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This study highlights that with positional scanning of the split-tetracysteine motif (Cys-Cys (show DNAJC5 Proteins)), the fluorogenic probe fluorescein arsenical hairpin detection method offers unique time-dependent conformational insights on the proteospecies assembled throughout the amyloidogenic pathway of IAPP.
Bri2 (show ITM2B Proteins) BRICHOS domain is a potent inhibitor of IAPP fibril formation.IAPP colocalizes with Bri2 (show ITM2B Proteins) both intracellularly and in islet amyloid deposits.
Insulin (show INS Proteins) resistance in rheumatoid arthritis does not appear to be mediated by amylin. This would imply that the mechanisms associated with IR in RA patients differ from those at work in type 2 diabetes.
Study presents a new Zn(2+) binding site in the N-terminus of fibrillary amylin with three different coordination modes. Simulations showed that Zn(2+) ions bind to polymorphic amylin fibrils with a preference to bind to four Cys (show DNAJC5 Proteins) residues rather than two Cys (show DNAJC5 Proteins) residues of two neighboring amylin monomers.
The IAPP beta-hairpin can serve as a molecular recognition motif enabling control of IAPP aggregation.
cholesterol significantly modulates the ability of model membranes to induce IAPP amyloid formation and IAPP-mediated membrane damage.
point mutations within the central aggregation-prone regions contribute to the reduction of the overall amyloidogenic potential of IAPP but do not completely abolish the formation of IAPP amyloid fibrils.
Using the Tg2576 AD mouse model, a single intraperitoneal injection of amylin significantly increased Abeta (show APP Proteins) serum levels, and the effect was abolished by AC253, an amylin receptor antagonist, suggesting that amylin effect could be mediated by its receptor. Subsequent mechanistic studies showed amylin enhanced Abeta (show APP Proteins) transport across a cell-based model of the blood-brain barrier.
These results suggest that protein segment structures represent polymorphs of their parent protein and that segment 19-29 S20G may serve as a model for the toxic spine of human IAPP.
All-atom explicit-water molecular dynamics (MD) simulations studying adsorption, orientation, and surface interaction of hIAPP aggregates with different sizes (monomer to tetramer) and conformations (monomer with alpha-helix and tetramer with beta-sheet-rich U-turn) upon adsorption. hIAPP monomer with alpha-helical conformation and hIAPP pentamer with beta-sheet conformation can adsorb on both POPC and POPC/POPE (show HMBS Proteins) bilayers.
These data provide for the first time evidences for the toxic nature of oligomeric assemblies of murine amylin and its existence in wild-type, non-transgenic mice.
n T2 mice, the mRNA expression of Retn (show RETN Proteins) showed a moderate up-regulation (fold change=8.32; p=0.0019) in the adipose tissues. Iapp expression was also significantly up-regulated (fold change=9.78; p=0.012). Moreover, a 6.36-fold up-regulation for Drd5 (show DRD5 Proteins) was observed in the adipose tissues of T2 mice
Data suggest that hybrid insulin (show INS Proteins) peptides (HIPs), formed in insulin (show INS Proteins)-secreting-cells by fusion of insulin (show INS Proteins) C-peptide fragments to peptide fragments of chromogranin A (show CHGA Proteins) or islet amyloid polypeptide, and reactivity of CD4 (show CD4 Proteins)+-T-lymphocytes to HIPs may act as biomarkers of autoimmunity in type 1 diabetes.
Circulating aggregated amylin accumulates preferentially in male vs. female hearts and its effects on myocyte Ca(2 (show CA2 Proteins)+) cycling do not require diabetic remodeling of the myocardium.
Results suggest that amylin directly acts, through a p-ERK (show EPHB2 Proteins)-mediated process, on POMC (show POMC Proteins) neurons to enhance arcuate nucleus-paraventricular nucleus alphaMSH (show POMC Proteins) pathway development.
These data suggest participation by both soluble and fibrillar aggregates in IAPP-induced islet inflammation. IAPP-induced activation of TLR2 and secretion of IL-1 (show IL1A Proteins) may be important therapeutic targets to prevent amyloid-associated beta cell dysfunction.
Hypothalamic amylin is transcriptionally regulated by leptin (show LEP Proteins), that it can act directly on ObRb (show LEPR Proteins) neurons in concert with leptin (show LEP Proteins), and that it regulates feeding.
Matrix Metalloproteinase-9 (show MMP9 Proteins) Protects Islets from Amyloid-induced Toxicity.
Data indicate that T-cell receptors that react to chromogranin A (ChgA (show CHGA Proteins)) and islet amyloid polypeptide precursor (IAPP) autoantigens were impaired when the thymic stromal cells lacked thymus-specific serine protease (TSSP (show PRSS16 Proteins)).
Study the physiologic actions of IAPP on pancreatic beta cells, which secrete this peptide together with insulin (show INS Proteins) upon glucose stimulation. Explore the signaling pathways and mitogenic actions of IAPP on beta cells.
Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
Islet amyloid polypeptide (diabetes-associated peptide; amylin)
, diabetes-associated peptide
, insulinoma amyloid peptide
, islet amyloid polypeptide
, amyloid protein