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pubmed-article:11587069pubmed:abstractTextGlutamine:fructose-6-phosphate amidotransferase (GFAT1) is the rate-limiting enzyme in the hexosamine biosynthetic pathway, which plays an important role in hyperglycemia-induced insulin resistance. To evaluate the role of GFAT1 expression, we analyzed the expression profiles of GFAT1 mRNA in various human tissues using reverse transcriptase-polymerase chain reaction. We report here the identification and cDNA cloning of a novel GFAT1 splice variant expressed abundantly in skeletal muscle and heart. This subtype, designated GFAT1-L, contains a 54-bp insertion within the GFAT1 coding sequence. Recombinant GFAT1-L protein possessed functional GFAT activities and biochemical characteristics similar to GFAT1. Previously, GFAT1 was considered a simplex enzyme. The identification of a novel GFAT1 subtype possessing functional enzymatic activity and tissue-specific expression should provide additional insight into the mechanism of skeletal muscle insulin resistance and diabetes complications.lld:pubmed
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pubmed-article:11587069pubmed:dateRevised2004-11-17lld:pubmed
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pubmed-article:11587069pubmed:articleTitleIdentification of GFAT1-L, a novel splice variant of human glutamine: fructose-6-phosphate amidotransferase (GFAT1) that is expressed abundantly in skeletal muscle.lld:pubmed
pubmed-article:11587069pubmed:affiliationOtsuka GEN Research Institute, Otsuka Pharmaceutical Co., Ltd., Tokushima, Japan.lld:pubmed
pubmed-article:11587069pubmed:publicationTypeJournal Articlelld:pubmed
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