Literature DB >> 8877314

Amylin, amyloid and age-related disease.

G J Cooper1, C A Tse.   

Abstract

Amylin, a 37-amino acid peptide, is cosecreted with insulin from the beta-cells of the pancreatic islets in normal response to physiological stimuli. It is the major protein of islet amyloid, which is usually present in the pancreases of people with non-insulin-dependent (type II) diabetes mellitus. Amylin elicits potent effects on carbohydrate metabolism in rodent tissues, causing insulin resistance in skeletal muscle and liver. A close structural relationship exists between amylin and the 2 calcitonin gene-related peptides, which are widely distributed neuropeptides and potent vasodilators. These exert biological effects similar to those of amylin on the organs primarily responsible for the regulation of carbohydrate metabolism. All 3 peptides are thought to cause their biological actions by binding to similar cell surface receptors. This article reviews the field of amylin and its role in the physiological regulation of carbohydrate metabolism, and in disease mechanisms associated with insulin resistance in diabetes mellitus, impaired glucose tolerance and essential hypertension. Potential therapeutic applications are also discussed.

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Year:  1996        PMID: 8877314     DOI: 10.2165/00002512-199609030-00006

Source DB:  PubMed          Journal:  Drugs Aging        ISSN: 1170-229X            Impact factor:   3.923


  127 in total

1.  In vivo insulin resistance induced by amylin primarily through inhibition of insulin-stimulated glycogen synthesis in skeletal muscle.

Authors:  S Frontoni; S B Choi; D Banduch; L Rossetti
Journal:  Diabetes       Date:  1991-05       Impact factor: 9.461

2.  Islet amyloid polypeptide amide causes peripheral insulin resistance in vivo in dogs.

Authors:  R Sowa; T Sanke; J Hirayama; H Tabata; H Furuta; S Nishimura; K Nanjo
Journal:  Diabetologia       Date:  1990-02       Impact factor: 10.122

3.  Insulin resistance is a characteristic feature of primary hypertension independent of obesity.

Authors:  T Pollare; H Lithell; C Berne
Journal:  Metabolism       Date:  1990-02       Impact factor: 8.694

4.  Amylin-induced in vivo insulin resistance in conscious rats: the liver is more sensitive to amylin than peripheral tissues.

Authors:  S J Koopmans; A D van Mansfeld; H S Jansz; H M Krans; J K Radder; M Frölich; S F de Boer; D K Kreutter; G C Andrews; J A Maassen
Journal:  Diabetologia       Date:  1991-04       Impact factor: 10.122

5.  Inhibitory effect of rat amylin on the insulin responses to glucose and arginine in the perfused rat pancreas.

Authors:  R A Silvestre; E Peiró; P Dégano; P Miralles; J Marco
Journal:  Regul Pept       Date:  1990-10-29

6.  Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus.

Authors:  A Lorenzo; B Razzaboni; G C Weir; B A Yankner
Journal:  Nature       Date:  1994-04-21       Impact factor: 49.962

7.  Hyperamylinemia, hyperinsulinemia, and insulin resistance in genetically obese LA/N-cp rats.

Authors:  H J Huang; A A Young; J E Koda; O L Tulp; M J Johnson; G J Cooper
Journal:  Hypertension       Date:  1992-01       Impact factor: 10.190

8.  Amylin modulates beta-cell glucose sensing via effects on stimulus-secretion coupling.

Authors:  P K Wagoner; C Chen; J F Worley; I D Dukes; G S Oxford
Journal:  Proc Natl Acad Sci U S A       Date:  1993-10-01       Impact factor: 11.205

9.  Amyloidosis of the islets of Langerhans. A restudy of islet hyalin in diabetic and non-diabetic individuals.

Authors:  J C EHRLICH; I M RATNER
Journal:  Am J Pathol       Date:  1961-01       Impact factor: 4.307

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

Authors:  Z L Wang; W M Bennet; M A Ghatei; P G Byfield; D M Smith; S R Bloom
Journal:  Diabetes       Date:  1993-02       Impact factor: 9.461

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