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Journal Article•DOI•

Relationship between glycerol-3-phosphate dehydrogenase, fatty acid synthase and fatty acid binding proteins in developing human placenta

Anup K Bandyopadhyay1, Tanya Das1, Gouri Sankar Sa1, Manju Mukherjea1•
University of Calcutta1
01 Jun 1995-Journal of Biosciences (Springer India)-Vol. 20, Iss: 2, pp 141-149
TL;DR: A correlation exists between glycerol-3-phosphate dehydrogenase, fatty acid synthase and fatty acid binding proteins in developing human placenta with the advancement of pregnancy when more lipids are required for the developingPlacenta.
Abstract: The activities of the enzymes glycerol-3-phosphate dehydrogenase and fatty acid synthase are inhibited by palmitoyl-coenzyme A and oleate. The two isoforms of fatty acid binding proteins (PI 6.9 and PI 5.4) enhance the activities of glycerol-3-phosphate dehydrogenase and fatty acid synthase in the absence of palmitoyl-coenzyme A or oleate and also protect them against palmitoyl-coenzyme A or oleate inhibition. Levels of fatty acid binding proteins, the activities of the enzymes fatty acid synthase and glycerol-3-phosphate dehydrogenase increase with gestation showing a peak at term. However, the activity of fatty acid synthase showed the same trend up to the 30th week of gestation and then declined slightly at term. With the advancement of pregnancy when more lipids are required for the developing placenta, fatty acid binding proteins supply more fatty acids and glycerol-3-phosphate for the synthesis of lipids. Thus a correlation exists between glycerol-3-phosphate dehydrogenase, fatty acid synthase and fatty acid binding proteins in developing human placenta.
References
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"Relationship between glycerol-3-pho..." refers methods in this paper

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Journal Article•DOI•
Structural and functional features of different types of cytoplasmic fatty acid-binding proteins

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J.H. Veerkamp1, Roger A. Peeters1, R.G.H.J. Maatman1•
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04 Jan 1991-Biochimica et Biophysica Acta
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366 citations

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Journal Article•DOI•
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Journal Article•DOI•
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David A. Sweetser, Robert O. Heuckeroth, Jeffrey I. Gordon
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Journal Article•DOI•
Functions of fatty acid binding proteins.

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R. M. Kaikaus1, Nathan M. Bass1, Robert K. Ockner1•
University of California, San Francisco1
15 Jun 1990-Cellular and Molecular Life Sciences
TL;DR: A considerable body of indirect evidence is provided supporting a broad role for the FABP in the intracellular transport and metabolism of long-chain fatty acids and the existence of structure- and tissue-specific specialization of function among different members of the F ABP gene family.
Abstract: Cytosolic fatty acid binding proteins (FABP) belong to a gene family of which eight members have been conclusively identified. These 14–15 kDa proteins are abundantly expressed in a highly tissue-specific manner. Although the functions of the cytosolic FABP are not clearly established, they appear to enhance the transfer of long-chain fatty acids between artificial and native lipid membranes, and also to have a stimulatory effect on a number of enzymes of fatty acid metabolism in vitro. These findings, as well as the tissue expression, ligand binding properties, ontogeny and regulation of these proteins provide a considerable body of indirect evidence supporting a broad role for the FABP in the intracellular transport and metabolism of long-chain fatty acids. The available data also support the existence of structure- and tissue-specific specialization of function among different members of the FABP gene family. Moreover, FABP may also have a possible role in the modulation of cell growth and proliferation, possibly by virtue of their affinity for ligands such as prostaglandins, leukotrienes and fatty acids, which are known to influence cell growth activity. FABP structurally unrelated to the cytosolic gene family have also been identified in the plasma membranes of several tissues (FABPpm). These proteins have not been fully characterized to date, but strong evidence suggests that they function in the transport of long-chain fatty acids across the plasma membrane.

167 citations

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  • ...FABPs bind appreciable amounts fatty acids and their CoA esters and thus create a readily available intracellular pool of these substances (Spener and Mukherjea 1990; Kaikaus et al 1990)....

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