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Reactivity of IGF binding protein‐3 isoforms towards concanavalin A in healthy adults and subjects with cirrhosis
Author(s) -
NEDIĆ OLGICA,
NIKOLIĆ JUDITH ANNA,
PRIŠIĆ SLA?ANA,
AĆIMOVIĆ JELENA,
HAJDUKOVIĆDRAGOJLOVIĆ LJILJANA
Publication year - 2003
Publication title -
addiction biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.445
H-Index - 78
eISSN - 1369-1600
pISSN - 1355-6215
DOI - 10.1080/1355621031000069927
Subject(s) - concanavalin a , glycosylation , glycoprotein , gene isoform , proteolysis , cirrhosis , blot , endocrinology , biology , biochemistry , lectin , medicine , follistatin , chemistry , gene , enzyme , in vitro
The capacity of the liver to synthesize insulin‐like growth factors (IGFs) and their binding proteins (IGFBPs) may be compromised by alcohol. The characteristics of IGFBP‐3 variants obtained from healthy individuals and patients with alcoholic cirrhosis (ALC) were compared. Concanavalin A (Con A) affinity electrophoresis and ligand blotting demonstrated that there was a gradual change in carbohydrate properties of putative IGFBP‐3 with progression of ALC from stages A to C. As many as 12 ionic species of IGFBP‐3 could be distinguished, corresponding probably to variously glycosylated and/or phosphorylated isoforms of the core protein. Three of them reacted significantly with the immobilized Con A, the pattern being altered in patients with ALC. Patients with ALC in stage B exhibited the presence of clearly differentiated IGFBP‐3 variants less and more Con A reactive, suggesting this stage to be a turning point with the most intensive changes in the IGF‐IGFBP system. Because the glycosylation pattern is tissue specific, pathological post‐translational modifications found for one glycoprotein (IGFBP‐3) are probably shared by others of the same tissue origin. This may affect their susceptibility to proteolysis and subsequently their function.