HOME HELP FEEDBACK 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 Email this article to a friend 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 Shemer, J. Articles by LeRoith, D. Search for Related Content PubMed PubMed Citation Articles by Shemer, J. Articles by LeRoith, D. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 262, Issue 16, 7693-7699, 06, 1987

Insulin-like growth factor I receptors in neuronal and glial cells. Characterization and biological effects in primary culture

J Shemer, MK Raizada, BA Masters, A Ota and D LeRoith

Primary cultures of neuronal and glial cells from 1-day-old neonatal rats contain high affinity receptors for insulin-like growth factor I (IGF-I). The IC50 for displacement of 125I-IGF-I binding by unlabeled IGF-I was 3 nM for neuronal cells and 4 nM for glial cells. Unlabeled insulin was 20-50 times less potent. Apparent molecular mass of the alpha subunits of the IGF-I receptor was 125 kDa in neuronal and 135 kDa in glial cells. IGF-I induced autophosphorylation of the IGF-I receptor beta subunit in lectin-purified membrane preparations in a dose-dependent manner. The major phosphoamino acid of the beta subunit in both cell types was tyrosine in the IGF-I-stimulated state and serine in the basal state. Apparent molecular mass of the beta subunits of the IGF-I receptors was 91 kDa for neuronal and 95 kDa for glial cells. Tyrosine kinase activity of the IGF-I receptors was demonstrated by IGF-I-induced phosphorylation of the exogenous substrate poly(Glu, Tyr) 4:1 in both cell types. IGF-I had no effect on 2-deoxyglucose uptake in neuronal cells. In contrast, in glial cells, IGF-I stimulated 2-deoxyglucose uptake at very high doses, presumably acting via the insulin receptor. The effect of IGF-I as a neurotrophic growth factor in both neuronal and glial cells was demonstrated by its stimulation of [3H]thymidine incorporation. These findings suggest the IGF-I is an important growth factor in nervous tissue-derived cells.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				M. García-de Lacoba, C. Alarcón, E. J. de la Rosa, and F. de Pablo Insulin/Insulin-Like Growth Factor-I Hybrid Receptors with High Affinity for Insulin Are Developmentally Regulated during Neurogenesis Endocrinology, January 1, 1999; 140(1): 233 - 243. [Abstract] [Full Text]

				Y. Arsenijevic and S. Weiss Insulin-Like Growth Factor-I Is a Differentiation Factor for Postmitotic CNS Stem Cell-Derived Neuronal Precursors: Distinct Actions from Those of Brain-Derived Neurotrophic Factor J. Neurosci., March 15, 1998; 18(6): 2118 - 2128. [Abstract] [Full Text] [PDF]

				S. Kar, D. Seto, S. Dore, U.-K. Hanisch, and R. Quirion Insulin-like growth factors-I and -II differentially regulate endogenous acetylcholine release from the rat hippocampal formation PNAS, December 9, 1997; 94(25): 14054 - 14059. [Abstract] [Full Text] [PDF]

				V. A. Blakesley, H. Kato, C. T. Roberts Jr., and D. LeRoith Mutation of a Conserved Amino Acid Residue (Tryptophan 1173) in the Tyrosine Kinase Domain of the IGF-I Receptor Abolishes Autophosphorylation but Does Not Eliminate Biologic Function J. Biol. Chem., February 10, 1995; 270(6): 2764 - 2769. [Abstract] [Full Text] [PDF]