Results 221 to 230 of about 20,996 (256)
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Structural Characterisation of Islet Amyloid Polypeptide Fibrils

Journal of Molecular Biology, 2004
Islet amyloid is found in many patients suffering from type 2 diabetes. Amyloid fibrils found deposited in the pancreatic islets are composed of a 37-residue peptide, known as islet amyloid polypeptide (IAPP) (also known as amylin) and are similar to those found in other amyloid diseases.
O, Sumner Makin, Louise C, Serpell
openaire   +2 more sources

Influence of islet amyloid polypeptide and the 8-37 fragment of islet amyloid polypeptide on insulin release from perifused rat islets

Diabetes, 1993
IAPP, or amylin, is a 37-amino acid peptide that is co-secreted with insulin from the pancreatic β-cells. We have determined the effects of IAPP and the antagonist 8–37 fragment of IAPP on the secretion of insulin from isolated rat islets studied in a perifusion system. Insulin secretion was stimulated by 8 mM glucose and 0.2 μM carbachol. IAPP at 10−7
Z L, Wang   +5 more
openaire   +2 more sources

The Inhibitory Effect of Hydroxylated Carbon Nanotubes on the Aggregation of Human Islet Amyloid Polypeptide Revealed by a Combined Computational and Experimental Study.

ACS Chemical Neuroscience, 2018
Fibrillar deposits formed by the aggregation of the human islet amyloid polypeptide (hIAPP) are the major pathological hallmark of type 2 diabetes mellitus (T2DM). Inhibiting the aggregation of hIAPP is considered the primary therapeutic strategy for the
Y. Mo   +6 more
semanticscholar   +1 more source

Amyloid protein in somatostatinoma differs from human islet amyloid polypeptide

Acta Endocrinologica, 1991
Abstract. Amyloid deposits in somatostatinomas are rare observations. To examine the characteristics of this amyloid, we compared amyloid deposits in a somatostatinoma to those found in pancreatic tissue in patients with Type II diabetes mellitus and in insulinomas, using immunohistochemical techniques and specific antibodies to islet amyloid ...
H, Ohsawa   +8 more
openaire   +2 more sources

Amyloidogenicity and cytotoxicity of islet amyloid polypeptide

Biopolymers, 2001
Insoluble amyloid formation by islet amyloid polypeptide (IAPP) in the islets of Langerhans of the pancreas is a major pathophysiological feature of noninsulin dependent diabetes mellitus (NIDDM) or type II diabetes. Because in vivo formed amyloid colocalizes with areas of cell degeneration and IAPP amyloid aggregates are cytotoxic per se, the process ...
openaire   +2 more sources

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

Diabetes, 2001
Islet amyloid polypeptide (IAPP) (amylin) is the unique peptide component of the amyloid deposits found at autopsy in >90% of subjects with type 2 diabetes (1). These amyloid deposits are thought to replace islet mass and to thereby contribute to the -cell dysfunction of the disease.
R L, Hull   +5 more
openaire   +2 more sources

Transgenic Overproduction of Islet Amyloid Polypeptide (Amylin) is Not Sufficient for Islet Amyloid Formation

Hormone and Metabolic Research, 1997
Islet amyloid polypeptide forms islet amyloid deposits in non-insulin-dependent diabetes mellitus. We have generated transgenic mice which express human islet amyloid polypeptide in their pancreatic beta cells yet do not develop islet amyloid deposits despite producing levels of the amyloidogenic human peptide 2 - 3 fold higher than the native (mouse ...
C B, Verchere   +4 more
openaire   +2 more sources

Leptin regulation of islet amyloid polypeptide secretion from mouse pancreatic islets

Biochemical Pharmacology, 1998
Leptin receptors are expressed in pancreatic beta-cells. However, leptin's role in islet hormone secretion is essentially unknown. In the present study, we aimed to elucidate leptin's effect on isolated pancreatic NMRI mouse islets by examining islet amyloid polypeptide (IAPP) and insulin secretion in acute experiments and after 48-hr exposure to ...
E, Karlsson, M, Stridsberg, S, Sandler
openaire   +2 more sources

ISLET AMYLOID POLYPEPTIDE

The Lancet, 1987
P, Westermark, E, Wilander, K H, Johnson
openaire   +2 more sources

Formation of islet amyloid from islet amyloid polypeptide

Biochemical Society Transactions, 1993
A, Clark, E J, de Koning, J F, Morris
openaire   +2 more sources

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