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Structure and activity of the B-chain of insulin.
- Source :
-
Biochemistry international [Biochem Int] 1989 Feb; Vol. 18 (2), pp. 373-81. - Publication Year :
- 1989
-
Abstract
- Despentapeptide (B26-30)-insulinamide (B25) prepared by a semisynthetic procedure was found to have about 65% of the hypoglycaemic activity of natural insulin. In contrast, the binding of the modified insulin analogue to insulin specific receptors was markedly increased. The discrepancy between the loss of biological potency and the apparent increase in binding affinity for membrane receptors reveals that not all of the biological activity of insulin is regulated by the receptor-binding system. The tetrapeptidamide of the B-chain of insulin (Arg-Gly-Phe-Phe-NH2) was clearly shown to have both insulin-like and insulin-potentiating actions in vivo although it had no effect on insulin receptor function in vitro. Evidence suggests that the small peptide fragment of insulin may be internalized and acts at the post-binding site(s) of the glucose metabolic pathway in target tissues. The present data support the general concept that insulin may exert its complex molecular actions through internalized hormonal fragment as well as the transmembrane mediators generated from receptor binding.
- Subjects :
- Adipose Tissue metabolism
Animals
Blood Glucose metabolism
Glucose metabolism
Glycogen biosynthesis
In Vitro Techniques
Insulin analogs & derivatives
Insulin metabolism
Male
Muscles drug effects
Muscles metabolism
Peptide Fragments pharmacology
Rats
Receptor, Insulin metabolism
Structure-Activity Relationship
Insulin pharmacology
Subjects
Details
- Language :
- English
- ISSN :
- 0158-5231
- Volume :
- 18
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochemistry international
- Publication Type :
- Academic Journal
- Accession number :
- 2669756