HOME HELP CONTACT US SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bates, P. C. Articles by Holder, A. T. Search for Related Content PubMed PubMed Citation Articles by Bates, P. C. Articles by Holder, A. T.

Monoclonal antibody (MAb) to GH has been shown to increase the anabolic response induced by the hormone in individual tissues of dwarf mice. Dwarf mice were treated with GH at a low and a high dose (2·5 and 50 mU/day respectively), with and without complexing to an MAb. Treatment was for 7 and 14 days, at which times protein synthesis rates in skeletal muscle, liver and heart were determined from incorporation of labelled phenylalanine following injection of a flooding dose. The MAb potentiated the actions of GH and produced increases in the rates of protein synthesis in each of the tissues to a significantly greater extent than did GH alone.

The increase in protein synthesis rate induced by MAb appears to be mechanistically distinct from that observed by increasing the dose of GH. In skeletal muscle and liver there was a dose–response to the GH alone in terms of the RNA concentration, i.e. the capacity for protein synthesis, whereas in each tissue examined the MAb caused very little further response in the RNA concentration. The MAb-induced enhancement of protein synthesis rate was almost entirely due to an increase in the RNA activity, i.e. the efficiency of the synthesizing system.

Complexing GH to a particular MAb, or to antisera of restricted epitope specificity, has previously been shown to enhance the in-vivo effects of GH on whole body protein content; the mechanism for this enhancement has not been adequately determined. The present results suggest that the mechanism of MAb enhancement of GH activity is unlikely to be through prolonging GH action by increasing its serum half-life, but may be through effects on GH-receptor response, possibly through targeting of the GH to a particular receptor sub-type or through inhibition of internalization of the GH-receptor complex.

Journal of Endocrinology (1992) 132, 369–375

This article has been cited by other articles:

				V. Beauloye, S. M. Muaku, P. Lause, D. Portetelle, R. Renaville, A. R. Robert, J. M. Ketelslegers, and D. Maiter Monoclonal antibodies to growth hormone (GH) prolong liver GH binding and GH-induced IGF-I/IGFBP-3 synthesis Am J Physiol Endocrinol Metab, August 1, 1999; 277(2): E308 - E315. [Abstract] [Full Text] [PDF]

				M. J. Gahl, N. J. Benevenga, and T. D. Crenshaw Rates of Lysine Catabolism Are Inversely Related to Rates of Protein Synthesis When Measured Concurrently in Adult Female Rats Induced to Grow at Different Rates J. Nutr., September 1, 1998; 128(9): 1503 - 1511. [Abstract] [Full Text]