Rat amylin: Cloning and tissue-specific expression in pancreatic islets

J. D. Leffert, C. B. Newgard, H. Okamoto, J. L. Milburn, K. L. Luskey

Research output: Contribution to journalArticlepeer-review

142 Citations (Scopus)


Amyloid deposits in the islets of Langerhans of the pancreas are a common finding in non-insulin-dependent diabetes mellitus. The main protein constituent of these deposits is a 37-amino acid peptide known as amylin that resembles calcitonin gene-related peptide, a neuropeptide. We have isolated cDN clones corresponding to the rat amylin precursor from an islet cDNA library and we show that this peptide is encoded in a 0.9-kilobase mRNA that is translated to yield a 93-amino acid precursor. The amylin peptide is bordered by dibasic residues, suggesting that it is proteolyzed like calcitonin gene-related peptide. The peptide sequences flanking the amylin sequence do not resemble the calcitonin gene-related peptide flanking sequences. RNA hybridization studies show that amylin mRNA is abundant in the islets of Langerhans but is not present in the brain or seven other tissues examined. Dietary changes, such as fasting or fasting and refeeding, have little effect on amylin mRNA expression. This tissue specificity suggests that amylin is involved in specific signaling pathways related to islet function.

Original languageEnglish
Pages (from-to)3127-3130
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number9
Publication statusPublished - 1989


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