@article{476a7e10865011dda5a8000ea68e967b,
title = "Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9",
abstract = "Matrix metalloproteinase 9 (MMP-9), also known as 92-kDa gelatinase/type IV collagenase, is secreted from neutrophils, macrophages, and a number of transformed cells in zymogen form. Here we report that matrix metalloproteinase 3 (MMP-3/stromelysin) is an activator of the precursor of matrix metalloproteinase 9 (proMMP-9). MMP-3 initially cleaves proMMP-9 at the Glu40-Met41 bond located in the middle of the propeptide to generate an 86-kDa intermediate. Cleavage of this bond triggers a change in proMMP-9 that renders the Arg87-Phe88 bond susceptible to the second cleavage by MMP-3, resulting in conversion to an 82-kDa form. alpha 2-Macroglobulin binding studies of partially activated MMP-9 demonstrate that the 82-kDa species is proteolytically active, but not the initial intermediate of 86 kDa. This stepwise activation mechanism of proMMP-9 is analogous to those of other members of the MMP family, but the action of MMP-3 on proMMP-9 is the first example of zymogen activation that can be triggered by another member of the MMP family. The results imply that MMP-3 may be an effective activator of proMMP-9 in vivo.",
keywords = "Amino Acid Sequence, Cell Line, Electrophoresis, Polyacrylamide Gel, Enzyme Activation, Enzyme Precursors, Humans, Matrix Metalloproteinase 3, Matrix Metalloproteinase 9, Metalloendopeptidases, Microbial Collagenase, Molecular Sequence Data, alpha-Macroglobulins",
author = "Y Ogata and Enghild, {J J} and H Nagase",
year = "1992",
language = "English",
volume = "267",
pages = "3581--4",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "6",
}