| Literature DB >> 11278559 |
J D Sandy1, J Westling, R D Kenagy, M L Iruela-Arispe, C Verscharen, J C Rodriguez-Mazaneque, D R Zimmermann, J M Lemire, J W Fischer, T N Wight, A W Clowes.
Abstract
Mature human aorta contains a 70-kDa versican fragment, which reacts with a neoepitope antiserum to the C-terminal peptide sequence DPEAAE. This protein therefore appears to represent the G1 domain of versican V1 (G1-DPEAAE(441)), which has been generated in vivo by proteolytic cleavage at the Glu(441)-Ala(442) bond, within the sequence DPEAAE(441)-A(442)RRGQ. Because the equivalent aggrecan product (G1-NITEGE(341)) and brevican product (G1-EAVESE(395)) are generated by ADAMTS-mediated cleavage of the respective proteoglycans, we tested the capacity of recombinant ADAMTS-1 and ADAMTS-4 to cleave versican at Glu(441)-Ala(442). Both enzymes cleaved a recombinant versican substrate and native human versican at the Glu(441)-Ala(442) bond and the mature form of ADAMTS-4 was detected by Western analysis of extracts of aortic intima. We conclude that versican V1 proteolysis in vivo can be catalyzed by one or more members of the ADAMTS family of metalloproteinases.Entities:
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Year: 2001 PMID： 11278559 DOI： 10.1074/jbc.M009737200
Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157