The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Stromelysin-1 (MMP-3)-independent gelatinase expression and activation in mice.

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.[1]


  1. Stromelysin-1 (MMP-3)-independent gelatinase expression and activation in mice. Lijnen, H.R., Silence, J., Van Hoef, B., Collen, D. Blood (1998) [Pubmed]
WikiGenes - Universities