help button home button Endocrine Society Endocrinology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Request Copyright Permission
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ashkenazi, A.
Right arrow Articles by Gertler, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ashkenazi, A.
Right arrow Articles by Gertler, A.

Endocrinology, Vol 121, 414-419, Copyright © 1987 by Endocrine Society

ARTICLES

Comparative study of in vitro and in vivo modulation of lactogenic and somatotropic receptors by native human growth hormone and its modified analog prepared by recombinant deoxyribonucleic acid technology

A Ashkenazi, T Vogel, I Barash, D Hadari, A Levanon, M Gorecki and A Gertler

A modified analog of human GH (hGH), prepared by recombinant DNA technology, that lacks 13 amino acids at the amino terminus (Met14hGH), was able to compete with [125I]hGH for binding to lactogenic receptors in Nb2-11C rat lymphoma cells, to somatotropic receptors in IM-9 human lymphocytes, and to both lactogenic and somatotropic receptors in the microsomal fraction of virgin female rat liver. Exposure of intact Nb2 or IM-9 cells to Met14hGH did not reduce the number of surface or intracellular receptors, as compared to the control without hormone. A parallel exposure to 500-fold lower concentrations of hGH resulted in 77-93% reduction in both surface and intracellular receptors. In contrast to [125I]hGH, [125I]Met14hGH was not taken up by the intact Nb2 lymphoma cells. Infusion of anesthetized female virgin rats for 3 h with hGH down-regulated both lactogenic and somatotropic receptors in the liver. A similar infusion with up to 200-fold higher amounts of Met14hGH did not lower the number of total receptors, indicating lack of down-regulation. Some decrease in the binding to free receptors was observed, suggesting that Met14hGH is capable of binding to liver receptors in vivo.


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
D. Vashdi-Elberg, N. R. Staten, E. Sakal, R. E. McKinnie, J. Djiane, G. G. Krivi, and A. Gertler
Selective Modification of Recombinant Bovine Placental Lactogen by Site-directed Mutagenesis at Its C Terminus
J. Biol. Chem., March 8, 1996; 271(10): 5558 - 5564.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
B. Cunningham, P Jhurani, P Ng, and J. Wells
Receptor and antibody epitopes in human growth hormone identified by homolog-scanning mutagenesis
Science, March 10, 1989; 243(4896): 1330 - 1336.
[Abstract] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Endocrinology Endocrine Reviews J. Clin. End. & Metab.
Molecular Endocrinology Recent Prog. Horm. Res. All Endocrine Journals
Copyright © 1987 by The Endocrine Society