Reactivity of IGF binding protein-3 isoforms towards concanavalin A in healthy adults and subjects with cirrhosis
| Autor: | Ljiljana Hajduković-Dragojlović, Sla Ana Prišić, Olgica Nedić, Judith Anna Nikolić, Jelena M. Aćimović |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Adult
Gene isoform medicine.medical_specialty Alcoholic liver disease Glycosylation Proteolysis Medicine (miscellaneous) Ligands DNA-binding protein 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Insulin-Like Growth Factor II Liver Cirrhosis Alcoholic Internal medicine Concanavalin A medicine Humans Protein Isoforms 030304 developmental biology Pharmacology chemistry.chemical_classification 0303 health sciences medicine.diagnostic_test biology medicine.disease Psychiatry and Mental health Insulin-Like Growth Factor Binding Protein 3 Endocrinology chemistry 030220 oncology & carcinogenesis biology.protein Affinity electrophoresis Glycoprotein |
| Zdroj: | Addiction Biology |
| ISSN: | 1355-6215 |
| DOI: | 10.1080/1355621031000069927 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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