Matrikines in the regulation of extracellular matrix degradation.
The term "matrikines" was coined for designating peptides liberated by partial proteolysis of extracellular matrix macromolecules, which are able to regulate cell activities. Among these peptides, some of them may modulate proliferation, migration, protease production, or apoptosis. In this review, we summarize the activity of matrikines derived from elastin and interstitial or basement membrane collagens on the regulation of matrix metalloproteinases expression and/or activation, and on the plasminogen/plasmin system. Due to their activity, matrikines may play a significant role in physiological or pathological processes such as wound healing or tumor invasion.
Maquart
F X
FX
Laboratory of Biochemistry and Molecular Biology, CNRS UMR 6198, IFR 53, Faculté de Médecine, Reims, France. fmaquart@chu-reims.fr
Bellon
G
G
Pasco
S
S
Monboisse
J C
JC
D000818:Animals; D001485:Basement Membrane / Q000378:metabolism; D003094:Collagen / Q000378:metabolism; D004549:Elastin / Q000378:metabolism; D004789:Enzyme Activation; D005109:Extracellular Matrix / Q000378:metabolism*; D005341:Fibrinolysin / Q000378:metabolism; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D020782:Matrix Metalloproteinases / Q000235:genetics / Q000378:metabolism; D008954:Models, Biological; D009361:Neoplasm Invasiveness / Q000473:pathology; D010447:Peptide Hydrolases / Q000378:metabolism; D010455:Peptides / Q000378:metabolism*; D014945:Wound Healing / Q000502:physiology
D010455:Peptides; D003094:Collagen; D004549:Elastin; D010447:Peptide Hydrolases; D005341:Fibrinolysin; D020782:Matrix Metalloproteinases