Fibroblasts degrade type I collagen, the major extracellular protein found in mammals,
during events ranging from bulk tissue resorption to invasion through the three-dimensional …

Pericellular degradation of interstitial collagens is a crucial event for cells to migrate through
the dense connective tissue matrices, where collagens exist as insoluble fibers. A key …

Vertebrate collagenases, matrix metalloproteinases (MMPs), cleave type I collagen at a
single helical locus. We show here that rodent interstitial collagenases (MMP-13), but not …

During tissue-invasive events, migrating cells penetrate type I collagen-rich interstitial
tissues by mobilizing undefined proteolytic enzymes. To screen for members of the matrix …

The proteolytic processing of collagen (collagenolysis) is critical in development and
homeostasis, but also contributes to numerous pathologies. Mammalian interstitial …

Every so often, a paper comes along that brings clarity to an issue. Clarity is not necessarily
a final resolution, but rather a conceptual framework for productively addressing that issue …

Degradation of collagen is important for the physiological remodeling of connective tissues
during growth and development as well as in wound healing, inflammatory diseases, and …

Members of the matrix metalloproteinase (MMP) family selectively cleave collagens in vivo.
However, the substrate structural determinants that facilitate interaction with specific MMPs …

Interstitial collagen mechanical and biological properties are altered by proteases that
catalyze the hydrolysis of the collagen triple-helical structure. Collagenolysis is critical in …

It is well established that the expression profiles of multiple and possibly redundant matrix-
remodeling proteases (eg, collagenases) differ strongly in health, disease, and …