functional screens have elucidated proteins that facilitate fatty acid import into mammalian cells. Although the mechanisms by which these proteins mediate LCFA import are not well understood, studies in both prokaryotic and eukaryotic organisms provide compelling evidence that uptake of LCFAs across cellular membranes is coupled to esterification by acyl-CoA synthetases. This review will summarize results of studies of non-protein-mediated and protein-mediated LCFA transport and discuss how these different mechanisms may contribute to cellular metabolism.

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“…Membrane protein was measured by the biuret reaction (40). After SDS/PAGE-Western blotting and autoradiography (20), membrane proteins were quantitated by scanning densitometry as the area under the densitometric curve (OD x mm). Expression of FABPpm antigen on the surface of control and transfected 3T3 fibroblasts was determined with rabbit anti rat-FABPpm as the primary antibody and fluorescein isothiocyanate-conjugated goat anti-rabbit IgG for detection (14).…”

mentioning

confidence: 99%

3T3 fibroblasts transfected with a cDNA for mitochondrial aspartate aminotransferase express plasma membrane fatty acid-binding protein and saturable fatty acid uptake.

Isola

Zhou

Kiang

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

134

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Isolation and partial characterization of plasma membrane fatty acid binding proteins from myocardium and adipose tissue and their relationship to analogous proteins in liver and gut

Cited by 55 publications

References 8 publications

Membrane Fatty Acid Transporters as Regulators of Lipid Metabolism: Implications for Metabolic Disease

Membrane Fatty Acid Transporters as Regulators of Lipid Metabolism: Implications for Metabolic Disease

Fatty acid transport: the roads taken

3T3 fibroblasts transfected with a cDNA for mitochondrial aspartate aminotransferase express plasma membrane fatty acid-binding protein and saturable fatty acid uptake.

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