Matrix degrading proteins

Cathepsins are intracellular proteinases that reside within lysosomes or specific intracellular granules. Cathepsins are used to degrade proteins or pqffides that are internalised from the extracellular space. Some cathepsins such as cathepsin-G or cathepsin-K may be released from the cell to degrade specific extracellular matrix proteins. All cathepsins except cathepsin-G (serine) and cathepsin-D (aspartyl) are cysteine proteinases. 

Sulfated galactans may interact with numerous regulatory proteins affording inhibition of complement activation, of tumor cell adhesion to P-selectin, of several matrix-degrading enzymes, and so on.668-670 These features depend strongly on the... 

A number of methods are available today for investigating the various aspects of this process of matrix degradation and tissue invasion. Study of degradation aims to identify and quantitate at mRNA or protein level a series of markers involved in the disruption of ECM molecules. These markers— hydrolases, their activators, inhibitors, receptors, degradation products, etc.— may be found to be involved or even crucial to invasive and metastatic aggressiveness. 

Corticosteroids have antiangiogenic, antifibrotic, and antipermeability properties. The principle effects of steroids are stabilization of the blood-retinal barrier, resorption of exudation, and downregulation of inflammatory stimuli. Antiangiogenesis is a secondary effect felt to be mediated primarily by upregulation of extracellular matrix protein plasminogen activator inhibitor-1 (PAI-1) in vascular endothelial cells (18). This inhibits activation of plasmin and alters extracellular matrix degradation. 

Tissue inhibitor of metalloproteinase Matrix (interstitial connective tissue) metalloproteinase (degrades proteins with metal cofactor). 

Chen, W. T. (1996). Proteases associated with invadopodia, and their role in degradation of extracellular matrix. Enzyme. Protein. 49, 59-71. 

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