Summary
An immunohistochemical study for islet amyloid polypeptide (IAPP) was made on the gastrointestinal (GI) tract and pancreas of man and rat, using antisera raised against a synthetic peptide of C-terminal human IAPP (24–37) and a synthetic peptide of rat IAPP (18–37). A large number of IAPP-immunoreactive cells were found in the pyloric antrum, and a small number in the body of the stomach in both man and rat. Cytoplasmic processes extended out from the bipolar peripheral region of the immunoreactive cells, rather like neuronal processes, and some appeared to make contact with other immunoreactive cells. In addition, small numbers of immunoreactive cells were also seen in the duodenum and rectum, whereas they were absent from the jejunum, ileum and large intestine. An examination was made for evidence of colocalization of IAPP-immunoreactive material with material immunoreactive for gastrin, somatostatin, vasoactive intestinal polypeptide, pancreatic polypeptide, insulin, and glucagon, but none was found. IAPP-immunoreactive cells were also found in the pancreas of non-diabetic and non-insulin-dependent diabetic patients, but they were completely absent from a patient with insulin-dependent diabetes mellitus despite the presence of IAPP in the plasma. The results of these studies suggest that the peptide may have a biological role in situ in the GI tract and, in addition to the pancreas, may be a possible source of plasma IAPP.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Buchan AJ, Polak JM (1980) The classification of the human gastroenteropancreatic endocrine cells. Invest Cell Pathol 3:51–71
Clark A, Cooper GJS, Lewis CE, Morris JF, Willis AC, Reid KBM, Turner RC (1987) Islet amyloid formed from diabetes-associated peptide may be pathogenic in type 2 diabetes. Lancet II:231–234
Cooper GJS, Willis AC, Clarks A, Turner RC, Sim RB, Reid KBM (1987) Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patient. Proc Natl Acad Sci USA 84:8628–8632
Cooper JGS, Leighton B, Dimitriadis GD, Parry-Billings M, Kowalchuk JM, Howland K, Rothbard JB, Willis AC, Reid KBM (1988) Amylin found in amyloid deposits in human type 2 diabetes mellitus may be a hormone that regulates glycogen metabolism in skeletal muscle. Proc Natl Acad Sci USA 85:7763–7766
Datta HK, Zaidi M, Wimalawansa SJ, Ghatei MA, Beecham JL, Bloom SR, MacIntyre I (1989) In vivo and in vitro effects of amylin and amylin-amide on calcium metabolism in the rat and rabbit. Biochem Biophys Res Commun 162:876–881
Ferrier GJM, Pierson AM, Jones PM, Bloom SR, Girgis SI, Legon S (1989) Expression of the rat amylin (IAPP/DAP) gene. J Mol Endocrinol 3:R1-R4
Kogire M, Chang JK, Thonpson JC, Greeley GH Jr (1989) Inhibitory action of diabetes-associated peptide and calcitonin gene-related peptide on insulin release. 71th Annual meeting of the endocrine society. Abstract p 55
Leighton B, Cooper GJS (1988) Pancreatic amylin and calcitonin gene-related peptide cause resistance to insulin in skeletal muscle in vitro. Nature 335:632–635
Lukinius A, Wilander E, Westermark GT, Engstrom U, Westermark P (1989) Co-localization of islet amyloid polypeptide and insulin in the B cell secretory granules of the human pancreatic islets. Diabetologia 32:240–244
Nakazato M, Asai J, Kangawa K, Matsukura S, Matsuo H (1989) Establishment of radioimmunoassay for human islet amyloid polypeptide and tissue content and plasma concentration. Biochem Biophys Res Commun 162:876–881
National Diabetes Group (1979) Classification and diagnosis of diabetes mellitus and categories of glucose intolerance. Diabetes 28:1039–1052
Nishi M, Chan JC, Nagamatsu S, Bell GI, Steiner DF (1989) Conservation of the sequence of islet amyloid polypeptide in five mammals is consistent with its putative role as an islet hormone. Proc Natl Acad Sci USA 86:5738–5742
Osawa H, Kanatsuka A, Yamaguchi T, Makino H, Yoshida S (1989) Islet amyloid polypeptide inhbits glucose-stimulated insulin secretion from isolated rat pancreatic islets. Biochem Biophys Res Commun 160:961–967
Sanke T, Bell GI, Sample C, Rubenstein AH, Steiner DF (1988) An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing. J Biol Chem 263:17243–17246
Toshimori H, Toshimori K, Ohura C, Matsuo H, Matsukura S (1988) The distribution of atrial natriuretic polypeptide (ANP)-containing cells in the adult rat heart. Anat Embryol 177:477–484
Westermark P, Wernstedt C, Wilander E, Hayden DW, O'Brien T, Johnson KH (1987a) Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc Natl Acad Sci USA 84:3881–3885
Westermark P, Wernstedt C, Wilander E, O'Brien T, Hayden DW, Johnson KH (1987b) Islet amyloid in type 2 human diabetes mellitus and adult diabetic cats contains a novel putative polypeptide hormone. Am J Pathol 127:414–417
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Toshimori, H., Narita, R., Nakazato, M. et al. Islet amyloid polypeptide (IAPP) in the gastrointestinal tract and pancreas of man and rat. Cell Tissue Res 262, 401–406 (1990). https://doi.org/10.1007/BF00305236
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00305236