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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0017797,
umls-concept:C0020792,
umls-concept:C0060775,
umls-concept:C0086418,
umls-concept:C0205314,
umls-concept:C0205419,
umls-concept:C0242692,
umls-concept:C0679622,
umls-concept:C1171362,
umls-concept:C1415046,
umls-concept:C1515670
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pubmed:issue |
10
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pubmed:dateCreated |
2001-10-5
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pubmed:abstractText |
Glutamine: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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1434-5161
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pubmed:author |
pubmed-author:BanTT,
pubmed-author:FujiwaraTT,
pubmed-author:FukuiHH,
pubmed-author:KamanJJ,
pubmed-author:KyushikiHH,
pubmed-author:NiimiMM,
pubmed-author:OgawaraTT,
pubmed-author:OkamotoTT,
pubmed-author:OzakiKK,
pubmed-author:TakahashiE IEI,
pubmed-author:TamanoiHH,
pubmed-author:TanigamiAA,
pubmed-author:UeyamaAA,
pubmed-author:YamamotoYY,
pubmed-author:YamashitaTT
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pubmed:issnType |
Print
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pubmed:volume |
46
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pubmed:owner |
NLM
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|
pubmed:authorsComplete |
Y
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pubmed:pagination |
566-71
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:11587069-Alternative Splicing,
pubmed-meshheading:11587069-Base Sequence,
pubmed-meshheading:11587069-Cloning, Molecular,
pubmed-meshheading:11587069-DNA, Complementary,
pubmed-meshheading:11587069-Escherichia coli,
pubmed-meshheading:11587069-Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing),
pubmed-meshheading:11587069-Humans,
pubmed-meshheading:11587069-Kinetics,
pubmed-meshheading:11587069-Molecular Sequence Data,
pubmed-meshheading:11587069-Muscle, Skeletal,
pubmed-meshheading:11587069-Polymerase Chain Reaction,
pubmed-meshheading:11587069-Protein Isoforms,
pubmed-meshheading:11587069-RNA, Messenger,
pubmed-meshheading:11587069-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:11587069-Sequence Homology, Nucleic Acid,
pubmed-meshheading:11587069-Tissue Distribution
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pubmed:year |
2001
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pubmed:articleTitle |
Identification of GFAT1-L, a novel splice variant of human glutamine: fructose-6-phosphate amidotransferase (GFAT1) that is expressed abundantly in skeletal muscle.
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pubmed:affiliation |
Otsuka GEN Research Institute, Otsuka Pharmaceutical Co., Ltd., Tokushima, Japan.
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pubmed:publicationType |
Journal Article
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