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
Hauptverfasser: Mort, J S, Magny, M C, Lee, E R
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.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj3350491