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Effects of Amylin and the Amylin Agonist Pramlintide on Glucose Metabolism

Diabetic Medicine, 1997
Since the discovery of the pancreatic islet hormone amylin in 1987, its metabolic effects have been investigated in a number of studies in animals and humans. Data from some early animal studies suggested that amylin might be associated with the development of insulin resistance, but other studies found that amylin had no effect on insulin sensitivity.
O, Schmitz   +4 more
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Molecular physiology of amylin

Journal of Cellular Biochemistry, 1994
Amylin is a 37-amino acid peptide first isolated, purified, and characterized from the amyloid deposits in the pancrease of type 2 diabetics. It is synthesized and secreted primarily from pancreatic beta cells along with insulin. The ability of amylin to potently reduce insulin-stimulated incorporation of glucose into glycogen in skeletal muscle ...
R A, Pittner   +7 more
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Amylin: History and Overview

Diabetic Medicine, 1997
The presence of amyloid deposits in the pancreas was first described at the beginning of the 20th century. However, it was not until 1987 that the structure of the amylin molecule was identified. Amylin is a 37-amino-acid peptide hormone that is co-secreted with insulin by the pancreatic beta-cells in response to a nutrient stimulus. It is deficient in
B, Ludvik   +4 more
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Structure and biology of amylin

Trends in Pharmacological Sciences, 1993
Amylin is a recently discovered 37 amino acid peptide secreted into the bloodstream, along with insulin, from pancreatic beta-cells. It is about 50% identical to calcitonin gene-related peptides (CGRP alpha and CGRP beta) and structurally related to the calcitonins.
T J, Rink   +3 more
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Pramlintide (Amylin).

Current opinion in investigational drugs (London, England : 2000), 2001
Pramlintide is a human amylin analog, under development by Amylin (originally in collaboration with Johnson & Johnson), as an adjunct with insulin for the potential prevention of complications of type I diabetes, and as a single agent for type II diabetes [279804], [295121], [305454].
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Amylin and the Gastrointestinal Tract

Diabetic Medicine, 1997
There is increasing evidence that alterations in the rate of gastric emptying - both acceleration and slowing - are present in patients with diabetes mellitus. A number of different factors can influence the rate of gastric emptying. For example, a large meal volume, a high-fat meal, and the presence of high glucose concentrations will all slow the ...
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Understanding Amylin Receptors

2009
Amylin is a 37 amino acid peptide that is co-secreted with insulin from pancreatic β-cells following nutrient ingestion, acting to inhibit gastric emptying, feeding and insulin-stimulated glycogen synthesis. Amylin is a member of the calcitonin (CT) family of peptides, which include CT, CT gene-related peptides (CGRP) and adrenomedullin (AM).
Just, Rasmus   +4 more
openaire   +2 more sources

Functional study of amylin and regulation of amylin receptor

2010
Amylin, a 37 amino acid peptide secreted from pancreatic beta cells upon stimulation by meal/glucose, belongs to the family of the calcitonin or calcitonin gene-related peptide (CGRP) and shares up to 50% homology with CGRP, which is a well-documented pain-related peptide.
openaire   +1 more source

Amylin and amylin receptors in Alzheimer's disease

2020
Wen Fu, Jack H. Jhamandas
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Amylin analogues

2016
JUST RASMUS   +8 more
openaire   +6 more sources

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