Interstitial collagenase (MMP-1), gelatinase (MMP-2) and stromelysin (MMP-3) released by human fibroblasts cultured on acellular sarcoid granulomas (sarcoid matrix complex, SMC).

We studied collagenase, gelatinase and stromelysin syntheses by human fibroblasts cultured on three models of tridimensional matrix: native collagen sponge, native collagen complexed with glycosaminoglycans sponge, and acellular sarcoid matrix complex prepared from human sarcoid granulomas. Collagenase and stromelysin biosyntheses were differently stimulated according to culture conditions. Fibroblasts secreted a same amount of collagenase or stromelysin when cultured on collagen and collagen-glycosaminoglycans sponges, while collagenase and stromelysin secretions were widely amplified when cultured on sarcoid matrix complex. In contrast, gelatinase production was equally induced by the three culture conditions. In the different culture conditions on tridimensional matrix, the three matrix metalloproteinases were synthesized in a latent form. Thus, the sarcoid matrix complex stimulated the release of collagenase and stromelysin by fibroblast, but did not stimulate the release of gelatinase. This suggests that collagenase and stromelysin syntheses are co-regulated while gelatinase production is controlled by a distinct mechanism.