Evidence for fibronectin degradation by calpain II.

Recent work supports the hypothesis that calpain II can be exteriorized. Indeed, this cysteine calcium-dependent proteinase was shown to be intercellularly, and, more particularly, associated to extracellular matrix components. Thereby, calpain II could be involved in hydrolysis of pericellular matrix components such as fibronectin, which is known to play an important role in cellular differentiation. Our in vitro studies provide evidence that fibronectin is a potential substrate for calpain II. On cultured cells, our findings show that calpain II is able, on the one hand, to cleave the fibrillar network of fibronectin secreted by fibroblasts, and, on the other, to decrease dramatically the fibronectin amount secreted by myoblasts just before fusion. Moreover, following this treatment, myoblasts become spherical due to the cleavage of this attachment factor. However, these cells, plated on an appropriate substrate are still able to differentiate. Our results suggest that calpain II is indeed involved in myoblast fusion via the fibronectin cleavage since it is well established that myogenic lineages lose this glycoprotein at the time of fusion.