Reactivity of IGF binding protein-3 isoforms towards concanavalin A in healthy adults and subjects with cirrhosis
Апстракт
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 glycosy...lation 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.
Извор:
Addiction Biology, 2003, 8, 1, 81-88Издавач:
- Carfax Publishing, Basingstoke
DOI: 10.1080/1355621031000069927
ISSN: 1355-6215
PubMed: 12745420
WoS: 000181603600011
Scopus: 2-s2.0-0037360212
Колекције
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Nedić, Olgica AU - Nikolić, J. A. AU - Prisic, S AU - Aćimović, Jelena M. AU - Hajdukovic-Dragojlovic, L PY - 2003 UR - https://cherry.chem.bg.ac.rs/handle/123456789/543 AB - 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. PB - Carfax Publishing, Basingstoke T2 - Addiction Biology T1 - Reactivity of IGF binding protein-3 isoforms towards concanavalin A in healthy adults and subjects with cirrhosis VL - 8 IS - 1 SP - 81 EP - 88 DO - 10.1080/1355621031000069927 ER -
@article{ author = "Nedić, Olgica and Nikolić, J. A. and Prisic, S and Aćimović, Jelena M. and Hajdukovic-Dragojlovic, L", year = "2003", abstract = "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.", publisher = "Carfax Publishing, Basingstoke", journal = "Addiction Biology", title = "Reactivity of IGF binding protein-3 isoforms towards concanavalin A in healthy adults and subjects with cirrhosis", volume = "8", number = "1", pages = "81-88", doi = "10.1080/1355621031000069927" }
Nedić, O., Nikolić, J. A., Prisic, S., Aćimović, J. M.,& Hajdukovic-Dragojlovic, L.. (2003). Reactivity of IGF binding protein-3 isoforms towards concanavalin A in healthy adults and subjects with cirrhosis. in Addiction Biology Carfax Publishing, Basingstoke., 8(1), 81-88. https://doi.org/10.1080/1355621031000069927
Nedić O, Nikolić JA, Prisic S, Aćimović JM, Hajdukovic-Dragojlovic L. Reactivity of IGF binding protein-3 isoforms towards concanavalin A in healthy adults and subjects with cirrhosis. in Addiction Biology. 2003;8(1):81-88. doi:10.1080/1355621031000069927 .
Nedić, Olgica, Nikolić, J. A., Prisic, S, Aćimović, Jelena M., Hajdukovic-Dragojlovic, L, "Reactivity of IGF binding protein-3 isoforms towards concanavalin A in healthy adults and subjects with cirrhosis" in Addiction Biology, 8, no. 1 (2003):81-88, https://doi.org/10.1080/1355621031000069927 . .