Results 31 to 40 of about 6,150 (181)

Secretion of islet amyloid polypeptide in response to glucose [PDF]

FEBS Letters, 1989
The content of isolet amyloid polypeptide (IAPP) in isolated rat pancreatic islets was determined by a radioimmunoassay. Reverse‐phase high‐performance liquid chromatography analysis revealed that a main peak of IAPP immunoreactivity in the extracts from the islets corresponded to a synthetic rat IAPP.
Kanatsuka, A., Makino, H., Ohsawa, H., Tokuyama, Y., Yamaguchi, T., Yoshida, S., Adachi, M.   +6 more
openaire   +2 more sources

Efficacy of IAPP suppression in mouse and human islets by GLP-1 analogue conjugated antisense oligonucleotide

Frontiers in Molecular Biosciences, 2023
Insulin resistance is the major risk factor for Type 2 diabetes (T2D). In vulnerable individuals, insulin resistance induces a progressive loss of insulin secretion with islet pathology revealing a partial deficit of beta cells and islet amyloid derived ...
Tatyana Gurlo, Thazha P. Prakash, Zhongying Wang, Maani Archang, Lina Pei, Madeline Rosenberger, Elaine Pirie, Richard G. Lee, Peter C. Butler   +8 more
doaj   +1 more source

Autoantibodies to Islet Amyloid Polypeptide in Diabetes

Diabetic Medicine, 1991
Islet amyloid polypeptide (IAPP) is the constituent peptide of amyloid in pancreatic islets of Type 2 diabetic patients and in insulinomas. Amyloid formation in Type 2 diabetes is associated with islet cell destruction which may promote formation of autoantibodies to IAPP.
Clark, A, Yon, S, de Koning, E, Holman, R   +3 more
openaire   +3 more sources

Islet amyloid polypeptide toxicity and membrane interactions [PDF]

Proceedings of the National Academy of Sciences, 2013
Significance Amyloid formation is a hallmark of a range of human diseases. The polypeptide hormone amylin forms amyloid deposits in type 2 diabetes, and amyloid formation is thought to be a contributor to the decline in β-cell mass in the disease, however the basis of amylin-induced cytotoxicity is not fully understood. Amylin-induced
Cao, Ping, Abedini, Andisheh, Wang, Hui, Tu, Ling-Hsien, Zhang, Xiaoxue, Schmidt, Ann Marie, Raleigh, Daniel P   +6 more
openaire   +4 more sources

Amyloid-Mediated Mechanisms of Membrane Disruption

Biophysica, 2021
Protein aggregation and amyloid formation are pathogenic events underlying the development of an increasingly large number of human diseases named “proteinopathies”.
Michele F. M. Sciacca, Carmelo La Rosa, Danilo Milardi   +2 more
doaj   +1 more source

Membrane interaction of islet amyloid polypeptide

Biochimica et Biophysica Acta (BBA) - Biomembranes, 2007
Increasing evidence suggests that the misfolding and deposition of IAPP plays an important role in the pathogenesis of type II, or non-insulin-dependent diabetes mellitus (T2DM). Membranes have been implicated in IAPP-dependent toxicity in several ways: Lipid membranes have been shown to promote the misfolding and aggregation of IAPP. Thus, potentially
Jayasinghe, Sajith A., Langen, Ralf
openaire   +2 more sources

Strategies for inducing diabetes in laboratory animals: Advances from chemical, surgical, immunologic, dietary, and genetic approaches

Animal Models and Experimental Medicine, EarlyView.
This review summarizes the principal experimental approaches used to induce diabetes in animal models. Strategies include chemical agents (streptozotocin, alloxan, dithizone, gold thioglucose), dietary interventions (high‐fat and high‐sugar diets), surgical methods (total or partial pancreatectomy), genetic models (db/db, ob/ob, Goto‐Kakizaki [GK ...
Milad Faraji, Maedeh Faraji, Nasrin Kazemipour   +2 more
wiley   +1 more source

Impact of Stabilizing Osmolytes on the Conformational Dynamics of Human and Rat Islet Amyloid Polypeptides

Proteins: Structure, Function, and Bioinformatics, EarlyView.
ABSTRACT The aggregation of human islet amyloid polypeptide (hIAPP) into cytotoxic oligomers and amyloid fibrils is a hallmark of type 2 diabetes mellitus (T2DM), leading to pancreatic β‐cell dysfunction. In contrast, rat IAPP (rIAPP) is largely non‐amyloidogenic. Osmolytes such as glucose, glycerol, and sorbitol are known to stabilize globular protein
Kiara A. Kidman, Claudio Pedrick, Cara A. Kreck, Ricardo L. Mancera   +3 more
wiley   +1 more source

Pro Islet Amyloid Polypeptide (ProIAPP) Immunoreactivity in the Islets of Langerhans [PDF]

Upsala Journal of Medical Sciences, 2000
Islet amyloid is typically found in type 2 diabetes mellitus and is believed to participate in the beta cell deterioration. The islet amyloid fibril consists of the 37-amino-acid islet amyloid polypeptide (IAPP) but its pathogenesis is only partly understood.
G T, Westermark, D F, Steiner, S, Gebre-Medhin, U, Engström, P, Westermark   +4 more
openaire   +2 more sources

Massively parallel quantification of mutational impact on IAPP amyloid formation

Nature Communications
Amyloid fibrils formed by the islet amyloid polypeptide cause pancreatic beta-cell damage, resulting in reduced insulin secretion and type 2 diabetes.
Marta Badia, Cristina Batlle, Benedetta Bolognesi   +2 more
doaj   +1 more source