Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain

Amanda J. Fosang, Karena Last, Yutaka Fujii, Motoharu Seiki, Yasunori Okada

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

An aggrecan G1-G2 substrate was used to determine sites within the interglobular domain that were susceptible to cleavage by MT1-MMP. Degradation products were identified by Western blotting with neo-epitope antibodies specific for MMP-derived N- and C-terminal sequences. The results showed that MT1-MMP cleaved at the N341-F342 and D441-L442 bonds, as shown for other MMPs, and also at a site 13 amino acids C-terminal to the N341-F342 site. The G2 product of this additional cleavage was identified by sequence analysis and revealed an N-terminus commencing T355 VxxPDVELPLP. The data are consistent with MT1-MMP cleavage at three sites in the aggrecan interglobular domain; one at N342-F342, a second at D441-L442 and a third at Q354-T355.

Original languageEnglish
Pages (from-to)186-190
Number of pages5
JournalFEBS Letters
Volume430
Issue number3
DOIs
Publication statusPublished - 1998 Jul 3

Keywords

  • Aggrecan
  • Arthritis
  • Matrix metalloproteinase
  • Membrane-type matrix metalloproteinase
  • Neo-epitope

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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