Limited proteolysis of αvβ3 integrin from human placenta

Lubkova O.N.1, Gureeva T.A.2, Solovyeva N.I.2, Dilakyan E.A.2, Belkin B.M.1

1. Hematological Scientific Center of the RAMS
2. Orekhovich Institute of Biomedical Chemistry RAMS
PubMed Id: 11204624
Year: 2000  Volume: 46  Issue: 5  Pages: 444-450
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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Lubkova O.N., Gureeva T.A., Solovyeva N.I., Dilakyan E.A., Belkin B.M. (2000) Voprosy meditsinskoi khimii, 46(5), 444-450.
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