PubMed · 2886827
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
1987-08-15. Looking inside arteries.. https://pubmed.ncbi.nlm.nih.gov/2886827/
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
The hypothesis that arterial wall remodeling permits accumulation of a large atherosclerotic burden before there is any detectable narrowing of the vessel lumen has received support from necropsy and intravascular ultrasound (IVUS) studies. In a series of transplant donors assessed by IVUS, coronary atheromas were found in 17% of those younger than 20 years, 37% of those aged 20 to 29 years, and 60% of those aged 30 to 39 years, whereas angiography results were negative in 97% of this population. Necropsy data indicate a similar age-related prevalence and suggest that atherosclerosis risk factors are operative from a very early age. The IVUS findings show that disease is characteristically diffuse and involves the entire arterial tree, with progression including formation of multiple, potentially rupture-prone plaques that are not associated with vessel stenosis. These findings indicate the need for aggressive and early systemic intervention that targets modifiable risk factors to reduce coronary artery disease morbidity and mortality in the general population.
Pro-matrix metalloproteinase-2 (pro-MMP-2) is expressed in vascular smooth muscle cells (SMCs). We report that activated coagulation factor X (FXa) induces the release of MMP-2 (65 kDa) from human SMCs. In addition, FXa cleaves pro-MMP-2 (72 kDa) into MMP-2. Pro-MMP-2 and MMP-2 were determined by gelatin zymography. MMP-2 was generated in conditioned medium containing pro-MMP-2 in a concentration-dependent fashion by FXa (3 to 100 nmol/L). FX at concentrations up to 300 nmol/L was ineffective. The conversion of pro-MMP-2 to MMP-2 was inhibited by a selective FXa inhibitor (DX-9065a) at 3 to 10 micromol/L. There was a concentration-dependent induction of an intermediate MMP-2 form (68 kDa) in lysates of FXa-treated cells. This indicates that cellular mechanisms are involved in FXa-induced conversion of pro-MMP-2. As a possible biological consequence of MMP-2 activation by FXa, DNA synthesis and matrix invasion of SMCs were determined. Both were stimulated by FXa and inhibited by the selective FXa inhibitor DX-9065a and the MMP inhibitor GM 6001 but not by hirudin or aprotinin. It is concluded that stimulation of SMCs by FXa increases the levels of MMP-2 in the extracellular space and that two different mechanisms are involved: release of active MMP-2 and cleavage of secreted pro-MMP-2. Both might contribute to the mitogenic potency of FXa and FXa-stimulated matrix invasion of SMCs.
Explore the source record for details and available documents.