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Gene Review

Iapp  -  islet amyloid polypeptide

Mus musculus

Synonyms: Amylin, DAP, Diabetes-associated peptide, Islet amyloid polypeptide, amylin
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Disease relevance of Iapp


Psychiatry related information on Iapp

  • Peripherally secreted amylin may play a role in the amnesia seen in diabetes and the memory enhancement following glucose administration [6].

High impact information on Iapp


Chemical compound and disease context of Iapp


Biological context of Iapp

  • Here we show that Amylin inactivation leads to a low bone mass due to an increase in bone resorption, whereas bone formation is unaffected [1].
  • Recently, a high affinity amylin binding site was identified in the mouse alpha-TSH thyrotroph cell line [9].
  • The current data demonstrate expression of two biochemically distinct receptor phenotypes in mouse alpha-TSH cells, a CT receptor phenotype and an amylin receptor phenotype that have highly similar protein backbones [9].
  • In cross-linking studies, 125I-rat amylin and 125I-CGRP specifically labeled a major band of relative molecular mass (Mr) approximately 80K, being approximately 10 kDa higher than the major 125I-sCT binding protein [9].
  • Therefore, we conclude (1) that the homologous amino acid sequence within IAPP and CGRP does not seem to be sufficient for inducing inhibition of insulin release in mice and rats and (2) that the possible involvement of IAPP in the pathogenesis of diabetes type 2 still remains speculative [10].

Anatomical context of Iapp


Associations of Iapp with chemical compounds


Physical interactions of Iapp


Regulatory relationships of Iapp


Other interactions of Iapp

  • Although Amylin +/- mice like Amylin-deficient mice display a low bone mass phenotype and increased bone resorption, Calcr +/- mice display a high bone mass due to an increase in bone formation [1].
  • These islets contained not only fully processed IAPP as in PC1/3(+/+) islets, but also elevated levels of a COOH-terminally unprocessed intermediate form, suggesting impaired processing at the COOH-terminus [21].
  • Coexpression of proIAPP and PC2 resulted in production of mature IAPP, whereas in cells that coexpressed proIAPP and PC1/3 only a 6-kDa intermediate was produced [21].
  • Gastrin infusion increased gastric IAPP but not PYY expression [22].
  • Role of carboxypeptidase E in processing of pro-islet amyloid polypeptide in {beta}-cells [23].

Analytical, diagnostic and therapeutic context of Iapp


  1. Amylin inhibits bone resorption while the calcitonin receptor controls bone formation in vivo. Dacquin, R., Davey, R.A., Laplace, C., Levasseur, R., Morris, H.A., Goldring, S.R., Gebre-Medhin, S., Galson, D.L., Zajac, J.D., Karsenty, G. J. Cell Biol. (2004) [Pubmed]
  2. Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide. Janson, J., Soeller, W.C., Roche, P.C., Nelson, R.T., Torchia, A.J., Kreutter, D.K., Butler, P.C. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  3. Induction of insulin and islet amyloid polypeptide production in pancreatic islet glucagonoma cells by insulin promoter factor 1. Serup, P., Jensen, J., Andersen, F.G., Jørgensen, M.C., Blume, N., Holst, J.J., Madsen, O.D. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  4. Islet amyloid polypeptide (amylin)-deficient mice develop a more severe form of alloxan-induced diabetes. Mulder, H., Gebre-Medhin, S., Betsholtz, C., Sundler, F., Ahrén, B. Am. J. Physiol. Endocrinol. Metab. (2000) [Pubmed]
  5. Immunochemical investigation of insulinomas for islet amyloid polypeptide and insulin: evidence for differential synthesis and storage. Williams, A.J., Coates, P.J., Lowe, D.G., McLean, C., Gale, E.A. Histopathology (1992) [Pubmed]
  6. Differential effects of amylin on memory processing using peripheral and central routes of administration. Flood, J.F., Morley, J.E. Peptides (1992) [Pubmed]
  7. Amylin, released from the gastric fundus, stimulates somatostatin and thus inhibits histamine and acid secretion in mice. Zaki, M., Koduru, S., McCuen, R., Vuyyuru, L., Schubert, M.L. Gastroenterology (2002) [Pubmed]
  8. The expression of Escherichia coli diaminopimelate decarboxylase in mouse 3T3 cells. Saqib, K.M., Hay, S.M., Rees, W.D. Biochim. Biophys. Acta (1994) [Pubmed]
  9. Characterization of amylin and calcitonin receptor binding in the mouse alpha-thyroid-stimulating hormone thyrotroph cell line. Perry, K.J., Quiza, M., Myers, D.E., Morfis, M., Christopoulos, G., Sexton, P.M. Endocrinology (1997) [Pubmed]
  10. Failure of islet amyloid polypeptide to inhibit basal and glucose-stimulated insulin secretion in model experiments in mice and rats. Pettersson, M., Ahrén, B. Acta Physiol. Scand. (1990) [Pubmed]
  11. Reduced nociceptive behavior in islet amyloid polypeptide (amylin) knockout mice. Gebre-Medhin, S., Mulder, H., Zhang, Y., Sundler, F., Betsholtz, C. Brain Res. Mol. Brain Res. (1998) [Pubmed]
  12. Islet amyloid polypeptide-like immunoreactivity in the islet B cells of type 2 (non-insulin-dependent) diabetic and non-diabetic individuals. Westermark, P., Wilander, E., Westermark, G.T., Johnson, K.H. Diabetologia (1987) [Pubmed]
  13. Amylin and adrenomedullin: novel regulators of bone growth. Cornish, J., Naot, D. Curr. Pharm. Des. (2002) [Pubmed]
  14. Modulation of food intake by peripherally administered amylin. Morley, J.E., Flood, J.F., Horowitz, M., Morley, P.M., Walter, M.J. Am. J. Physiol. (1994) [Pubmed]
  15. Mutation at position -132 in the islet amyloid polypeptide ( IAPP) gene promoter enhances basal transcriptional activity through a new CRE-like binding site. Novials, A., Mato, E., Lucas, M., Franco, C., Rivas, M., Santisteban, P., Gomis, R. Diabetologia (2004) [Pubmed]
  16. Transcription factor occupancy of the insulin gene in vivo. Evidence for direct regulation by Nkx2.2. Cissell, M.A., Zhao, L., Sussel, L., Henderson, E., Stein, R. J. Biol. Chem. (2003) [Pubmed]
  17. Binding sites for islet amyloid polypeptide in mammalian lung: species variation and effects on adenylyl cyclase. Bhogal, R., Smith, D.M., Owji, A.A., Bloom, S.R. Can. J. Physiol. Pharmacol. (1995) [Pubmed]
  18. Amylin and food intake in mice: effects on motivation to eat and mechanism of action. Morley, J.E., Suarez, M.D., Mattamal, M., Flood, J.F. Pharmacol. Biochem. Behav. (1997) [Pubmed]
  19. Inhibition of food intake. Young, A. Adv. Pharmacol. (2005) [Pubmed]
  20. Islet amyloid polypeptide inhibits glucagon release and exerts a dual action on insulin release from isolated islets. Akesson, B., Panagiotidis, G., Westermark, P., Lundquist, I. Regul. Pept. (2003) [Pubmed]
  21. Role of beta-cell prohormone convertase (PC)1/3 in processing of pro-islet amyloid polypeptide. Marzban, L., Trigo-Gonzalez, G., Zhu, X., Rhodes, C.J., Halban, P.A., Steiner, D.F., Verchere, C.B. Diabetes (2004) [Pubmed]
  22. Reduced ghrelin, islet amyloid polypeptide, and peptide YY expression in the stomach of gastrin-cholecystokinin knockout mice. Friis-Hansen, L., Wierup, N., Rehfeld, J.F., Sundler, F. Endocrinology (2005) [Pubmed]
  23. Role of carboxypeptidase E in processing of pro-islet amyloid polypeptide in {beta}-cells. Marzban, L., Soukhatcheva, G., Verchere, C.B. Endocrinology (2005) [Pubmed]
  24. Salmon calcitonin - a potent inhibitor of food intake in states of impaired leptin signalling in laboratory rodents. Eiden, S., Daniel, C., Steinbrueck, A., Schmidt, I., Simon, E. J. Physiol. (Lond.) (2002) [Pubmed]
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