scholarly journals Islet amyloid polypeptide in pancreatic islets from type 2 diabetic subjects

Islets ◽  
2012 ◽  
Vol 4 (3) ◽  
pp. 223-232 ◽  
Author(s):  
Tatsuo Tomita
Keyword(s):  
Pancreatic Islets ◽  
Islet Amyloid Polypeptide ◽  
Islet Amyloid ◽  
Type 2 Diabetic

scholarly journals Membrane-Mediated Misfolding of Islet Amyloid Polypeptide is a Shared Mechanism among Type 2 Diabetic Risk Factors

2016 ◽  
Vol 110 (3) ◽  
pp. 399a
Author(s):  
Alan K. Okada ◽  
Kazuki Teranishi ◽  
Robert H. Chow ◽  
Ralf Langen
Keyword(s):  
Risk Factors ◽  
Islet Amyloid Polypeptide ◽  
Islet Amyloid ◽  
Type 2 Diabetic

PEG modified graphene oxide loaded with EALYLV peptides for inhibiting the aggregation of hIAPP associated with type-2 diabetes

2015 ◽  
Vol 3 (35) ◽  
pp. 7055-7067 ◽  
Author(s):  
Xianbo Zhou ◽  
Chengwen Cao ◽  
Qingchang Chen ◽  
Qianqian Yu ◽  
Yanan Liu ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Graphene Oxide ◽  
Pancreatic Islets ◽  
Islet Amyloid Polypeptide ◽  
Human Islet ◽  
Islet Amyloid ◽  
Amyloid Aggregate ◽  
Modified Graphene Oxide ◽  
Modified Graphene

Human islet amyloid polypeptide (hIAPP) was found as amyloid aggregate deposits in the pancreatic islets of patients with type-2 diabetes and studies showed that insulin and its derivatives were the potent inhibitors of hIAPP aggregation.

Azadirachtin inhibits amyloid formation, disaggregates pre-formed fibrils and protects pancreatic β-cells from human islet amyloid polypeptide/amylin-induced cytotoxicity

2019 ◽  
Vol 476 (5) ◽  
pp. 889-907 ◽  
Author(s):  
Richa Dubey ◽  
Ketaki Patil ◽  
Sarath C. Dantu ◽  
Devika M. Sardesai ◽  
Parnika Bhatia ◽  
...  
Keyword(s):  
Pancreatic Islets ◽  
Islet Amyloid Polypeptide ◽  
Human Islet ◽  
Dynamics Simulation ◽  
Major Constituent ◽  
Β Cells ◽  
Pancreatic Β Cells ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide

Abstract The human islet amyloid polypeptide (hIAPP) or amylin is the major constituent of amyloidogenic aggregates found in pancreatic islets of type 2 diabetic patients that have been associated with β-cell dysfunction and/or death associated with type 2 diabetes mellitus (T2DM). Therefore, developing and/or identifying inhibitors of hIAPP aggregation pathway and/or compound that can mediate disaggregation of preformed aggregates holds promise as a medical intervention for T2DM management. In the current study, the anti-amyloidogenic potential of Azadirachtin (AZD)—a secondary metabolite isolated from traditional medicinal plant Neem (Azadirachta indica)—was investigated by using a combination of biophysical and cellular assays. Our results indicate that AZD supplementation not only inhibits hIAPP aggregation but also disaggregates pre-existing hIAPP fibrils by forming amorphous aggregates that are non-toxic to pancreatic β-cells. Furthermore, AZD supplementation in pancreatic β-cells (INS-1E) resulted in inhibition of oxidative stress; along with restoration of the DNA damage, lipid peroxidation and the associated membrane damage, endoplasmic reticulum stress and mitochondrial membrane potential. AZD treatment also restored glucose-stimulated insulin secretion from pancreatic islets exposed to hIAPP. All-atom molecular dynamics simulation studies on full-length hIAPP pentamer with AZD suggested that AZD interacted with four possible binding sites in the amyloidogenic region of hIAPP. In summary, our results suggest AZD to be a promising candidate for combating T2DM and related amyloidogenic disorders.

Islet amyloid polypeptide gene: no evidence of abnormal promoter region in thirty-five type 2 diabetic patients

1994 ◽  
Vol 22 (2-3) ◽  
pp. 99-105 ◽  
Author(s):  
Yoshiharu Tokuyama ◽  
Azuma Kanatsuka ◽  
Yoshihumi Suzuki ◽  
Takahide Yamaguchi ◽  
Masato Taira ◽  
...  
Keyword(s):  
Promoter Region ◽  
Islet Amyloid Polypeptide ◽  
Diabetic Patients ◽  
Islet Amyloid ◽  
Type 2 Diabetic Patients ◽  
Type 2 Diabetic

Islet Amyloid Polypeptide, Islet Amyloid, and Diabetes Mellitus

2011 ◽  
Vol 91 (3) ◽  
pp. 795-826 ◽  
Author(s):  
Per Westermark ◽  
Arne Andersson ◽  
Gunilla T. Westermark
Keyword(s):  
Type 2 Diabetes ◽  
Pancreatic Islets ◽  
Amyloid Fibrils ◽  
Mammalian Species ◽  
Islet Amyloid Polypeptide ◽  
Glucagon Secretion ◽  
Β Cells ◽  
Islet Amyloid ◽  
Pancreatic Islets Of Langerhans

Islet amyloid polypeptide (IAPP, or amylin) is one of the major secretory products of β-cells of the pancreatic islets of Langerhans. It is a regulatory peptide with putative function both locally in the islets, where it inhibits insulin and glucagon secretion, and at distant targets. It has binding sites in the brain, possibly contributing also to satiety regulation and inhibits gastric emptying. Effects on several other organs have also been described. IAPP was discovered through its ability to aggregate into pancreatic islet amyloid deposits, which are seen particularly in association with type 2 diabetes in humans and with diabetes in a few other mammalian species, especially monkeys and cats. Aggregated IAPP has cytotoxic properties and is believed to be of critical importance for the loss of β-cells in type 2 diabetes and also in pancreatic islets transplanted into individuals with type 1 diabetes. This review deals both with physiological aspects of IAPP and with the pathophysiological role of aggregated forms of IAPP, including mechanisms whereby human IAPP forms toxic aggregates and amyloid fibrils.

Photodegradation of porphyrin-bound hIAPP(1–37) fibrils

2020 ◽  
Vol 44 (22) ◽  
pp. 9438-9443
Author(s):  
Yongxiu Song ◽  
Ping Li ◽  
Zhiming Zhang ◽  
Yin Wang ◽  
Zhefei Zhang ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Type 2 Diabetes ◽  
Type 2 Diabetes Mellitus ◽  
Pancreatic Islets ◽  
Islet Amyloid Polypeptide ◽  
Human Islet ◽  
Preventive Strategy ◽  
Islet Amyloid ◽  
Amyloid Deposits

Amyloid deposits in pancreatic islets of type 2 diabetes mellitus (T2DM) are mainly comprised of human islet amyloid polypeptide (hIAPP), the degradation of hIAPP fibrils by photoactive porphyrin could be a preventive strategy against T2DM.

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