| Budget Amount *help |
¥6,600,000 (Direct Cost: ¥6,600,000)
Fiscal Year 1996: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 1995: ¥5,000,000 (Direct Cost: ¥5,000,000)
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| Research Abstract |
Amylin, also designated islet amyloid polypeptide, is a 37-amino acid peptide that was isolated from islet amyloid in 1987. The peptide is thought to be involved in the etiology of NIDDM by opposing insulin action in peripheral tissues and by destroying islet construction through amyloid deposition. We studied the properties of amylin, its synthesis and secretion in abnormal glucose tolerance, and amyloidogenesis of the islet in NIDDM.
We developed three RIAs for amylin : human and rat common N-terminal region of amylin, and both human and rat C-terminal amylin. We also identified endogenous molecular forms of amylin in pancreata, gastrointestinal tracts and plasma of many mammals. Amylin messenger RNA whose size is 900 bases is predminantly expressed in the pancreas. Amylin is detected in rat fetal pancreas, and its content gradually increases during development. Amylin in the antrum appears 3 days after birth. In the human pancreas, amylin is detected at 15 weeks of gestation. Pancreatic amylin content was 221.6<plus-minus>78.2 pmol/g wet weight in man and 328.5<plus-minus>25.0 pmol/g wet weight in rat, being approximately 1-2% of insulin content. Basal plasma immunoreactive amylin level in normal individuals was 2.4-5.8 fmol/ml, being increased in subjects with ovesity or impaired glucose tolerance, and decreased in diabetic patients. Amylin was co-secreted with insulin in physiological conditi
Islet amyloid deposition is not responsible for the primary etiology of NIDDM,however, the amyloid deposits could intensify islet dysfunction and contribute to the progression of NIDDM.
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