Recombinant human procathepsin S is capable of autocatalytic processing at neutral pH in the presence of glycosaminoglycans |
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Authors: | Vasiljeva Olga Dolinar Marko Pungercar Jerica Rozman Turk Vito Turk Boris |
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Institution: | Department of Biochemistry and Molecular Biology, Jozef Stefan Institute, Jamova 39, 1000 Ljubljana, Slovenia. |
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Abstract: | Cathepsin S is unique among mammalian cysteine cathepsins in being active and stable at neutral pH. We show that autocatalytic activation of procathepsin S at low pH is a bimolecular process that is considerably accelerated (approximately 20-fold) by glycosaminoglycans and polysaccharides such as dextran sulfate, chondroitin sulfates A and E, and dermatan sulfate through electrostatic interaction with the proenzyme. Procathepsin S is also shown to undergo autoactivation at neutral pH in the presence of dextran sulfate with t1/2 of approximately 20 min at pH 7.5. This novel property of procathepsin S may have implications in pathological conditions associated with the appearance of active cathepsins outside lysosomes. |
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Keywords: | Cathepsin Lysosomal cysteine protease Processing Autocatalytic activation Glycosaminoglycan Ionic strength |
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