Voprosy meditsinskoi khimii (ISSN 0042-8809)

Limited proteolysis of avb3 integrin from human placenta

   


1. Hematological Scientific Center of the RAMS
2. Orekhovich Institute of Biomedical Chemistry RAMS
PubMed Id: 11204624
Year: 2000 vol: 46  issue:5  pages: 444-450
Abstract: Purification of avb3 integrin from human placenta with successive usage of two affinity sorbents - immobilized monoclonal antibodies to avb3 integrin and immobilized RGD-containing decapeptid allowed to purify this integrin’s partially degraded fraction, that was nevertheless able to interact with its ligand. During the incubation of partially degraded avb3 integrin at 37°C its further degradation went on. Addition of serine proteinase inhibitors: (phenylmethilsulfonyl fluoride, leupeptin and aprotinin) completely suppressed integrin further degradation of avb3. In preparations of intact and partially degraded avb3 integrin specific activity of two serine proteinaes - urokinase and dipeptidilpeptidase IV - was discovered. avb3 integrin, undergoing limited proteolysis, had lesser affinity towards RGD peptide, thar intact integrin. The results show, that avb3 integin from human placenta co-purifies with serine proteinases. It is suggested that a definite part of functionally active avb3 integin, extracted from human placenta by triton X-100, forms a stable complex with serine proteinases
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Reference: Lubkova O.N., Gureeva T.A., Solovyeva N.I., Dilakyan E.A., Belkin B.M., Limited proteolysis of avb3 integrin from human placenta, Voprosy meditsinskoi khimii, 2000, vol: 46(5), 444-450.
References
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