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, cathepsin B, also generate this epitope, suggesting that it should no longer be considered as an exclusive marker of metalloproteinase activity.
Mort
J S
JS
Joint Diseases Laboratory, Shriners Hospital for Children and Department of Surgery, McGill University, 1529 Cedar Avenue, Montreal, Quebec, Canada H3G 1A6. jmort@shriners.mcgill.ca
Magny
M C
MC
Lee
E R
ER
D053674:Aggrecans; D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D002401:Cathepsin B / Q000378:metabolism*; D056668:Cathepsin L; D002403:Cathepsins / Q000378:metabolism; D011508:Chondroitin Sulfate Proteoglycans / Q000737:chemistry / Q000378:metabolism; D003546:Cysteine Endopeptidases; D010450:Endopeptidases; D000939:Epitopes / Q000032:analysis / Q000737:chemistry; D016326:Extracellular Matrix Proteins; D006801:Humans; D037181:Lectins, C-Type; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000276:immunology; D011509:Proteoglycans / Q000737:chemistry / Q000378:metabolism*; D051381:Rats; D011994:Recombinant Proteins / Q000378:metabolism
C508321:Acan protein, rat; D053674:Aggrecans; D000906:Antibodies; D011508:Chondroitin Sulfate Proteoglycans; D000939:Epitopes; D016326:Extracellular Matrix Proteins; D037181:Lectins, C-Type; D010446:Peptide Fragments; D011509:Proteoglycans; D011994:Recombinant Proteins; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D002401:Cathepsin B; C534281:CTSL protein, human; D056668:Cathepsin L; C534280:Ctsl protein, rat