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Journal of Biochemistry Advance Access published online on March 3, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn029
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© 2008 The Japanese Biochemical Society

Affinity Modulation of Human Placental Insulin and Insulin-Like Growth Factor Receptors by Lectins

Romana Masnikosa, Anna Nikolic and Olgica Nedic

INEP-Institute for the Application of Nuclear Energy, University of Belgrade, Banatska 31 b, 11080 Belgrade,381 Serbia

Corresponding author: Dr. Romana Masnikosa, INEP-Institute for the Application of Nuclear Energy, University of Belgrade, Banatska 31b, 11080 Belgrade, Serbiam, Tel.: (+) 381 11 617 252, Fax.: (+) 381 11 618 724, E-mail: romana{at}inep.co.yu, masnikosa_romana{at}yahoo.co.uk

Received February 14, 2008; Accepted February 25, 2008


  Abstract

The ability of plant lectins to modify the interactions of the insulin receptor (IR) and insulin-like growth factor (IGF) receptors (IGFRs) with their ligands was investigated. The lectins profoundly affected the competition binding curves for 125I-labelled IGF-I and insulin, causing an increase in the affinity of placental IGF1R and IR towards their ligands. This increment was of such a magnitude that it could affect the receptors' specificity towards these ligands. The lower the ligand concentration, the greater was the lectin-induced affinity shift, which suggests potential physiological significance of the effect. The affinity modulation ocurred in a lectin specific and dose-dependent manner. In contrast to IGF1R and IR, the binding of 125I-labelled IGF-II to its receptors resisted lectin modulation. Here we provide evidence of the possibility of external modulation of the affinity of placental IGF1R and IR via interactions of the receptors' carbohydrate moieties with lectins. The existence of modulators that would selectively inhibit or enhance the binding of IGFs or insulin to their corresponding receptors may have important implications for placental cell responses to these molecules.

Key Words: IGF1R, IR, WGA, Con A, PHA


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