IAPP
Synonyms
DAP, Amylin, Insulinoma amyloid peptide, IAPP, Diabetes-Associated Peptide, Islet Amyloid Polypeptide (Diabetes-Associated Peptide, Amylin), IAP, Islet Amyloid Polypeptide, Islet Amyloid Polypeptide (Diabetes-Associated Peptide; Amylin)
Description
Islet amyloid polypeptide (IAPP), the main component of islet amyloid in type 2 diabetes and islet transplants, is now recognized as a contributor to beta cell dysfunction. It selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
KO Status
F0
Drug Information
Drugs in clinical trials: 3
Latest Research Phase: Phase 3 Clinical
Drug Name
Code
Phase
Company
Indications
Clinical Trials
Allogeneic human islets of Langerhans (University of Illinois)
Phase 3 Clinical
University Of Illinois
Diabetes Mellitus, Type 1
Nirogacestat
PF-3084014, PF-03084014
Phase 3 Clinical
Pfizer Inc
Fibromatosis, Aggressive, Solid tumours, Triple Negative Breast Neoplasms, Pancreatic Neoplasms, Multiple Myeloma, Breast Neoplasms, Alzheimer Disease
NCT Number
NCT03785964
NCT01981551
NCT02338531
NCT04195399
NCT02299635
NCT02109445
NCT01876251
NCT04722146
NCT00878189
NCT02462707
NCT02955446
Intervention Type
Drug
Drug
Procedure, Drug
Other, Drug
Drug
Drug
Drug
Drug
Drug
Drug
Drug
Indications
Desmoid Tumor; Aggressive Fibromatosis
Desmoid Tumors; Aggressive Fibromatosis
Breast Cancer
Desmoid-Type Fibromatosis; Recurrent Desmoid-Type Fibromatosis; Unresectable Desmoid-Type Fibromatosis
Triple Negative Breast Neoplasms
Metastatic Cancer Pancreas
Breast Cancer Metastatic
Multiple Myeloma
Neoplasms by Histologic Type
Advanced Solid Tumors
Neoplasm; Desmoid Tumor
Study Phase
Phase 3
Phase 2
Phase 2
Phase 2
Phase 2
Phase 2
Phase 1
Phase 1
Phase 1
Phase 1
N/A
Recruitment Status
Active, not recruiting
Active, not recruiting
Withdrawn
Recruiting
Terminated
Terminated
Terminated
Recruiting
Completed
Withdrawn
No longer available
Bisnorcymserine
ANVS-301
Phase 1 Clinical
Horizon Therapeutics Plc
Alzheimer Disease
NCT Number
NCT01747213
Intervention Type
Other, Drug
Indications
Healthy Volunteers
Study Phase
Phase 1
Recruitment Status
Completed
NI-203
NI-203
Preclinical
Neurimmune
Diabetes Mellitus, Type 2
Caprospinol
SP-08, SP-004, SP-008, SP-04m, SP-233, SP-04-Samaritan
Pending
Samaritan
Alzheimer Disease
AC-187
Discontinued
Amylin Pharmaceutical
Diabetes Mellitus
Phenserine tartrate
DWJ301
Discontinued
Qr Pharma
Alzheimer Disease
BI-473494
BI-473494
Discontinued
Zealand Pharma
Obesity, Diabetes Mellitus
NCT Number
NCT03195088
Intervention Type
Drug
Indications
Healthy
Study Phase
Phase 1
Recruitment Status
Terminated
ACO-253
AC-253, GG-747, ACO-253, GR-1150747A
Discontinued
Astrazeneca Plc, Bristol-Myers Squibb Company
Diabetes Mellitus, Type 2, Obesity
AC-625
AC-625
Discontinued
Astrazeneca Plc, Bristol-Myers Squibb Company
Hypertension
References
Title
Authors
Source
The complete islet amyloid polypeptide precursor is encoded by two exons
Mosselman S., Hoeppener J.W.M., Lips C.J.M., Jansz H.S.,
FEBS Lett. 247:154-158(1989)
Human islet amyloid polypeptide gene: complete nucleotide sequence, chromosomal localization, and evolutionary history
Nishi M., Sanke T., Seino S., Eddy R.L., Fan Y.-S., Byers M.G., Shows T.B., Bell G.I., Steiner D.F.,
Mol. Endocrinol. 3:1775-1781(1989)
An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing
Sanke T., Bell G.I., Sample C., Rubenstein A.H., Steiner D.F.,
J. Biol. Chem. 263:17243-17246(1988)
The human islet amyloid polypeptide (IAPP) gene. Organization, chromosomal localization and functional identification of a promoter region
Christmanson L., Rorsman F., Stenman G., Westermark P., Betsholtz C.,
FEBS Lett. 267:160-166(1990)
Islet amyloid polypeptide: structure and upstream sequences of the IAPP gene in rat and man
van Mansfeld A.D.M., Mosselman S., Hoeppener J.W.M., Zandberg J., van Teeffelen H.A.A.M., Baas P.D., Lips C.J.M., Jansz H.S.,
Biochim. Biophys. Acta 1087:235-240(1990)
Characterization of the human islet amyloid polypeptide/amylin gene transcripts: identification of a new polyadenylation site
Hoeppener J.W.M., Oosterwijk C., Visser-Vernooy H.J., Lips C.J.M., Jansz H.S.,
Biochem. Biophys. Res. Commun. 189:1569-1577(1992)
Cloning and expression of human islet amyloid polypeptide in cultured cells
Bhattacharya S., Naveena Lavanya Latha J., Kumresan R., Singh S.,
Biochem. Biophys. Res. Commun. 356:622-628(2007)
Islet amyloid polypeptide: identification and chromosomal localization of the human gene
Mosselman S., Hoeppener J.W.M., Zandberg J., van Mansfeld A.D.M., Geurts van Kessel A.H.M., Lips C.J.M., Jansz H.S.,
FEBS Lett. 239:227-232(1988)
Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus
Roberts A.N., Leighton B., Todd J.A., Cockburn D., Schofield P.N., Sutton R., Holt S., Boyd Y., Day A.J., Foot E.A., Willis A.C., Reid K.B.M., Cooper G.J.S.,
Proc. Natl. Acad. Sci. U.S.A. 86:9662-9666(1989)
Solution structures of calcitonin-gene-related-peptide analogues of calcitonin-gene-related peptide and amylin
Hubbard J.A.M., Martin S.R., Chaplin L.C., Bose C., Kelly S.M., Price N.C.,
Biochem. J. 275:785-788(1991)
Conformational preferences of the amylin nucleation site in SDS micelles: an NMR study
Mascioni A., Porcelli F., Ilangovan U., Ramamoorthy A., Veglia G.,
Biopolymers 69:29-41(2003)
Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism
Shen Y., Joachimiak A., Rosner M.R., Tang W.-J.,
Nature 443:870-874(2006)
Dynamic alpha-helix structure of micelle-bound human amylin
Patil S.M., Xu S., Sheftic S.R., Alexandrescu A.T.,
J. Biol. Chem. 284:11982-11991(2009)
Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process
Wiltzius J.J., Sievers S.A., Sawaya M.R., Eisenberg D.,
Protein Sci. 18:1521-1530(2009)
Missense mutation of amylin gene (S20G) in Japanese NIDDM patients
Sakagashira S., Sanke T., Hanabusa T., Shimomura H., Ohagi S., Kumagaye K.Y., Nakajima K., Nanjo K.,
Diabetes 45:1279-1281(1996)
Role of S20G mutation of amylin gene in insulin secretion, insulin sensitivity, and type II diabetes mellitus in Taiwanese patients
Chuang L.M., Lee K.C., Huang C.N., Wu H.P., Tai T.Y., Lin B.J.,
Diabetologia 41:1250-1251(1998)
Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients
Cooper G.J., Willis A.C., Clark A., Turner R.C., Sim R.B., Reid K.B.,
Proc. Natl. Acad. Sci. U.S.A. 84:8628-8632(1987)
Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species
Betsholtz C., Christmansson L., Engstroem U., Rorsman F., Svensson V., Johnson K.H., Westermark P.,
FEBS Lett. 251:261-264(1989)
Isolation and identification of islet amyloid polypeptide in normal human pancreas
Nakazato M., Asai J., Miyazato M., Matsukura S., Kangawa K., Matsuo H.,
Regul. Pept. 31:179-186(1990)
A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas
Westermark P., Wernstedt C., Wilander E., Sletten K.,
Biochem. Biophys. Res. Commun. 140:827-831(1986)
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
Westermark P., Wernstedt C., Wilander E., Hayden D.W., O'Brien T.D., Johnson K.H.,
Proc. Natl. Acad. Sci. U.S.A. 84:3881-3885(1987)
The complete islet amyloid polypeptide precursor is encoded by two exons.
Mosselman S., Hoeppener J.W.M., Lips C.J.M., Jansz H.S.,
FEBS Lett. 247:154-158(1989)
Human islet amyloid polypeptide gene: complete nucleotide sequence, chromosomal localization, and evolutionary history.
Nishi M., Sanke T., Seino S., Eddy R.L., Fan Y.-S., Byers M.G., Shows T.B., Bell G.I., Steiner D.F.,
Mol. Endocrinol. 3:1775-1781(1989)
An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing.
Sanke T., Bell G.I., Sample C., Rubenstein A.H., Steiner D.F.,
J. Biol. Chem. 263:17243-17246(1988)
The human islet amyloid polypeptide (IAPP) gene. Organization, chromosomal localization and functional identification of a promoter region.
Christmanson L., Rorsman F., Stenman G., Westermark P., Betsholtz C.,
FEBS Lett. 267:160-166(1990)
Islet amyloid polypeptide: structure and upstream sequences of the IAPP gene in rat and man.
van Mansfeld A.D.M., Mosselman S., Hoeppener J.W.M., Zandberg J., van Teeffelen H.A.A.M., Baas P.D., Lips C.J.M., Jansz H.S.,
Biochim. Biophys. Acta 1087:235-240(1990)
Characterization of the human islet amyloid polypeptide/amylin gene transcripts: identification of a new polyadenylation site.
Hoeppener J.W.M., Oosterwijk C., Visser-Vernooy H.J., Lips C.J.M., Jansz H.S.,
Biochem. Biophys. Res. Commun. 189:1569-1577(1992)
Cloning and expression of human islet amyloid polypeptide in cultured cells.
Bhattacharya S., Naveena Lavanya Latha J., Kumresan R., Singh S.,
Biochem. Biophys. Res. Commun. 356:622-628(2007)
Islet amyloid polypeptide: identification and chromosomal localization of the human gene.
Mosselman S., Hoeppener J.W.M., Zandberg J., van Mansfeld A.D.M., Geurts van Kessel A.H.M., Lips C.J.M., Jansz H.S.,
FEBS Lett. 239:227-232(1988)
Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients.
Cooper G.J., Willis A.C., Clark A., Turner R.C., Sim R.B., Reid K.B.,
Proc. Natl. Acad. Sci. U.S.A. 84:8628-8632(1987)
Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species.
Betsholtz C., Christmansson L., Engstroem U., Rorsman F., Svensson V., Johnson K.H., Westermark P.,
FEBS Lett. 251:261-264(1989)
Isolation and identification of islet amyloid polypeptide in normal human pancreas.
Nakazato M., Asai J., Miyazato M., Matsukura S., Kangawa K., Matsuo H.,
Regul. Pept. 31:179-186(1990)
A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas.
Westermark P., Wernstedt C., Wilander E., Sletten K.,
Biochem. Biophys. Res. Commun. 140:827-831(1986)
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.
Westermark P., Wernstedt C., Wilander E., Hayden D.W., O'Brien T.D., Johnson K.H.,
Proc. Natl. Acad. Sci. U.S.A. 84:3881-3885(1987)
Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus.
Roberts A.N., Leighton B., Todd J.A., Cockburn D., Schofield P.N., Sutton R., Holt S., Boyd Y., Day A.J., Foot E.A., Willis A.C., Reid K.B.M., Cooper G.J.S.,
Proc. Natl. Acad. Sci. U.S.A. 86:9662-9666(1989)
Solution structures of calcitonin-gene-related-peptide analogues of calcitonin-gene-related peptide and amylin.
Hubbard J.A.M., Martin S.R., Chaplin L.C., Bose C., Kelly S.M., Price N.C.,
Biochem. J. 275:785-788(1991)
Conformational preferences of the amylin nucleation site in SDS micelles: an NMR study.
Mascioni A., Porcelli F., Ilangovan U., Ramamoorthy A., Veglia G.,
Biopolymers 69:29-41(2003)
Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism.
Shen Y., Joachimiak A., Rosner M.R., Tang W.-J.,
Nature 443:870-874(2006)
Dynamic alpha-helix structure of micelle-bound human amylin.
Patil S.M., Xu S., Sheftic S.R., Alexandrescu A.T.,
J. Biol. Chem. 284:11982-11991(2009)
Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process.
Wiltzius J.J., Sievers S.A., Sawaya M.R., Eisenberg D.,
Protein Sci. 18:1521-1530(2009)
Missense mutation of amylin gene (S20G) in Japanese NIDDM patients.
Sakagashira S., Sanke T., Hanabusa T., Shimomura H., Ohagi S., Kumagaye K.Y., Nakajima K., Nanjo K.,
Diabetes 45:1279-1281(1996)
Role of S20G mutation of amylin gene in insulin secretion, insulin sensitivity, and type II diabetes mellitus in Taiwanese patients.
Chuang L.M., Lee K.C., Huang C.N., Wu H.P., Tai T.Y., Lin B.J.,
Diabetologia 41:1250-1251(1998)
A stop-codon mutation in the BRI gene associated with familial British dementia.
Vidal R., Frangione B., Rostagno A., Mead S., Revesz T., Plant G., Ghiso J.,
Nature 399:776-781(1999)
Medin: an integral fragment of aortic smooth muscle cell-produced lactadherin forms the most common human amyloid.
Haeggqvist B., Naeslund J., Sletten K., Westermark G.T., Mucchiano G., Tjernberg L.O., Nordstedt C., Engstroem U., Westermark P.,
Proc. Natl. Acad. Sci. U.S.A. 96:8669-8674(1999)
Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth.
McLaurin J., Franklin T., Zhang X., Deng J., Fraser P.E.,
Eur J Biochem 266:1101-1110(1999)
The islet amyloid polypeptide (amylin) gene S20G mutation in Chinese subjects: evidence for associations with type 2 diabetes and cholesterol levels.
Lee S.C., Hashim Y., Li J.K., Ko G.T., Critchley J.A., Cockram C.S., Chan J.C.,
Clin Endocrinol (Oxf) 54:541-546(2001)
A new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene.
Benson M.D., Liepnieks J.J., Yazaki M., Yamashita T., Hamidi Asl K., Guenther B., Kluve-Beckerman B.,
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Codeposition of apolipoprotein A-IV and transthyretin in senile systemic (ATTR) amyloidosis.
Bergstrom J., Murphy C., Eulitz M., Weiss D.T., Westermark G.T., Solomon A., Westermark P.,
Biochem Biophys Res Commun 285:903-908(2001)
Structure-based design and study of non-amyloidogenic, double N-methylated IAPP amyloid core sequences as inhibitors of IAPP amyloid formation and cytotoxicity.
Kapurniotu A., Schmauder A., Tenidis K.,
J Mol Biol 315:339-350(2002)
Quantitative assessment of gene targeting in vitro and in vivo by the pancreatic transcription factor, Pdx1. Importance of chromatin structure in directing promoter binding.
Chakrabarti S.K., James J.C., Mirmira R.G.,
J Biol Chem 277:13286-13293(2002)
Binding of serum amyloid P-component (SAP) by amyloid fibrils.
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Glucoregulatory endocrine responses to intermittent exercise of different intensities: plasma changes in a pancreatic beta-cell peptide, amylin.
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Metabolism 51:657-663(2002)
Selective inhibition of heterotrimeric Gs signaling. Targeting the receptor-G protein interface using a peptide minigene encoding the Galpha(s) carboxyl terminus.
Feldman D.S., Zamah A.M., Pierce K.L., Miller W.E., Kelly F., Rapacciuolo A., Rockman H.A., Koch W.J., Luttrell L.M.,
J Biol Chem 277:28631-28640(2002)
Estrogen can prevent or reverse obesity and diabetes in mice expressing human islet amyloid polypeptide.
Geisler J.G., Zawalich W., Zawalich K., Lakey J.R., Stukenbrok H., Milici A.J., Soeller W.C.,
Diabetes 51:2158-2169(2002)
Similarities and differences in the coupling of human beta1- and beta2-adrenoceptors to Gs(alpha) splice variants.
Wenzel-Seifert K., Liu H.Y., Seifert R.,
Biochem Pharmacol 64:9-20(2002)
Islet amyloid, metabolic syndrome, and the natural progressive history of type 2 diabetes mellitus.
Hayden M.R.,
JOP 3:126-138(2002)
Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and alpha-hydroxy acid residue containing peptides.
Rijkers D.T., Hoppener J.W., Posthuma G., Lips C.J., Liskamp R.M.,
Chemistry 8:4285-4291(2002)
Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide.
Mazor Y., Gilead S., Benhar I., Gazit E.,
J Mol Biol 322:1013-1024(2002)
Increased expression and activation of c-Jun contributes to human amylin-induced apoptosis in pancreatic islet beta-cells.
Zhang S., Liu J., MacGibbon G., Dragunow M., Cooper G.J.,
J Mol Biol 324:271-285(2002)
Increased dietary fat promotes islet amyloid formation and beta-cell secretory dysfunction in a transgenic mouse model of islet amyloid.
Hull R.L., Andrikopoulos S., Verchere C.B., Vidal J., Wang F., Cnop M., Prigeon R.L., Kahn S.E.,
Diabetes 52:372-379(2003)
Polymorphism in intron 2 of islet amyloid polypeptide gene is associated with lower low-density lipoprotein cholesterol in nondiabetic subjects and in type 2 diabetic patients.
Rojas I., Gomis R., Casals E., Quinto L.I., Franco C., Novials A.,
Endocrine 19:185-189(2002)
Full-length rat amylin forms fibrils following substitution of single residues from human amylin.
Green J., Goldsbury C., Mini T., Sunderji S., Frey P., Kistler J., Cooper G., Aebi U.,
J Mol Biol 326:1147-1156(2003)
Human amylin actions on rat cholinergic basal forebrain neurons: antagonism of beta-amyloid effects.
Jhamandas J.H., Harris K.H., Cho C., Fu W., MacTavish D.,
J Neurophysiol 89:2923-2930(2003)
Amylin gene promoter mutations predispose to Type 2 diabetes in New Zealand Maori.
Poa N.R., Cooper G.J., Edgar P.F.,
Diabetologia 46:574-578(2003)
Apolipoprotein E genotype, islet amyloid deposition and severity of Type 2 diabetes.
Powell D.S., Maksoud H., Charge S.B., Moffitt J.H., Desai M., Da Silva Fihlo R.L., Hattersley A.T., Stratton I.M., Matthews D.R., Levy J.C., Clark A.,
Diabetes Res Clin Pract 60:105-110(2003)
S20G mutation of the amylin gene is associated with a lower body mass index in Korean type 2 diabetic patients.
Cho Y.M., Kim M., Park K.S., Kim S.Y., Lee H.K.,
Diabetes Res Clin Pract 60:125-129(2003)
Isolation and partial characterization of SAA-an amyloid-related protein from human serum.
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J Mol Biol 329:565-584(2003)
Characterization of the 5-HT6 receptor coupled to Ca2+ signaling using an enabling chimeric G-protein.
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Eur J Pharmacol 472:33-38(2003)
Cloning, characterization, and expression of a human calcitonin receptor from an ovarian carcinoma cell line.
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Fibrillogenic amylin evokes islet beta-cell apoptosis through linked activation of a caspase cascade and JNK1.
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J Biol Chem 278:52810-52819(2003)
Prevalence and clinicopathological characteristics of islet amyloid in chinese patients with type 2 diabetes.
Zhao H.L., Lai F.M., Tong P.C., Zhong D.R., Yang D., Tomlinson B., Chan J.C.,
Diabetes 52:2759-2766(2003)
Immunohistochemical localization of amylin in human pancreas, thyroid, pituitary and their tumors.
Rotondo F., Vidal S., Bell D., Horvath E., Kovacs K., Scheithauer B.W., Lloyd R.V.,
Acta Histochem 105:303-307(2003)
The mechanism of insulin action on islet amyloid polypeptide fiber formation.
Larson J.L., Miranker A.D.,
J Mol Biol 335:221-231(2004)
Amyloidogenicity and cytotoxicity of recombinant mature human islet amyloid polypeptide (rhIAPP).
Lopes D.H., Colin C., Degaki T.L., de Sousa A.C., Vieira M.N., Sebollela A., Martinez A.M., Bloch C. Jr., Ferreira S.T., Sogayar M.C.,
J Biol Chem 279:42803-42810(2004)
Phospholipid catalysis of diabetic amyloid assembly.
Knight J.D., Miranker A.D.,
J Mol Biol 341:1175-1187(2004)
Atomic force microscopy reveals defects within mica supported lipid bilayers induced by the amyloidogenic human amylin peptide.
Green J.D., Kreplak L., Goldsbury C., Li Blatter X., Stolz M., Cooper G.S., Seelig A., Kistler J., Aebi U.,
J Mol Biol 342:877-887(2004)
Islet amyloid polypeptide-induced membrane leakage involves uptake of lipids by forming amyloid fibers.
Sparr E., Engel M.F., Sakharov D.V., Sprong M., Jacobs J., de Kruijff B., Hoppener J.W., Killian J.A.,
FEBS Lett 577:117-120(2004)
Atomic force microscopy study of human amylin (20-29) fibrils.
Sedman V.L., Allen S., Chan W.C., Davies M.C., Roberts C.J., Tendler S.J., Williams P.M.,
Protein Pept Lett 12:79-83(2005)
Neutron diffraction reveals sequence-specific membrane insertion of pre-fibrillar islet amyloid polypeptide and inhibition by rifampicin.
Balali-Mood K., Ashley R.H., Hauss T., Bradshaw J.P.,
FEBS Lett 579:1143-1148(2005)
Molecular dynamics simulation of the aggregation of the core-recognition motif of the islet amyloid polypeptide in explicit water.
Colombo G., Daidone I., Gazit E., Amadei A., Di Nola A.,
Proteins 59:519-527(2005)
The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin.
Kajava A.V., Aebi U., Steven A.C.,
J Mol Biol 348:247-252(2005)
Islet amyloid polypeptide gene promoter polymorphisms are not associated with Type 2 diabetes or with the severity of islet amyloidosis.
Esapa C., Moffitt J.H., Novials A., McNamara C.M., Levy J.C., Laakso M., Gomis R., Clark A.,
Biochim Biophys Acta 1740:74-78(2005)
Is aggregated IAPP a cause of beta-cell failure in transplanted human pancreatic islets?
Westermark P., Andersson A., Westermark G.T.,
Curr Diab Rep 5:184-188(2005)
Senile seminal vesicle amyloid is derived from semenogelin I.
Linke R.P., Joswig R., Murphy C.L., Wang S., Zhou H., Gross U., Rocken C., Westermark P., Weiss D.T., Solomon A.,
J Lab Clin Med 145:187-193(2005)
Long-term treatment with rosiglitazone and metformin reduces the extent of, but does not prevent, islet amyloid deposition in mice expressing the gene for human islet amyloid polypeptide.
Hull R.L., Shen Z.P., Watts M.R., Kodama K., Carr D.B., Utzschneider K.M., Zraika S., Wang F., Kahn S.E.,
Diabetes 54:2235-2244(2005)
Lipid membranes modulate the structure of islet amyloid polypeptide.
Jayasinghe S.A., Langen R.,
Biochemistry 44:12113-12119(2005)
Activation of peroxisome proliferator-activated receptor-gamma by rosiglitazone protects human islet cells against human islet amyloid polypeptide toxicity by a phosphatidylinositol 3'-kinase-dependent pathway.
Lin C.Y., Gurlo T., Haataja L., Hsueh W.A., Butler P.C.,
J Clin Endocrinol Metab 90:6678-6686(2005)
Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: is there a critical amyloidogenic domain in human IAPP?
Abedini A., Raleigh D.P.,
J Mol Biol 355:274-281(2006)
The role of His-18 in amyloid formation by human islet amyloid polypeptide.
Abedini A., Raleigh D.P.,
Biochemistry 44:16284-16291(2005)
Islet amyloid polypeptide inserts into phospholipid monolayers as monomer.
Engel M.F., Yigittop H., Elgersma R.C., Rijkers D.T., Liskamp R.M., de Kruijff B., Hoppener J.W., Antoinette Killian J.,
J Mol Biol 356:783-789(2006)
Beta-cell deficit due to increased apoptosis in the human islet amyloid polypeptide transgenic (HIP) rat recapitulates the metabolic defects present in type 2 diabetes.
Matveyenko A.V., Butler P.C.,
Diabetes 55:2106-2114(2006)
Characterization of the heparin binding site in the N-terminus of human pro-islet amyloid polypeptide: implications for amyloid formation.
Abedini A., Tracz S.M., Cho J.H., Raleigh D.P.,
Biochemistry 45:9228-9237(2006)
Amylin S20G mutation in Mexican population.
Garcia-Gonzalez C.L., Montoya-Fuentes H., Padilla-Rosas M., Sanchez-Corona J.,
Diabetes Res Clin Pract 76:146-148(2007)
Direct detection of transient alpha-helical states in islet amyloid polypeptide.
Williamson J.A., Miranker A.D.,
Protein Sci 16:110-117(2007)
The minimal amyloid-forming fragment of the islet amyloid polypeptide is a glycolipid-binding domain.
Levy M., Garmy N., Gazit E., Fantini J.,
FEBS J 273:5724-5735(2006)
Amylin and hypertension: association of an amylin -G132A gene mutation and hypertension in humans and amylin-induced endothelium dysfunction in rats.
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