Milagros Balbín

TL;DR: A cDNA coding for a new human matrix metalloproteinase (MMP) has been cloned from a cDNA library derived from a breast tumor, providing support to the hypothesis that the isolated cDNA codes for an authentic collagenase.

TL;DR: It is found that fibroblasts and cancer cells express an indistinguishable pericellular collagenolytic activity that allows them to traverse the ECM and that MT1-MMP serves as the major cell-associated proteinase necessary to confer normal or neoplastic cells with invasive activity.

TL;DR: A paradoxical protective role for Mmp8 in cancer is identified and a genetic model to evaluate the molecular basis of gender differences in cancer susceptibility is provided andBone marrow transplantation experiments confirmed that MMP8 supplied by neutrophils was sufficient to restore the natural protection against tumor development mediated by this protease in male mice.

TL;DR: In vivo evidence is provided that collagenase 3 is a target of the transcriptional activator Cbfa1 in these cells, and it is proposed that this enzyme may play a key role in the process of bone formation and remodeling.

TL;DR: Data indicate that MMP‐8 participates in wound repair by contributing to the resolution of inflammation and open the possibility to develop new strategies for treating wound healing defects.