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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Keywords: human placenta, avp3 integrin, proteolysis, serine proteinases
Citation:
Lubkova O.N., Gureeva T.A., Solovyeva N.I., Dilakyan E.A., Belkin B.M. (2000) Limited proteolysis of αvβ3 integrin from human placenta. Voprosy Meditsinskoi Khimii, 46(5), 444-450.
Lubkova O.N. et al. Limited proteolysis of αvβ3 integrin from human placenta // Voprosy Meditsinskoi Khimii. - 2000. - V. 46. -N 5. - P. 444-450.
Lubkova O.N. et al., "Limited proteolysis of αvβ3 integrin from human placenta." Voprosy Meditsinskoi Khimii 46.5 (2000): 444-450.
Lubkova, O. N., Gureeva, T. A., Solovyeva, N. I., Dilakyan, E. A., Belkin, B. M. (2000). Limited proteolysis of αvβ3 integrin from human placenta. Voprosy Meditsinskoi Khimii, 46(5), 444-450.
