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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.
Data (including data from studies using tissues from transgenic mice) suggest that IL1B (show IL1B Proteins) plays dual roles by (1) mediating islet amyloid-induced FAS (show FAS Proteins) up-regulation and apoptosis in pancreatic beta-cells and (2) down-regulating IAPP precursor processing thereby potentiating islet amyloid formation. (IL1B (show IL1B Proteins) = interleukin-1beta; FAS (show FAS Proteins) = FAS (show FAS Proteins) cell surface death receptor; IAPP = islet amyloid polypeptide)
Data suggest that single aromatic/hydrophobic amino acid residues within IAPP (islet amyloid polypeptide) amyloid core region are able to control its interaction with amyloid-beta(1-40) or amyloid-beta(1-42) but not IAPP self-assembly; four aromatic/hydrophobic residues are able to control both IAPP amyloid self-assembly and its cross-interaction with amyloid-beta(1-40) or amyloid-beta(1-42).
Data show that aluminum (Al3+) could inhibit islet amyloid polypeptide hIAPP(11-28) fibrillogenesis.
The absence of BACE2 (show BACE2 Proteins) ameliorates glucose tolerance defects induced by IAPP overexpression in the beta-cell and promotes beta-cell survival.
This study supports the elucidation of the structural basis of IAPP amyloid formation and highlights the extent of amyloid fibril polymorphism.
Data suggest that a single GlcNAc residue at CTR (show CALCR Proteins) N130 (asparagine 130) is responsible for enhanced affinity of calcitonin (show CALCA Proteins) for CTR (show CALCR Proteins) ECD (show SHFM1 Proteins); the same appears to apply for enhanced affinity of amylin for RAMP2 (show RAMP2 Proteins)-CTR (show CALCR Proteins) ECD (show SHFM1 Proteins). [GlcNAc = N-acetylglucosamine; CTR (show CALCR Proteins) = calcitonin receptor (show CALCR Proteins); ECD (show SHFM1 Proteins) = extracellular domain; RAMP2 (show RAMP2 Proteins) = receptor (calcitonin) activity modifying protein 2 (show RAMP2 Proteins)].
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.
deletion of the DeltaN isoforms of p63 (show CKAP4 Proteins) or p73 (show ARHGAP24 Proteins) leads to metabolic reprogramming and regression of p53 (show TP53 Proteins)-deficient tumours through upregulation of IAPP, the gene that encodes amylin, a 37-amino-acid peptide co-secreted with insulin (show INS Proteins) by the beta cells of the pancreas
The stability, conformational dynamics and association force of different single-layer models of the full-length wild-type and glycine mutants of amylin, were investigated.
studies have identified a novel TXNIP (show TXNIP Proteins)/miR (show MLXIP Proteins)-124a/FoxA2 (show FOXA2 Proteins)/IAPP signaling cascade linking the critical beta-cell signaling pathways of TXNIP (show TXNIP Proteins) and IAPP
MMP-9 (show MMP9 Proteins) constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP.
Data suggest that amylin and leptin (show LEP Proteins) play additive roles in regulating energy homeostasis via activation of overlapping signalling pathways; mechanisms may be different in hypothalamus, muscle, and liver and in cases of endoplasmic reticulum stress.
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