Further characterisation of an IGF-I enhancing antibody: Actions on IGF-I-induced hypoglycaemia and interaction with the analogue LR 3 IGF-I

J. M. Pell, H. C. Flick-Smith, S. Dye, R. A. Hill

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

We have previously shown that a polyclonal anti-IGF-I antiserum administered together with IGF-I potentiates IGF-I activity in vivo. The anti-IGF-I antiserum has a modest affinity for IGF-I, similar to that for enhancing IGFBPs, and treated animals have significantly higher circulating IGF-I concentrations than their controls. Our recent findings have demonstrated that the anti-IGF-I activity decreases the clearance of IGF-I by at least 2-fold and that it abolishes the acute hypoglycaemic action of a single subcutaneous dose of IGF-I. Interestingly, we have been unable to demonstrate potentiation of the growth-promoting activity of the potent non-IGFBP binding IGF-I analogue LR 3 IGF-I, even though the analogue binds to the antiserum in vitro; rather native IGF-I/antibody complexes perform even better than LR 3 IGF-I. In IGF-I/antibody-treated dwarf rats, most IGF-I may be found in an uncharacterised high molecular weight antibody complex which is probably responsible for improved IGF-I performance. Thus, the anti-IGF-I antibody may be behaving in a similar manner to a high molecular weight IGFBP and is effective in potentiating IGF-I action in vivo.

Original languageEnglish
Pages (from-to)367-375
Number of pages9
JournalProgress in Growth Factor Research
Volume6
Issue number2-4
DOIs
Publication statusPublished - 1995

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