Cathepsin B: an alternative protease for the generation of an aggrecan 'metalloproteinase' cleavage neoepitope
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, catheps...
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Veröffentlicht in: | Biochemical journal 1998-11, Vol.335 ( Pt 3) (3), p.491-494 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 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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ISSN: | 0264-6021 1470-8728 |
DOI: | 10.1042/bj3350491 |