[Limited proteolysis of integrin alpha v beta3 from human placenta].
Purification of alpha v beta 3 integrin from human placenta with successive usage of two affinity sorbents--immobilized monoclonal antibodies to alpha v beta 3 integrin and immobilized RGD-containing decapeptide allowed to purify this integrin's partially degraded fraction, that was nevertheless able to interact with its ligand. During the incubation of partially degraded alpha v beta 3 integrin at 37 degrees C its further degradation went on. Addition of serine proteinase inhibitors: (phenylmethilsulfonyl fluoride, leupeptin and aprotinin) completely suppressed integrin further degradation of alpha v beta 3. In preparations of intact and partially degraded alpha v beta 3 integrin specific activity of two serine proteinases--urokinase and dipeptidilpeptidase IV--was discovered. alpha v beta 3 integrin, undergoing limited proteolysis, had lesser affinity towards RGD peptide, that intact integrin. The results show, that alpha v beta 3 integrin from human placenta co-purifies with serine proteinases. It is suggested that a definite part of functionally active alpha v beta 3 integrin, extracted from human placenta by triton X-100, forms a stable complex with serine proteinases.
Lubkova
O N
ON
Hematological Scientific Center of the RAMS, 125167, Moscow, Novoyazikovskiy proyezd, 4a.
Gureeva
T A
TA
Dilakian
E A
EA
Solov'eva
N I
NI
Belkin
V M
VM
D005260:Female; D005456:Fluorescent Dyes; D006801:Humans; D006868:Hydrolysis; D009842:Oligopeptides / Q000378:metabolism; D010920:Placenta / Q000378:metabolism*; D011247:Pregnancy; D019030:Receptors, Vitronectin / Q000378:metabolism*
D005456:Fluorescent Dyes; D009842:Oligopeptides; D019030:Receptors, Vitronectin; C047981:arginyl-glycyl-aspartic acid
Ogranichennyĭ proteoliz integrina alpha v beta3 iz platsenty cheloveka.