Regulation of mitochondrial and microsmal phospholipid synthesis by liver fatty acid-binding protein

Recently we have detected and partially purified a 15-kDa cytosolic L- alpha -lysophosphatidic acid (LPA)-binding protein (LPABP), which stimulates export of LPA from mitochondria. Now we have purified this protein to homogeneity. By Western immunoblot analysis, amino acid sequence analysis, and bin...

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Bibliographic Details
Published in:The Journal of biological chemistry 1992-07, Vol.267 (20), p.14353-14359
Main Authors: VANCURA, A, HALDAR, D
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Binding and carrier proteins
Biological and medical sciences
biosynthesis
fatty acid-binding protein
Fundamental and applied biological sciences. Psychology
liver
microsomes
mitochondria
phospholipids
Proteins
rats
regulation
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Summary:Recently we have detected and partially purified a 15-kDa cytosolic L- alpha -lysophosphatidic acid (LPA)-binding protein (LPABP), which stimulates export of LPA from mitochondria. Now we have purified this protein to homogeneity. By Western immunoblot analysis, amino acid sequence analysis, and binding characteristics we have shown that LPABP is identical with liver fatty acid-binding protein (L-FABP). This protein binds LPA, and stimulates mitochondrial and microsomal glycerophosphate acyltransferase (GAT) and the export of LPA from both the organelles. The mitochondrially synthesized LPA exported by L-FABP can be converted to phosphatidic acid by microsomes. L-FABP also stimulates microsomal conversion of LPA to phosphatidic acid but strongly inhibits this reaction in mitochondria. However, in the absence of L-FABP mitochondria predominantly synthesize PA.
ISSN:0021-9258
1083-351X