Results 121 to 130 of about 5,646 (167)

Islet amyloid polypeptide: demonstration of mRNA in human pancreatic islets by in situ hybridization in islets with and without amyloid deposits [PDF]

open access: yesDiabetologia, 1993
Islet amyloid polypeptide which is normally coexpressed with insulin in beta cells, forms amyloid deposits especially in islets of Type 2 (non-insulin-dependent) diabetic subjects. Occurrence of islet amyloid is paradoxically associated with loss of islet amyloid polypeptide immunoreactivity in beta cells.
Per Westermark   +2 more
exaly   +3 more sources
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Introduction and Fundamentals of Human Islet Amyloid Polypeptide Inhibitors

ACS Applied Bio Materials, 2020
Type 2 diabetes (T2D) is a common protein misfolding disease (PMD), and its pathogenesis is considered to be tightly associated with the aggregation of the disease-causative hIAPP (or amylin). Numerous studies have shown a possible pathological link between hIAPP aggregation and β-cell death; thus, different-level strategies from basic research to ...
Yijing Tang   +7 more
openaire   +2 more sources

Aggregation of an amyloidogenic fragment of human islet amyloid polypeptide

BBA - Proteins and Proteomics, 2000
Native human islet amyloid polypeptide (hIAPP) has been identified as the major component of amyloid plaques found in the pancreatic islets of Langerhans of persons affected by type 2 diabetes mellitus. Early studies of hIAPP determined that a segment of the molecule, amino acids 20-29, is responsible for its aggregation into amyloid fibrils.
Elizabeth Rhoades, Ari Gafni, A Gafni
exaly   +3 more sources

Islet amyloid polypeptide: Identification and chromosomal localization of the human gene [PDF]

open access: yesFEBS Letters, 1988
Islet or insulinoma amyloid polypeptide (IAPP) is a 37 amino acid polypeptide isolated from pancreatic amyloid. Here, we describe the isolation and partial characterization of the human gene encoding IAPP. The DNA sequence predicts that IAPP is excised from a larger precursor protein and that its carboxy‐terminus is probably amidated.
A D Van Mansfeld   +2 more
exaly   +4 more sources

Regulation of Islet Amyloid Polypeptide in Human Pancreatic Islets

Diabetes, 1993
This study investigated the effect of glucose on islet amyloid polypeptide secretion, content, and mRNA synthesis of human pancreatic islets. The release of islet amyloid polypeptide from fresh isolated islets in response to glucose was parallel to that of insulin.
A, Novials   +4 more
openaire   +2 more sources

Amyloid in Human Islets of Langerhans: Immunologic Evidence That Islet Amyloid Polypeptide Is Modified in Amyloidogenesis

Pancreas, 2000
Amyloid derived from the beta-cell product islet amyloid polypeptide (IAPP) has been implicated for a beta-cell lesion in Type II diabetes mellitus. The pathogenesis of islet amyloid is poorly understood, and in addition to an amyloidogenic IAPP molecule and possibly increased concentration of IAPP, other unknown factors seem to be included.
Z, Ma, P, Westermark, G T, Westermark
openaire   +2 more sources

Ganglioside‐induced amyloid formation by human islet amyloid polypeptide in lipid rafts [PDF]

open access: yesFEBS Letters, 2009
Human islet amyloid polypeptide (hIAPP) is the primary component of the amyloid deposits found in the pancreatic islets of patients with type 2 diabetes mellitus. However, it is unknown how amyloid fibrils are formed in vivo. In this study, we demonstrate that gangliosides play an essential role in the formation of amyloid deposits by hIAPP on plasma ...
Katsumi Matsuzaki, Masaki Wakabayashi
exaly   +3 more sources

Amyloidogenicity of recombinant human pro-islet amyloid polypeptide (ProIAPP) [PDF]

open access: yesChemistry and Biology, 2000
Pancreatic amyloid has been associated with type II diabetes. The major constituent of pancreatic amyloid is the 37-residue peptide islet amyloid polypeptide (IAPP). IAPP is expressed as a 67-residue pro-peptide called ProIAPP which is processed to IAPP following stimulation.
Aphrodite Kapurniotu   +1 more
exaly   +3 more sources

Biflavones inhibit the fibrillation and cytotoxicity of the human islet amyloid polypeptide

Journal of Materials Chemistry B, 2022
Biflavones reverse the fibrillation and cytotoxicity induced by human islet amyloid polypeptide.
Jufei Xu   +4 more
openaire   +2 more sources

Isolation and identification of islet amyloid polypeptide in normal human pancreas

Regulatory Peptides, 1990
To identify islet amyloid polypeptide (IAPP) present in normal human pancreas, we isolated the peptide from a soluble peptide fraction of amyloid deposit-free pancreata of two non-diabetic patients by using reverse-phase high performance liquid chromatography coupled with a radioimmunoassay specific for human IAPP.
Msamitsu Nakazato   +2 more
exaly   +3 more sources

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