scholarly journals Inhibitory effects of choline-O-sulfate on amyloid formation of human islet amyloid polypeptide

FEBS Open Bio ◽  
2012 ◽  
Vol 2 (1) ◽  
pp. 20-25 ◽  
Author(s):  
Mamoru Hagihara ◽  
Ayaka Takei ◽  
Takeshi Ishii ◽  
Fumio Hayashi ◽  
Kenji Kubota ◽  
...  
Keyword(s):  
Islet Amyloid Polypeptide ◽  
Human Islet ◽  
Amyloid Formation ◽  
Inhibitory Effects ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide

Extended life span is associated with insulin resistance in a transgenic mouse model of insulinoma secreting human islet amyloid polypeptide

2004 ◽  
Vol 286 (3) ◽  
pp. E418-E424 ◽  
Author(s):  
Sofianos Andrikopoulos ◽  
Rebecca L. Hull ◽  
C. Bruce Verchere ◽  
Feng Wang ◽  
Shani M. Wilbur ◽  
...  
Keyword(s):  
Insulin Resistance ◽  
Life Span ◽  
Amyloid Fibrils ◽  
Islet Amyloid Polypeptide ◽  
Transgenic Animals ◽  
Human Islet ◽  
Amyloid Formation ◽  
Islet Amyloid ◽  
Glucose Levels ◽  
Human Islet Amyloid Polypeptide

Pancreatic amyloid is found in patients with insulinomas and type 2 diabetes. To study mechanisms of islet amyloidogenesis, we produced transgenic mice expressing the unique component of human islet amyloid, human islet amyloid polypeptide (hIAPP). These mice develop islet amyloid after 12 mo of high-fat feeding. To determine whether we could accelerate the rate of islet amyloid formation, we crossbred our hIAPP transgenic animals with RIP-Tag mice that develop islet tumors and die at 12 wk of age from hypoglycemia. At 12 wk of age, this new line of hIAPP×RIP-Tag mice was heavier (29.7 ± 1.0 vs. 25.0 ± 1.3 g, P < 0.05) and had increased plasma glucose levels (4.6 ± 0.4 vs. 2.9 ± 0.6 mmol/l, P < 0.05) compared with littermate RIP-Tag mice. However, the hIAPP×RIP-Tag mice did not display islet amyloid or amyloid fibrils despite high circulating hIAPP levels (24.6 ± 7.0 pmol/l). Interestingly, hIAPP×RIP-Tag mice had a longer life span than RIP-Tag mice (121 ± 8 vs. 102 ± 5 days, P < 0.05). This increase in life span in hIAPP×RIP-Tag was positively correlated with body weight ( r = 0.48, P < 0.05) and was associated with decreased insulin sensitivity compared with RIP-Tag mice. hIAPP×RIP-Tag mice did not develop amyloid during their 4-mo life span, suggesting that increased hIAPP secretion is insufficient for islet amyloid formation within such a short time. However, hIAPP×RIP-Tag mice did have an increase in life span that was associated with insulin resistance, suggesting that hIAPP has extrapancreatic effects, possibly on peripheral glucose metabolism.

Bisphenol analogues differently affect human islet polypeptide amyloid formation

RSC Advances ◽  
2016 ◽  
Vol 6 (9) ◽  
pp. 7239-7248 ◽  
Author(s):  
Lizi Huang ◽  
Mingyan Liao ◽  
Xin Yang ◽  
Hao Gong ◽  
Liang Ma ◽  
...  
Keyword(s):  
Plastic Material ◽  
Islet Amyloid Polypeptide ◽  
Human Islet ◽  
Causal Factor ◽  
Amyloid Formation ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide ◽  
Bisphenol Analogues

Bisphenols (BPs) are widely used in the production of plastic material, misfolded human islet amyloid polypeptide (hIAPP) is a causal factor in diabetes. We demonstrated BPs analogues show different effects on hIAPP amyloid formation.

Oophorectomy promotes islet amyloid formation in human islet amyloid polypeptide transgenic mice

Diabetes ◽  
2001 ◽  
Vol 50 (Supplement 1) ◽  
pp. S184-S185 ◽  
Author(s):  
R. L. Hull ◽  
B. Verchere ◽  
S. Andrikopoulos ◽  
F. Wang ◽  
J. Vidal ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Islet Amyloid Polypeptide ◽  
Human Islet ◽  
Amyloid Formation ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide

scholarly journals Extracellular vesicles from human pancreatic islets suppress human islet amyloid polypeptide amyloid formation

2017 ◽  
Vol 114 (42) ◽  
pp. 11127-11132 ◽  
Author(s):  
Diana Ribeiro ◽  
Istvan Horvath ◽  
Nikki Heath ◽  
Ryan Hicks ◽  
Anna Forslöw ◽  
...  
Keyword(s):  
Pancreatic Islets ◽  
Extracellular Vesicles ◽  
Islet Amyloid Polypeptide ◽  
Cell Communication ◽  
Human Islet ◽  
Amyloid Formation ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide ◽  
Amyloid Deposits

Extracellular vesicles (EVs) are small vesicles released by cells to aid cell–cell communication and tissue homeostasis. Human islet amyloid polypeptide (IAPP) is the major component of amyloid deposits found in pancreatic islets of patients with type 2 diabetes (T2D). IAPP is secreted in conjunction with insulin from pancreatic β cells to regulate glucose metabolism. Here, using a combination of analytical and biophysical methods in vitro, we tested whether EVs isolated from pancreatic islets of healthy patients and patients with T2D modulate IAPP amyloid formation. We discovered that pancreatic EVs from healthy patients reduce IAPP amyloid formation by peptide scavenging, but T2D pancreatic and human serum EVs have no effect. In accordance with these differential effects, the insulin:C-peptide ratio and lipid composition differ between EVs from healthy pancreas and EVs from T2D pancreas and serum. It appears that healthy pancreatic EVs limit IAPP amyloid formation via direct binding as a tissue-specific control mechanism.

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