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Distinguishing Biochemical Activities of Splice Variants of Human FATP2
Author(s) -
Melton Elaina Marie,
AriasBarrau Elsa,
Srinivasan Padmamalini,
DiRusso Concetta C.,
Black Paul N.
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.691.2
Subject(s) - biochemistry , splice , adenylate kinase , gene isoform , intron , chemistry , exon , gene , biology , microbiology and biotechnology , enzyme
Fatty acid transport proteins (FATPs) represent a family of integral membrane proteins, which function in transport and activation of exogenous fatty acids (FA). Splice variants of human FATP2 have been identified that differ in the ATP binding region, which is required for adenylate formation. FATP2a contains the entire ATP/AMP motif while FATP2b lacks exon 3 resulting in a protein lacking critical residues within this motif. Using T‐REx 293 cells expressing FATP2a or FATP2b, we have [1] defined their individual roles in long chain FA transport and long and very long chain FA activation and [2] initiated studies addressing whether they direct specific classes of exogenous FA into downstream acyl CoA pools using stable isotopically labeled FA and high resolution mass spectroscopy. Our current data is consistent with the postulate that FATP2a activates exogenous very long‐chain FA via vectorial acylation. FATP2a is able to activate the very long chain FA, lignoceric acid (C24:0), while FATP2b is devoid of this activity. Expression of both FATP2a and FATP2b, however increase the import of the fluorescent long‐chain FA C 1 ‐BODIPY‐C 12 , which indicates probable interaction with an unknown long chain acyl CoA synthetase. These findings are consistent with the hypothesis that different FATP isoforms function in the trafficking of specific classes of very long chain FA. [Supported by NIH grants: GM056840 and DK071076].