Synthesis of an insulin-like compound consisting of the A chain of insulin and a B chain corresponding to the B domain of human insulin-like growth factor I

An insulin-like hybrid molecule consisting of the A chain of insulin and a B chain corresponding to the B domain of human insulin-like growth factor I (growth factor I sequence 1-30) has been synthesized essentially by the procedures developed in this laboratory for the synthesis of insulin and anal...

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Bibliographic Details
Published in:Biochemistry (Easton) 1985-07, Vol.24 (15), p.4208-4214
Main Authors: Joshi, Satish, Burke, G. Thompson, Katsoyannis, Panayotis G.
Format: Article
Language:English
Subjects:
Adipose Tissue - drug effects
Adipose Tissue - metabolism
Amino Acid Sequence
Amino Acids - analysis
Aminoacids, peptides. Hormones. Neuropeptides
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Cattle
Cell Membrane - metabolism
Fundamental and applied biological sciences. Psychology
Humans
Insulin - chemical synthesis
Insulin - pharmacology
Insulin-Like Growth Factor I - chemical synthesis
Lipids - biosynthesis
Liver - metabolism
Macromolecular Substances
Peptide Fragments
Protein Multimerization
Proteins
Rats
Receptor, Insulin - metabolism
Somatomedins - chemical synthesis
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Summary:An insulin-like hybrid molecule consisting of the A chain of insulin and a B chain corresponding to the B domain of human insulin-like growth factor I (growth factor I sequence 1-30) has been synthesized essentially by the procedures developed in this laboratory for the synthesis of insulin and analogues. The hybrid competed with 125I-insulin for insulin receptors in rat liver plasma membranes and was a full agonist in stimulating incorporation of [3(-3)H]glucose into lipids in rat adipocytes. In both assays, the compound displayed ca. 2% of the potency of insulin. The compound was recognized by anti-insulin antibodies but was only ca. 0.25% as potent as insulin in this activity. The hybrid exhibited growth-promoting activity in fibroblasts, displaying 3-8% of the activity of insulin. In contrast, the compound was recognized by insulin-like growth factor carrier proteins, a property not associated with insulin. Two points of nonhomology between the B chain of insulin and the B domain of insulin-like growth factor I are considered in connection with these observations.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00336a059