1996 Fiscal Year Final Research Report Summary
Regulation of glycolysis by a novel brain-type isozyme of fructose 6-phosphate 2kinase/fructose 2,6-bisphosphatase
| Project/Area Number |
07670157
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
General medical chemistry
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| Research Institution | OSAKA MEDICAL SCHOOL |
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Principal Investigator |
WATANABE Fusao OSAKA MEDICAL SCHOOL,DEPARTMENT OF CHEMISTRY ; ASSOCIATE PRPFESSOR, 教養部, 講師 (40183719)
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| Project Period (FY) |
1995 – 1996
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| Keywords | glycolysis / fructose 2,6 bisphospate / brain / fructose 6-phosphate 2-kinase / fructose 2,6-bisphosphatase / alternative splicing |
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| Research Abstract |
Fructose 6-phospate, 2-kinase/fructose 2,6-bisphosphatase catalyzes the synthesis and degradation of fructose 2,6-bisphosphate, which is the most potent activator of glycolysis. We have shown previouslt the occurrence of a partial cDNA (RB7) encoding the catalytic core domain of a novel brain type isozyme. To elucidate the full-length sequence of RB7 cDNA,we have carried out cDNA cloning using 3'- and 5'- rapid amplification cDNA ends method and have isolated eight isoforms from rat brain. The cDNA sequences encoding the 5'-untranslated region, the amino-terminal domain, and the catalytic core domain were identical among all th isoforms. However, heterogeneity of the carboxyl-terminus was found by sequence analysis. This heterogeneity was shown not to have resulted from transcription of multiple genes, as Southern blot and genomic sequence analysis revealed that the gene was a single copy in the rat genome. It is likely that these transcripts represent splice variants of the gene. High-level expression of the gene was also observed northern blot analysis in skeletal muscle. However, the pattern of alternative splicing was different from that of brain, and only four isoforms were detected in skeletal muscle.
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