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Recombinant human procathepsin S is capable of autocatalytic processing at neutral pH in the presence of glycosaminoglycans
Author(s) -
Vasiljeva Olga,
Dolinar Marko,
Pungerčar Jerica Rozman,
Turk Vito,
Turk Boris
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.12.093
Subject(s) - chemistry , dermatan sulfate , autocatalysis , glycosaminoglycan , cathepsin , chondroitin sulfate , biochemistry , cathepsin o , chondroitin , cathepsin a , dextran , cysteine , enzyme , biophysics , catalysis , biology
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 (∼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 t 1/2 of ∼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.