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Proteolytic activation of the precursor of membrane type 1 matrix metalloproteinase by human plasmin
Author(s) -
Okumura Yuushi,
Sato Hiroshi,
Seiki Motoharu,
Kido Hiroshi
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01523-2
Subject(s) - plasmin , metalloproteinase , matrix metalloproteinase , chemistry , proteolytic enzymes , microbiology and biotechnology , biophysics , biochemistry , enzyme , biology
Membrane type 1 matrix metalloproteinase (MT1‐MMP) was suggested to play a critical role in the regulation of tissue invasion by normal and neoplastic cells by directly mediating the activation of pro‐gelatinase A. Recently, the proteolytic activation of a pro‐MT1‐MMP by an intracellular proprotein convertase, furin, was reported. In this study, we found that plasmin efficiently activates the pro‐MT1‐MMP by cleaving immediately downstream of Arg 108 and Arg 111 in the multi‐basic motif between its pro‐ and catalytic domains that participates in the activation of pro‐gelatinase A. Our present data suggest that pro‐MT1‐MMP transported to the plasma membrane is activated by plasmin extracellularly and thus it may play an important role in the matrix degradation process.