Cathepsin B: an alternative protease for the generation of an aggrecan'metalloproteinase'cleavage neoepitope.
JS Mort, MC Magny, ER Lee - Biochemical Journal, 1998 - ncbi.nlm.nih.gov
JS Mort, MC Magny, ER Lee
Biochemical Journal, 1998•ncbi.nlm.nih.govPreviously, only matrix metalloproteinases were believed capable of cleaving the cartilage
proteoglycan, aggrecan, between Asn341 and Phe342, to yield a small G1 fragment
terminating in the residues VDIPEN. We show that the combined endo-and exopeptidase
activities of the cysteine protease, cathepsin B, also generate this epitope, suggesting that it
should no longer be considered as an exclusive marker of metalloproteinase activity.
proteoglycan, aggrecan, between Asn341 and Phe342, to yield a small G1 fragment
terminating in the residues VDIPEN. We show that the combined endo-and exopeptidase
activities of the cysteine protease, cathepsin B, also generate this epitope, suggesting that it
should no longer be considered as an exclusive marker of metalloproteinase activity.
Abstract
Previously, only matrix metalloproteinases were believed capable of cleaving the cartilage proteoglycan, aggrecan, between Asn341 and Phe342, to yield a small G1 fragment terminating in the residues VDIPEN. We show that the combined endo-and exopeptidase activities of the cysteine protease, cathepsin B, also generate this epitope, suggesting that it should no longer be considered as an exclusive marker of metalloproteinase activity.
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