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Department of Clinical Chemistry, Bispebjerg Hospital, Copenhagen, Denmark [S. G.]; INSERM U 145, Faculté de Médicine, Université de Nice, Nice, France [R. B., A. K., E. V. O.]; and Department of Pathology, University of Uppsala, Uppsala, Sweden [B. W.]
Two types of receptors for insulin-like growth factors (IGFs) were characterized in glioma cell lines established from different human brain tumors of glial origin (astrocytoma grades III and IV) by competitive binding assay, affinity labeling, and protein phosphorylation. Type I IGF receptor is a heterodimer composed of 
-subunits (Mr 130,000), which bind IGF I and II with equal affinity, and of ß-subunits (Mr 98,000), which show tyrosine kinase activity and autophosphorylation stimulated by IGF I and II with equal potency. The type II IGF binding site is a monomer (Mr 250,000) which binds IGF II with 10 times higher affinity than IGF I. The cellular concentration of type II IGF binding site is about 2- to 5-fold higher than the amount of type I IGF receptor. The characteristics of the two types of IGF receptors in human glioma cell lines are similar to those described recently in fetal rat astrocytes. In contrast the type I IGF receptor in glioma cells is different from that studied previously in normal adult brain regarding the equal affinity for IGF I and II, and the higher molecular size of the -subunit (130,000 versus 115,000). It is suggested that glioma cells may represent a fetal cell type in tumor development of adult human brain. A role of IGF in malignant glioma has not yet been determined, but the presence of IGF receptors is a prerequisite for cellular actions of IGF.
1 This study was supported by grants from INSERM, France; NOVO Foundation, Denmark; the Danish Cancer Society; Fonden til Laegevidenskabens Fremme, Denmark; the Danish Medical Research Council; and the Swedish Cancer Society.
2 To whom requests for reprints should be addressed at Department of Clinical Chemistry, Bispebjerg Hospital, DK-2400 Copenhagen NV, Denmark.
Received 4/ 1/87. Revised 10/ 6/87. Accepted 10/13/87.
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