scholarly journals Effect of dexamethasone on insulin sensitivity, islet amyloid polypeptide and insulin secretion in humans

Diabetologia ◽  
1993 ◽  
Vol 36 (1) ◽  
pp. 84-87 ◽  
Author(s):  
B. Ludvik ◽  
M. Clodi ◽  
A. Kautzky-Willer ◽  
M. Capek ◽  
E. Hartter ◽  
...  
Keyword(s):  
Insulin Secretion ◽  
Insulin Sensitivity ◽  
Islet Amyloid Polypeptide ◽  
Islet Amyloid

scholarly journals Molecular Docking Studies of Possible Treatment of Diabetes using Vasicine against Islet Amyloid Polypeptide

2021 ◽  
Vol 9 (VI) ◽  
pp. 4202-4209
Author(s):  
Tushar Kumar
Keyword(s):  
Type 2 Diabetes ◽  
Insulin Secretion ◽  
Molecular Docking ◽  
Islet Amyloid Polypeptide ◽  
Docking Studies ◽  
Islet Amyloid ◽  
Molecular Docking Studies ◽  
The World ◽  
Treatment Of Diabetes

Diabetes is the becoming one of the most common problem all over the world. About 1 in 10 persons are suffering from diabetes and most from type 2 diabetes. It occurs due to problem in pancreas which further results defect in the insulin secretion, as insulin maintains blood glucose level. The effect of Alpha-Amyrin Acetate, Myrcene and Vasicine compounds against Islet Amyloid polypeptide (IAPP) protein was seen through molecular docking studies. IAPP acts as complementary to insulin in regulating the sugar level for the treatment of diabetes disease by virtual screening. Different tools and software used in this research were Uniprot, Pubchem, Swiss ADMS, PyRx, Auto dock Vina/MGL tool and PyMOL.

scholarly journals Lipid Modulation in the Formation of β-Sheet Structures. Implications for De Novo Design of Human Islet Amyloid Polypeptide and the Impact on β-Cell Homeostasis

Biomolecules ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 1201 ◽  
Author(s):  
Israel Martínez-Navarro ◽  
Raúl Díaz-Molina ◽  
Angel Pulido-Capiz ◽  
Jaime Mas-Oliva ◽  
Ismael Luna-Reyes ◽  
...  
Keyword(s):  
Insulin Secretion ◽  
Membrane Lipids ◽  
Islet Amyloid Polypeptide ◽  
Human Islet ◽  
Β Cells ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide ◽  
Insulin Granules ◽  
The Impact ◽  
Β Sheet

Human islet amyloid polypeptide (hIAPP) corresponds to a 37-residue hormone present in insulin granules that maintains a high propensity to form β-sheet structures during co-secretion with insulin. Previously, employing a biomimetic approach, we proposed a panel of optimized IAPP sequences with only one residue substitution that shows the capability to reduce amyloidogenesis. Taking into account that specific membrane lipids have been considered as a key factor in the induction of cytotoxicity, in this study, following the same design strategy, we characterize the effect of a series of lipids upon several polypeptide domains that show the highest aggregation propensity. The characterization of the C-native segment of hIAPP (residues F23-Y37), together with novel variants F23R and I26A allowed us to demonstrate an effect upon the formation of β-sheet structures. Our results suggest that zwitterionic phospholipids promote adsorption of the C-native segments at the lipid-interface and β-sheet formation with the exception of the F23R variant. Moreover, the presence of cholesterol did not modify this behavior, and the β-sheet structural transitions were not registered when the N-terminal domain of hIAPP (K1-S20) was characterized. Considering that insulin granules are enriched in phosphatidylserine (PS), the property of lipid vesicles containing negatively charged lipids was also evaluated. We found that these types of lipids promote β-sheet conformational transitions in both the C-native segment and the new variants. Furthermore, these PS/peptides arrangements are internalized in Langerhans islet β-cells, localized in the endoplasmic reticulum, and trigger critical pathways such as unfolded protein response (UPR), affecting insulin secretion. Since this phenomenon was associated with the presence of cytotoxicity on Langerhans islet β-cells, it can be concluded that the anionic lipid environment and degree of solvation are critical conditions for the stability of segments with the propensity to form β-sheet structures, a situation that will eventually affect the structural characteristics and stability of IAPP within insulin granules, thus modifying the insulin secretion.

Increased Insulin Secretion and Glucose Tolerance in Mice Lacking Islet Amyloid Polypeptide (Amylin)

1998 ◽  
Vol 250 (2) ◽  
pp. 271-277 ◽  
Author(s):  
Samuel Gebre-Medhin ◽  
Hindrik Mulder ◽  
Milos Pekny ◽  
Gunilla Westermark ◽  
Jan Törnell ◽  
...  
Keyword(s):  
Insulin Secretion ◽  
Glucose Tolerance ◽  
Islet Amyloid Polypeptide ◽  
Islet Amyloid

Islet Amyloid Polypeptide (IAPP) and Insulin Secretion

1994 ◽  
pp. 381-398 ◽  
Author(s):  
Peter C. Butler ◽  
Norman L. Eberhardt ◽  
Timothy D. O’Brien
Keyword(s):  
Insulin Secretion ◽  
Islet Amyloid Polypeptide ◽  
Islet Amyloid
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