PURPOSE: Although matrix metalloproteinase (MMP) expression has been correlated with proliferation and migration of various tumor cells, the relation between MMP expression and smooth muscle cell (SMC) proliferation and migration has not been established. METHODS: We measured MMP expression (gelatin, casein, and elastin zymography) by vascular wall cells in balloon-injured carotid artery during the period of medial SMC proliferation, migration of SMC from the media to the intima, and subsequent intimal SMC proliferation. RESULTS: The 72 and 64-kd gelatinases (presumably 72 kd type IV collagenase or MMP 2) were constitutively expressed in normal carotid arteries, and the activated (59 and 54 kd) forms of this enzyme were increased at 5 days when SMCs start to migrate. A 92 kd gelatinase (presumably 92 kd type IV collagenase or MMP 9) was increased at 24 hours, when SMCs entered the growth cycle, and decreased thereafter. A low-molecular-weight metalloproteinase with elastolytic activity was present in the adventitia, and the activity was increased at 5 days after surgery. CONCLUSIONS: These results suggest that the 72 kd and 92 kd gelatinases may be involved in basement membrane and matrix degradation in the media in relation to SMC proliferation and migration, whereas the low-molecular-weight metalloproteinase may have a role in elastin turnover in the adventitia.
PURPOSE: Although matrix metalloproteinase (MMP) expression has been correlated with proliferation and migration of various tumor cells, the relation between MMP expression and smooth muscle cell (SMC) proliferation and migration has not been established. METHODS: We measured MMP expression (gelatin, casein, and elastin zymography) by vascular wall cells in balloon-injured carotid artery during the period of medial SMC proliferation, migration of SMC from the media to the intima, and subsequent intimal SMC proliferation. RESULTS: The 72 and 64-kd gelatinases (presumably 72 kd type IV collagenase or MMP 2) were constitutively expressed in normal carotid arteries, and the activated (59 and 54 kd) forms of this enzyme were increased at 5 days when SMCs start to migrate. A 92 kd gelatinase (presumably 92 kd type IV collagenase or MMP 9) was increased at 24 hours, when SMCs entered the growth cycle, and decreased thereafter. A low-molecular-weight metalloproteinase with elastolytic activity was present in the adventitia, and the activity was increased at 5 days after surgery. CONCLUSIONS: These results suggest that the 72 kd and 92 kd gelatinases may be involved in basement membrane and matrix degradation in the media in relation to SMC proliferation and migration, whereas the low-molecular-weight metalloproteinase may have a role in elastin turnover in the adventitia.
Authors: Ian Cummings; Sarah George; Jens Kelm; Doerthe Schmidt; Maximilian Y Emmert; Benedikt Weber; Gregor Zünd; Simon P Hoerstrup Journal: Eur J Cardiothorac Surg Date: 2012-01 Impact factor: 4.191