Recombinant Rat Islet amyloid polypeptide (Iapp)

1. IAPP role in the pancreatic islet cell damage in the Type 2 diabetes mellitus. PMID: 29523142
2. this study reinforces the notion that IAPP amyloidogenesis is governed by precise intermolecular interactions involving specific Asn side chains. PMID: 28665109
3. C4BP protects beta-cells from IAPP cytotoxicity by modulating IAPP fibril formation extracellularly and also, after uptake by the cells, by enhancing cholesterol synthesis. PMID: 27566545
4. ventromedial hypothalamus amylin signaling is required for full leptin signaling and protection from high fat diet induced obesity PMID: 26676252
5. Secondary Structure of Rat and Human Amylin PMID: 26221949
6. cross-seeding assemblies between hIAPP and rIAPP oligomers PMID: 25706385
7. Inhibition of IAPP aggregation by insulin depends on the insulin oligomeric state regulated by zinc ion concentration PMID: 25649462
8. The data indicate minimal membrane disruption by both human and rat-IAPP20-29 when compared to the full-length IAPP peptide. PMID: 23493863
9. Amylin receptors are located mostly on presynaptic glutamatergic terminals connecting to area postrema neurons not displaying hyperpolarization-activated cation current. Amylin concentrations can increase glutamate release enough to cause cell firing. PMID: 23219578
10. C4BP binds to IAPP thereby limiting complement activation and may be enhancing formation of IAPP fibrils from cytotoxic oligomers PMID: 22334700
11. co-expression of calcitonin receptor(a) with rRAMP1 or 3 produces functional AMY receptor subtypes in rats, which display equivalent potency for rAmy and raCGRP PMID: 22014233
12. at 8 h after mixing, rat amylin blocks the N-terminal beta-sheet of fibrils. At 24 h after mixing, rat amylin blocks neither beta-sheet and forms its own beta-sheet PMID: 22522254
13. Data show that the multiplicity in islet amyloid polypeptide (rIAPP) assembly structures indicates the polydispersity of the rIAPP(8-37) beta-like motifs. PMID: 22106265
14. The results implicate amylin in the control of maternal adaptations, possibly exerting its actions on maternal behaviors via amylin receptors present in brain regions to which preoptic neurons project. PMID: 21965599
15. hIAPP overexpression inhibits insulin and IAPP secretion in response to glucose affecting the activity of K(ATP) channels PMID: 21984830
16. an actin-mediated and cholesterol-dependent mechanism for selective uptake and clearance of amylin oligomers, impairment of which greatly potentiates amylin toxicity. PMID: 21865171
17. The study is comparing the structural properties of human and rat islet amyloid polypeptide by MD computer simulations at 310 and 330 K and shows the effect of the disulfide bridge on the conformation of Iapp. PMID: 21266296
18. Data show that IAPP oligomeric species that arise through stochastic nucleation on membranes and result in disruption of the lipid bilayer. PMID: 21606325
19. Ca2+ entry via L-type Ca2+ channels, activation of PKC and Ca2+ release from sarcoplasmic reticulum through ryanodine-sensitive Ca2+ channels may be involved in amylin's positive inotropic effect. PMID: 21138812
20. Rats centrally infused with amylin had lower body weight gain controls independent of whether prior body weight was decreased by fasting, increased by voluntary overfeeding or unmanipulated. PMID: 20416330
21. Data indicate that basal insulin, leptin, ghrelin, and amylin do not encode AT mass in rats dynamically regulating BW and adiposity during recovery from OW. PMID: 20668029
22. we present detailed solution structures of rat amylin; the similarity of rat and human amylin sequences near the N-terminus suggests that human amylin might also exhibit a similar a-helical secondary structure PMID: 20141758
23. This His/Arg-18 mutation results in reduced affinity binding of human IAPP to insulin in comparison to rat IAPP. PMID: 19146426
24. Inhibition of human IAPP amyloid formation by rat IAPP can be rationalized by a model that postulates formation of an early helical intermediate during amyloid formation where the helical region is localized to the N-terminal region of IAPP. PMID: 20028124
25. these newly observed differences between human and rat amylin in solution and their possible relation to aggregation and to the physiological function of amylin binding to the calcitonin receptor PMID: 19948124
26. Data show that the three specific proline residues in human and rat amylin play a dominant negative role in fibril formation. PMID: 12589759
27. conformational preferences of hIAPP(20-29) in membrane-mimicking environments PMID: 12717720
28. Feeding-induced amylin release activates area postrema neurons projecting to relay stations known to transmit meal-related signals to the forebrain. Activation of this pathway seems to coincide with an inhibition of lateral hypothalamic area neurons. PMID: 12958059
29. amylin has a role in evoking a JNK1-mediated apoptotic pathway, which is partially dependent and partially independent of caspase-8, and in which caspase-3 acts as a common downstream effector PMID: 14532296
30. These results indicate that amylin is positively regulated by cyclic AMP and protein kinase A through the transcription factors HNF-1 and NFY. PMID: 14615061
31. results support the hypothesis that endogenous amylin plays an essential role in reducing meal size and increasing the postmeal interval of satiety PMID: 15130879
32. found that amylin increased GSK3alpha activity, which in turn led to increased phosphorylation of glycogen synthase and decreased glycogen synthesis de novo in rat soleus muscle PMID: 15572200
33. findings are consistent with the hypothesis that membrane-active pre-fibrillar IAPP oligomers insert into beta cell membranes in NIDDM PMID: 15710403
34. analysis of pro-islet amyloid polypeptide processing in the constitutive and regulated secretory pathways of beta cells PMID: 15802374
35. conditions that promote weakly stable alpha-helical conformations may promote IAPP aggregation PMID: 16142909
36. Data show that GABAA receptor antagonists prevent abnormalities in leptin, insulin and amylin actions on paraventricular hypothalamic neurons of overweight rats. PMID: 16553787
37. The data suggests that both KNT and KNTvd4(-) participate in microtubule-dependent secretion of amylin in islet beta-cells. PMID: 16890462
38. The inability of IAPP to self assemble can be ascribed, in part, to several slowly exchanging conformations evident as multiple chemical shift assignments in the immediate vicinity of three proline residues residing outside of this helical region. PMID: 17123962
39. Amylin did not influence energy expenditure or respiratory quotient in normal or food-restricted rats. PMID: 17428511
40. Results indicate that the lipostatic signals leptin and insulin may synergize with amylin to reduce food intake. PMID: 17481674
41. amylin effectively reduced food intake in ad libitum chow fed rats despite the low level of amylin-induced c-Fos expression in the area postrema PMID: 17703089
42. Central and peripheral administration of amylin induces energy expenditure in anesthetized rats. PMID: 18346817
43. amylin agonism restores leptin responsiveness in diet-induced obesity PMID: 18458326
44. Rat amylin does not share neurotoxic properties with Abeta42. PMID: 18486611
45. Amylin/leptin interact synergistically to reduce body weight and adiposity in diet-induced obese rodents through a number of anorexigenic and metabolic effects. PMID: 18669592
46. NMR structures of the human and rat IAPP(1-19) peptides in DPC micelles PMID: 18989932
47. the high-resolution structure of rat IAPP in the membrane-mimicking detergent micelles composed of dodecylphosphocholine was solved. PMID: 19456151
48. Amylin is expressed in rat placenta and regulated by nutritional status. PMID: 19554505
49. This studt indicted that the expression of amylin in the mammalian brain and described its distribution in the preoptic area of the hypothalamus. Our data also indicate that the level of amylin mRNA is dramatically induced in mother rats PMID: 19811608

Show More

Hide All

KEGG: rno:24476

STRING: 10116.ENSRNOP00000016614

UniGene: Rn.11394