help button home button Endocrine Society JCEM JCEM Call for Nominations for EIC
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Submit a related Letter to the Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
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 Misra, P.
Right arrow Articles by Rosenfeld, R. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Misra, P.
Right arrow Articles by Rosenfeld, R. G.

Journal of Clinical Endocrinology & Metabolism, Vol 63, 1400-1405, Copyright © 1986 by Endocrine Society

ARTICLES

Structural and immunological characterization of insulin-like growth factor II binding to IM-9 cells

P Misra, RL Hintz and RG Rosenfeld

The structural and immunological properties of the insulin-like growth factor II (IGF-II) receptor on IM-9 lymphoblasts were studied using a combination of competitive binding and affinity cross-linking techniques as well as with a panel of polyclonal and monoclonal antireceptor antibodies. Unlike IGF-II binding to the classical type II IGF receptor, [125I] IGF-II binding to IM-9 cells was potently inhibited not only by unlabeled IGF-II, but also by insulin (50% inhibition of binding at 2.5 and 1.5 nM, respectively). Affinity cross- linking of [125I] IGF-II to intact cells, followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, demonstrated that the overwhelming majority of IGF-II binding was to a type I receptor (apparent mol wt, greater than 300,000 unreduced and 135,000 reduced), with minimal binding to a type II receptor (apparent mol wt, 220,000 unreduced and 240,000 reduced). After preincubation with five different antireceptor antibodies, inhibition of [125I] IGF-II binding was comparable to inhibition of [125I]insulin binding. These studies demonstrate that in IM-9 cells, the majority of IGF-II binding is to a type I receptor with high affinity for both insulin and IGF-II. Whether this is an atypical insulin receptor or a unique type I receptor remains to be established.


This article has been cited by other articles:


Home page
 EndocrinologyHome page
M. Navarro, B. Barenton, V. Garandel, J. Schnekenburger, and H. Bernardi
Insulin-Like Growth Factor I (IGF-I) Receptor Overexpression Abolishes the IGF Requirement for Differentiation and Induces a Ligand-Dependent Transformed Phenotype in C2 Inducible Myoblasts
Endocrinology, December 1, 1997; 138(12): 5210 - 5219.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
R. Roth
Structure of the receptor for insulin-like growth factor II: the puzzle amplified
Science, March 11, 1988; 239(4845): 1269 - 1271.
[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 © 1986 by The Endocrine Society