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Title: Stromelysin-1 (MMP-3)-independent gelatinase expression and activation in mice
Authors: Lijnen, Roger ×
Silence, Jurgen
Van Hoef, Bertha
Collen, Desire #
Issue Date: Mar-1998
Series Title: Blood vol:91 issue:6 pages:2045-53
Abstract: A potential physiological role of stromelysin-1 (MMP-3) in the expression or activation of gelatinase A (MMP-2) or gelatinase B (MMP-9) in the wall of injured arteries was studied with the use of homozygous MMP-3-deficient (MMP-3-/-) mice. One week after perivascular electric injury of the carotid or femoral artery in wild-type (MMP-3+/+) or MMP-3-/- mice, 70 kD and 65 kD proMMP-2 levels were enhanced by twofold to fourfold, with corresponding increases of 20- to 40-fold for active 61 kD and 58 kD MMP-2, and of 10- to 80-fold for 94 kD proMMP-9. Active MMP-2 species represented approximately one third of the total MMP-2 concentration for both MMP-3+/+ and MMP-3-/- mice. Active 83 kD MMP-9 was not detected in noninjured carotid or femoral arteries, whereas one week after injury its contribution to the total MMP-9 level was 11% to 18% for MMP-3+/+ and MMP-3-/- mice. Immunostaining of arterial sections confirmed enhanced expression of both MMP-2 and MMP-9 after vascular injury. Double immunostaining showed colocalization of MMP-9 with macrophages in the adventitia, whereas MMP-2 was also detected mainly in the adventitia but failed to colocalize with smooth muscle cells. Cell culture experiments confirmed comparable ratios of active versus latent MMP-2 in skin fibroblasts and smooth muscle cells derived from MMP-3+/+ and MMP-3-/- mice. Addition of plasmin(ogen) did not significantly affect activation of proMMP-2. In MMP-3+/+ and MMP-3-/- macrophages, comparable levels of 94 kD proMMP-9 were detected, and plasmin(ogen)-mediated conversion to 83 kD MMP-9 was obtained in both genotypes. These data thus indicate that proMMP-2 activation may occur via a plasmin- and MMP-3-independent mechanism, whereas plasmin can directly activate proMMP-9 via a MMP-3-independent mechanism.
ISSN: 0006-4971
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular and Vascular Biology
× corresponding author
# (joint) last author

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