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iapp-islet-amyloid-polypeptide

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Journal Articles
Journal: Diabetes
Diabetes 2007;56(5):1324–1332
Published: 01 May 2007
...Chia-Yu Lin; Tatyana Gurlo; Rakez Kayed; Alexandra E. Butler; Leena Haataja; Charles G. Glabe; Peter C. Butler OBJECTIVE —Islets in type 2 diabetes are characterized by a deficit in β-cells, increased β-cell apoptosis, and islet amyloid derived from islet amyloid polypeptide (IAPP). The toxic form...
Meeting Abstracts
Journal: Diabetes
Diabetes 2019;68(Supplement_1):2143-P
Published: 01 June 2019
... dysfunction.1 Two factors that contribute to beta cell dysfunction are IAPP and oxidative stress. A key inhibitor of the intracellular anti-oxidative response is Keap1. We treated isolated islets with parent or GLP-1R-L conjugated ASOs targeting either Keap1 or IAPP. At the highest dose, the parent...
Meeting Abstracts
Journal: Diabetes
Diabetes 2001;50(suppl_1):S160
Published: 01 February 2001
.... This review summarizes the nature of the amyloid deposition process and its association with disproportionate hyperproinsulinemia. It reviews recent studies in IAPP (islet-amyloid polypeptide, or amylin) transgenic mice developing islet amyloid deposits and hyperglycemia to suggest that the process of amyloid...
Images
Quantitative gene expression profile of pancreatic transcription factors an...
Published: 17 July 2013
FIG. 5. Quantitative gene expression profile of pancreatic transcription factors and glucose metabolism–related (A) and insulin secretory (B) genes in Mitf mutant (Mitfce/ce) and wild-type (wt/het) islets (n ≥ 4 per genotype). The data were normalized to HPRT mRNA and are presented relative to control (set to 1). IA-2, insulinoma-associated protein-2; IAPP, islet amyloid polypeptide. ***P < 0.001. FIG. 5. Quantitative gene expression profile of pancreatic transcription factors and glucose metabolism–related (A) and insulin secretory (B) genes in Mitf mutant (Mitfce/ce) and wild-type (wt/het) islets (n ≥ 4 per genotype). The data were normalized to HPRT mRNA and are presented relative to control (set to 1). IA-2, insulinoma-associated protein-2; IAPP, islet amyloid polypeptide. ***P < 0.001. More
Images
Type 1 diabetes incidence in NOD mice immunized with a control (<em>A</em>...
Published: 01 September 2009
FIG. 2. Type 1 diabetes incidence in NOD mice immunized with a control (A), target (B), or ignored (C) antigen. Mice were immunized at 12 weeks of age with the indicated antigen. *P < 0.05 and **P < 0.01 relative to the unmanipulated NOD mouse group. (Details are provided in ref. 28 ). CALB, calbindin; IAPP, islet amyloid polypeptide; MSA, mouse serum albumin; REC, reduced expression in cancer. FIG. 2. Type 1 diabetes incidence in NOD mice immunized with a control (A), target (B), or ignored (C) antigen. Mice were immunized at 12 weeks of age with the indicated antigen. *P < 0.05 and **P < 0.01 relative to the unmanipulated NOD mouse group. (Details are provided in ref. 28). CALB, calbindin; IAPP, islet amyloid polypeptide; MSA, mouse serum albumin; REC, reduced expression in cancer. More
Images
Beneficial and harmful effects of PERK activation. Normal PERK function is ...
Published: 22 October 2021
Figure 2 Beneficial and harmful effects of PERK activation. Normal PERK function is required for proinsulin folding, ER calcium balance, translation regulation, and cell survival, but PERK activation can also lead to cell death and loss of maturation markers. Activated by ER stress, low glucose, and low ER calcium, PERK phosphorylates eIF2α to simultaneously suppress global translation but selectively activate translation of some transcripts such as Atf4 and Aatf. Beneficial effects of PERK activation include suppression of translation when the ER is overloaded with peptide inputs, promotion of cell survival through activation of ATF4 and AATF, improved SERCA pump function by dephosphorylation of CLNX to derepress calcium transport, and proliferation. Harmful effects of PERK activation include suppression of translation of required genes including maturation factors and insulin itself (although PERK deletion also caused loss of MAFA and PDX1), as well as increased cell death through CHOP and inflammatory pathways. Green arrows indicate transcriptional regulation. AATF, apoptosis antagonizing transcription factor; AKT1, protein kinase B; ATF4, activating transcription factor 4; CALN, calcineurin; CHOP, C/EBP homologous protein; CLNX, calnexin; eIF2α, eukaryotic translation initiation factor 2 subunit 1; GRP78, glucose-regulated protein 78; Iapp, islet amyloid polypeptide precursor; IFNAR1, interferon α and β subunit 1; Ins1/2, insulin 1/2; MAFA, Maf bZIP transcription factor A; circled P indicates phosphorylation; PDX1, pancreatic and duodenal homeobox 1; PERK, protein kinase R-like ER kinase; UTR, untranslated region. Figure 2. Beneficial and harmful effects of PERK activation. Normal PERK function is required for proinsulin folding, ER calcium balance, translation regulation, and cell survival, but PERK activation can also lead to cell death and loss of maturation markers. Activated by ER stress, low glucose, and low ER calcium, PERK phosphorylates eIF2α to simultaneously suppress global translation but selectively activate translation of some transcripts such as Atf4 and Aatf. Beneficial effects of PERK activation include suppression of translation when the ER is overloaded with peptide inputs, promotion of cell survival through activation of ATF4 and AATF, improved SERCA pump function by dephosphorylation of CLNX to derepress calcium transport, and proliferation. Harmful effects of PERK activation include suppression of translation of required genes including maturation factors and insulin itself (although PERK deletion also caused loss of MAFA and PDX1), as well as increased cell death through CHOP and inflammatory pathways. Green arrows indicate transcriptional regulation. AATF, apoptosis antagonizing transcription factor; AKT1, protein kinase B; ATF4, activating transcription factor 4; CALN, calcineurin; CHOP, C/EBP homologous protein; CLNX, calnexin; eIF2α, eukaryotic translation initiation factor 2 subunit 1; GRP78, glucose-regulated protein 78; Iapp, islet amyloid polypeptide precursor; IFNAR1, interferon α and β subunit 1; Ins1/2, insulin 1/2; MAFA, Maf bZIP transcription factor A; circled P indicates phosphorylation; PDX1, pancreatic and duodenal homeobox 1; PERK, protein kinase R-like ER kinase; UTR, untranslated region. More
Journal Articles
Journal: Diabetes
Diabetes 1993;42(10):1514–1519
Published: 01 October 1993
... the islet amyloid polypeptide response of islets to the same stimulus was blunted. The IAPP content was > insulin content in a molar ratio (1:50 to 1:30) after long exposure of islets to concentrations of high glucose even though the increase was significant for both peptides (P < 0.005...
Meeting Abstracts
Journal: Diabetes
Diabetes 2001;50(suppl_1):S184
Published: 01 February 2001
...R L Hull; C B Verchere; S Andrikopoulos; F Wang; J Vidal; S E Kahn Oophorectomy Promotes Islet Amyloid Formation in Human Islet Amyloid Polypeptide Transgenic Mice Rebecca L. Hull, C. Bruce Verchere, So anos Andrikopoulos, Feng Wang, Josep Vidal, and Steven E. Kahn Islet amyloid polypeptide (IAPP...
Journal Articles
Journal: Diabetes
Diabetes 1994;43(12):1457–1461
Published: 01 December 1994
...David A D'Alessio; C Bruce Verchere; Steven E Kahn; Vicki Hoagland; Denis G Baskin; Richard D Palmiter; John W Ensinck Islet amyloid polypeptide (IAPP) is a secretory product of the pancreatic β-cell, which is the primary constituent of the islet amyloid that develops in type II diabetes. To study...
Journal Articles
Journal: Diabetes
Diabetes 2001;50(3):534–539
Published: 01 March 2001
...Jing Wang; Jun Xu; Jennifer Finnerty; Machi Furuta; Donald F. Steiner; C. Bruce Verchere Impaired processing of pro-islet amyloid polypeptide (proIAPP), the precursor of the β-cell peptide islet amyloid polypeptide (IAPP) (amylin), has been implicated in islet amyloid formation in type 2 diabetes...
Journal Articles
Journal: Diabetes
Diabetes 1994;43(2):329–336
Published: 01 February 1994
...Timothy D O'Brien; Alexandra E Butler; Patrick C Roche; Kenneth H Johnson; Peter C Butler Amyloid deposits that characteristically form in the pancreatic islets of patients with non-insulin-dependent diabetes mellitus (NIDDM) and in insulinomas are both derived from islet amyloid polypeptide (IAPP...
Journal Articles
Journal: Diabetes
Diabetes 1996;45(8):1094–1101
Published: 01 August 1996
...Marta Couce; Laurie A Kane; Timothy D O'Brien; Jon Charlesworth; Walter Soeller; John McNeish; David Kreutter; Patrick Roche; Peter C Butler Islet amyloid derived from islet amyloid polypeptide (IAPP) is a well-recognized feature of type II diabetes. However, the mechanism of islet amyloidogenesis...
Journal Articles
Journal: Diabetes
Diabetes 1994;43(3):454–458
Published: 01 March 1994
...Annika M Svensson; Stellan Sandler; Leif Jansson Anesthetized male Sprague-Dawley rats (350–400 g) were injected intravenously with either 0.1, 1, 15, or 25 nmol rat islet amyloid polypeptide (IAPP), 65 or 650 pmol rat calcitonin gene-related peptide (CGRP), or saline alone. IAPP at the two highest...
Meeting Abstracts
Journal: Diabetes
Diabetes 1999;48(10):1962–1970
Published: 01 October 1999
...S Andrikopoulos; C B Verchere; J C Teague; W M Howell; W Y Fujimoto; T N Wight; S E Kahn Type 2 diabetes is characterized by islet amyloid deposits, which are primarily composed of the amyloidogenic human form of islet amyloid polypeptide (IAPP, amylin). The mechanism of islet amyloido-genesis...
Meeting Abstracts
Journal: Diabetes
Diabetes 1999;48(3):491–498
Published: 01 March 1999
...J Janson; R H Ashley; D Harrison; S McIntyre; P C Butler NIDDM is characterized by islet amyloid deposits and decreased beta-cell mass. Islet amyloid is derived from the locally expressed protein islet amyloid polypeptide (IAPP). While it is now widely accepted that abnormal aggregation of IAPP has...
Meeting Abstracts
Journal: Diabetes
Diabetes 2000;49(12):2056–2062
Published: 01 December 2000
...S Andrikopoulos; C B Verchere; Y Terauchi; T Kadowaki; S E Kahn Type 2 diabetes is characterized by impaired beta-cell function, hyperglycemia, and islet amyloid deposition. The primary constituent of islet amyloid is the 37-amino acid beta-cell product called islet amyloid polypeptide (IAPP...
Journal Articles
Journal: Diabetes
Diabetes 2004;53(6):1509–1516
Published: 01 June 2004
... of islet amyloid derived from islet amyloid polypeptide (IAPP), a 37–amino acid protein cosecreted with insulin by β-cells. Several lines of evidence suggest that proteins with a capacity to develop amyloid fibrils may also form small toxic oligomers that can initiate apoptosis. The amino acid sequence...
Journal Articles
Journal: Diabetes
Diabetes 2003;52(7):1701–1708
Published: 01 July 2003
...Robert A. Ritzel; Peter C. Butler Type 2 diabetes is characterized by a relative β-cell deficit as a result of increased β-cell apoptosis and islet amyloid derived from the β-cell peptide islet amyloid polypeptide (IAPP). Human IAPP (h-IAPP) but not mouse IAPP (m-IAPP) induces apoptosis...
Meeting Abstracts
Journal: Diabetes
Diabetes 2000;49(9):1477–1484
Published: 01 September 2000
...C B Verchere; D A D'Alessio; R L Prigeon; R L Hull; S E Kahn Islet amyloid polypeptide (IAPP or amylin) is a normal secretory product of the pancreatic beta-cell that is cosecreted with insulin and is the major constituent of islet amyloid deposits in individuals with type 2 diabetes or insulinomas...
Journal Articles
Journal: Diabetes
Diabetes 2007;56(1):65–71
Published: 01 January 2007
... progressively declines in type 2 diabetes and following islet transplantation. Both are characterized by the presence of islet amyloid derived from islet amyloid polypeptide (IAPP). In the present studies, we examined the action of extracellular human IAPP (h-IAPP) on morphology and function of human islets...