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1. A peptide hormone that is secreted along with insulin by the beta cells of the pancreas and helps to regulate blood sugar levels by inhibiting glucagon secretion and by slowing the rate at which food leaves the stomach.
2. Archaic Any of various components of starch.
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An, "Causative factors for formation of toxic islet amyloid polypeptide oligomer in type 2 diabetes mellitus," Clinical Interventions in Aging, vol.
Islet amyloid polypeptide in pancreatic islets from type 2 diabetic subjects.
Extra-pancreatic expression of the rat islet amyloid polypeptide (amylin) gene.
Raleigh, "Rifampicin does not prevent amyloid fibril formation by human islet amyloid polypeptide but does inhibit fibril thioflavin-T interactions: implications for mechanistic studies of [beta]-cell death," Biochemistry, vol.
Fasting plasma islet amyloid polypeptide (IAPP) was reported to be increased in patients with PC (1), and a soluble factor from PC cells was reported to stimulate IAPP secretion (2), suggesting the possibility of an increase of IAPP in the plasma of patients with PC.
[beta]-Cells are capable of producing chemokines (e.g., MCP1/CCL2) in the presence of high FFA levels, and hyperglycemia forces [beta]-cells to produce islet amyloid polypeptide (IAPP) [35, 75-77].
In addition to being the major regulator of the insulin gene, Pdx1 also regulates the expression of additional islet-specific genes through its interaction with their promoter regions, which include GLUT2, Nkx6.1, islet amyloid polypeptide and somatostatin (Babu et al., 2007).
Insulin resistance, lipotoxicity, glucotoxicity, and incretin defects, are four factors, however, which can be modified to improve beta cell function.1 Hypersecretion of islet amyloid polypeptide (IAPP), which is co-secreted with insulin, can lead to progressive b-cell failure as well.
Lundquist, "Islet amyloid polypeptide inhibits glucagon release and exerts a dual action on insulin release from isolated islets," Regulatory Peptides, vol.
Human islet amyloid polypeptide (hIAPP) or amylin is a 37-residue peptide hormone secreted from [beta]-cells within the islet of Langerhans in the pancreas.
The deposits were originally assumed to be composed of insulin, fragments of insulin, or proinsulin, but 85 years after Opie's initial observation two groups independently identified the major protein component of islet amyloid as a 37-residue polypeptide neuropancreatic hormone, now known as islet amyloid polypeptide (IAPP) or amylin [2, 3] (Figure 1).
It is only in 1987 that the major component of islet amyloids was identified as a 37-residue peptide, the islet amyloid polypeptide (IAPP) [15] or amylin [16].