ECM

MMP24 is an extracellular matrix (ECM) degradative peptidase enzyme that is a member of the large family of matrix metalloproteinases (MMP). Each MMP has a different substrate specificity, and the aberrant or derailed expression of these is strongly correlated with unregulated events such as tumor invasion, metastasis, angiogenesis, and arthritis. This is in contrast to the tightly controlled normal physiological processes such as tissue remodeling, reproduction, rebuilding, and embryonic development. Deregulation often occurs through the loss of negative checks.

MMP2 is a peptidase enzyme that belongs to the large family of matrix metalloproteinases (MMPs) which degrade the extracellular matrix (ECM) with different substrate specificities. Aberrant and unregulated expression of MMPs via deregulation of key negative check controls is strongly associated with increased tumor invasiveness, metastasis potential, and angiogenesis. This uncontrolled behavior is in direct contrast to the tightly controlled physiological systems of embryonic development, tissue remodeling, and rebuilding.

Fibronectin is a glycoprotein found in the extracellular matrix (ECM) that binds to integrins and other components of the ECM such as collagen and fibrin. Under normal physiological conditions, fibronectin is an important factor in cell adhesion, growth, differentiation, and migration.

The extracellular matrix (ECM) is a well-structured composite of collagens, proteoglycans, glycoproteins, and growth factors proficient of generating variable measures of tissue tensile potency, from mucosal linings to bones. ECM predominantly comprises the cellular milieu outside the circulation and is established as having a major regulatory effect on cell activity.  There has been a considerable amount of attention towards the disparate conditions in which ECM unambiguously sends or alters signals to the surrounding cells.