Premium
Identification of Two Splice Variants of Human FATP2, Which Distinguish Fatty Acid Transport and Activation Activities
Author(s) -
Melton Elaina Marie,
Watkins Paul,
Jia Zhenzhen,
DiRusso Concetta C.,
Black Paul N.
Publication year - 2007
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.21.5.a236-a
Subject(s) - biochemistry , fatty acid , chemistry , splice , alternative splicing , biology , exon , gene
Fatty acid transport proteins (FATP) are involved in the vectorial movement and activation of fatty acids. In the context of fatty acid transport, these proteins may work alone or in conjunction with a cognate long chain acyl CoA synthetase. We have identified two splice variants of human FATP2, which have distinguishing biochemical activities. hsFATP2a contains the entire ATP/AMP motif, which has been shown to contribute to fatty acid activation; hsFATP2b lacks exon 3 resulting in a protein lacking part of the ATP/AMP motif. When expressed in humanized yeast deficient in fatty acid transport and activation, both forms of FATP2 were proficient in the transport of the fluorescent long chain fatty acid C 1 ‐BODIPY‐C 12 . When evaluated for ability to activate very long chain fatty acids, only hsFATP2a provided that function. These natural splice variants demonstrate the fatty acid transport and activation functions intrinsic to this family of proteins are distinguishable. Both forms of FATP2 have been subcloned into pcDNA4/TO/myc‐His‐A and transfected into 293 T‐REx cells, which allows regulated expression using tetracycline. The expression of hsFATP2a and 2b were varied in concert with changes in the concentration of tetracycline. Expression and characterization of hsFATP2a and 2b in 293 T‐REx cells are providing insights into their differential biological roles in lipid homeostasis. Supported by NIH grant RO1‐GM56850.