This Article Order Full text via Infotrieve Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Westermark, P. Articles by Johnson, K. H. Search for Related Content PubMed PubMed Citation Articles by Westermark, P. Articles by Johnson, K. H.

American Journal of Pathology, Vol 127, 414-417, Copyright © 1987 by American Society for Investigative Pathology

REGULAR ARTICLES

Islet amyloid in type 2 human diabetes mellitus and adult diabetic cats contains a novel putative polypeptide hormone

P Westermark, C Wernstedt, TD O'Brien, DW Hayden and KH Johnson

Amyloid deposition is a very typical alteration in the islets of Langerhans in human Type 2 (non-insulin-dependent) diabetes mellitus and in feline diabetes mellitus. Amyloid infiltration is also commonly found in insulin-producing pancreatic tumors. It was shown recently that amyloid purified from an insulinoma was composed mainly of a novel polypeptide (insulinoma amyloid polypeptide, IAPP), which had partial identity with the neuropeptide calcitonin gene-related peptide (CGRP). Cat islet amyloid contained a similar polypeptide. This finding is verified in the present study, and it is shown that the cat IAPP differs from the human peptide only in two of the 16 elucidated amino acid residues. The authors now also show by N-terminal amino acid sequence analysis that human islet amyloid is of IAPP origin. Although the significance of IAPP is unknown, its occurrence in pancreatic endocrine tissue and partial identity with a known neuropeptide suggests an endocrine regulatory function.

This article has been cited by other articles:

				L. Haataja, T. Gurlo, C. J. Huang, and P. C. Butler Islet Amyloid in Type 2 Diabetes, and the Toxic Oligomer Hypothesis Endocr. Rev., May 1, 2008; 29(3): 303 - 316. [Abstract] [Full Text] [PDF]

				M. Fry, T. D. Hoyda, and A. V. Ferguson Making Sense of It: Roles of the Sensory Circumventricular Organs in Feeding and Regulation of Energy Homeostasis Experimental Biology and Medicine, January 1, 2007; 232(1): 14 - 26. [Abstract] [Full Text] [PDF]

				C. Wu, H. Lei, Z. Wang, W. Zhang, and Y. Duan Phenol Red Interacts with the Protofibril-Like Oligomers of an Amyloidogenic Hexapeptide NFGAIL through Both Hydrophobic and Aromatic Contacts Biophys. J., November 15, 2006; 91(10): 3664 - 3672. [Abstract] [Full Text] [PDF]

				C. Lin Chang, J. Roh, J.-I. Park, C. Klein, N. Cushman, R. V. Haberberger, and S. Y. T. Hsu Intermedin Functions as a Pituitary Paracrine Factor Regulating Prolactin Release Mol. Endocrinol., November 1, 2005; 19(11): 2824 - 2838. [Abstract] [Full Text] [PDF]

				C. Wu, H. Lei, and Y. Duan The Role of Phe in the Formation of Well-Ordered Oligomers of Amyloidogenic Hexapeptide (NFGAIL) Observed in Molecular Dynamics Simulations with Explicit Solvent Biophys. J., April 1, 2005; 88(4): 2897 - 2906. [Abstract] [Full Text] [PDF]

				O. Schmitz, B. Brock, and J. Rungby Amylin Agonists: A Novel Approach in the Treatment of Diabetes Diabetes, December 1, 2004; 53(suppl_3): S233 - S238. [Abstract] [Full Text] [PDF]

				S. A. Jayasinghe and R. Langen Identifying Structural Features of Fibrillar Islet Amyloid Polypeptide Using Site-directed Spin Labeling J. Biol. Chem., November 12, 2004; 279(46): 48420 - 48425. [Abstract] [Full Text] [PDF]

				C. Wu, H. Lei, and Y. Duan Formation of Partially Ordered Oligomers of Amyloidogenic Hexapeptide (NFGAIL) in Aqueous Solution Observed in Molecular Dynamics Simulations Biophys. J., November 1, 2004; 87(5): 3000 - 3009. [Abstract] [Full Text] [PDF]

				R. D. Reidelberger, A. C. Haver, U. Arnelo, D. D. Smith, C. S. Schaffert, and J. Permert Amylin receptor blockade stimulates food intake in rats Am J Physiol Regulatory Integrative Comp Physiol, September 1, 2004; 287(3): R568 - R574. [Abstract] [Full Text] [PDF]

				S. D. Brain and A. D. Grant Vascular Actions of Calcitonin Gene-Related Peptide and Adrenomedullin Physiol Rev, July 1, 2004; 84(3): 903 - 934. [Abstract] [Full Text] [PDF]

				H. T. Blumenthal Amyloidosis: A Universal Disease of Aging? J. Gerontol. A Biol. Sci. Med. Sci., April 1, 2004; 59(4): M361 - M369. [Full Text] [PDF]

				R. Dacquin, R. A. Davey, C. Laplace, R. Levasseur, H. A. Morris, S. R. Goldring, S. Gebre-Medhin, D. L. Galson, J. D. Zajac, and G. Karsenty Amylin inhibits bone resorption while the calcitonin receptor controls bone formation in vivo J. Cell Biol., February 16, 2004; 164(4): 509 - 514. [Abstract] [Full Text] [PDF]

				M. Hoenig, G. Hall, D. Ferguson, K. Jordan, M. Henson, K. Johnson, and T. O'Brien A Feline Model of Experimentally Induced Islet Amyloidosis Am. J. Pathol., December 1, 2000; 157(6): 2143 - 2150. [Abstract] [Full Text] [PDF]

				J. E. Dimsdale, O. Kolterman, J. Koda, and R. Nelesen Effect of Race and Hypertension on Plasma Amylin Concentrations Hypertension, June 1, 1996; 27(6): 1273 - 1276. [Abstract] [Full Text]

				K. Park and C. B. Verchere Identification of a Heparin Binding Domain in the N-terminal Cleavage Site of Pro-islet Amyloid Polypeptide. IMPLICATIONS FOR ISLET AMYLOID FORMATION J. Biol. Chem., May 11, 2001; 276(20): 16611 - 16616. [Abstract] [Full Text] [PDF]

				R. Azriel and E. Gazit Analysis of the Minimal Amyloid-forming Fragment of the Islet Amyloid Polypeptide. AN EXPERIMENTAL SUPPORT FOR THE KEY ROLE OF THE PHENYLALANINE RESIDUE IN AMYLOID FORMATION J. Biol. Chem., August 31, 2001; 276(36): 34156 - 34161. [Abstract] [Full Text] [PDF]