title: Matricryptins derived from collagens and proteoglycans.
abstract: Controlled proteolysis of extracellular matrix components releases bioactive fragments or unmasks cryptic sites that play key roles in controlling various physio-pathological processes including angiogenesis, tissue remodeling, wound healing, inflammation, tumor growth, and metastasis. We review here the structure and mechanisms of release of i) the proteolytic fragments (matricryptins) cleaved from collagens, proteoglycans and glycosaminoglycans, and ii) the matricryptic sites existing in these molecules. The cell surface receptors and the signaling pathways they trigger to exert their biological activities is discussed with the major physio-pathological processes they control. Their involvement in autoimmune and inherited diseases is reported. Most matricryptins issued from collagens, proteoglycans and glycosaminoglycans exhibit anti-angiogenic and anti-tumor properties and their use as potential drugs and as potential disease markers is discussed. Perspectives for identifying the common structural features, if any, of the matricryptins and their use in combination with chemotherapy and radiotherapy in the treatment of cancer are presented.
authors.affiliation: Institut de Biologie et Chimie des Proteines, UMR 5086 CNRS - University Lyon 1, France. s.ricard-blum@ibcp.fr
authors.forename: Sylvie
authors.initials: S
authors.lastname: Ricard-Blum
authors.forename: Lionel
authors.initials: L
authors.lastname: Ballut
mesh_terms: D020533:Angiogenesis Inhibitors / Q000502:physiology; D000818:Animals; D000970:Antineoplastic Agents / Q000494:pharmacology; D002135:Calcium-Binding Proteins / Q000378:metabolism; D003094:Collagen / Q000378:metabolism*; D024042:Collagen Type I / Q000378:metabolism; D024043:Collagen Type II / Q000378:metabolism; D024141:Collagen Type IV / Q000378:metabolism; D043170:Collagen Type XVIII / Q000378:metabolism; D005109:Extracellular Matrix / Q000378:metabolism* / Q000473:pathology; D006025:Glycosaminoglycans / Q000378:metabolism; D019812:Heparan Sulfate Proteoglycans / Q000378:metabolism; D006801:Humans; D006820:Hyaluronic Acid / Q000378:metabolism; D020782:Matrix Metalloproteinases / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D009363:Neoplasm Proteins / Q000378:metabolism; D018919:Neovascularization, Physiologic; D010446:Peptide Fragments / Q000096:biosynthesis* / Q000378:metabolism / Q000627:therapeutic use; D011509:Proteoglycans / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000378:metabolism; D014945:Wound Healing / Q000502:physiology
chemical_list: D020533:Angiogenesis Inhibitors; D000970:Antineoplastic Agents; D002135:Calcium-Binding Proteins; D024042:Collagen Type I; D024043:Collagen Type II; D024141:Collagen Type IV; D043170:Collagen Type XVIII; D006025:Glycosaminoglycans; D019812:Heparan Sulfate Proteoglycans; D008869:Microtubule-Associated Proteins; D009363:Neoplasm Proteins; D010446:Peptide Fragments; D011509:Proteoglycans; D011956:Receptors, Cell Surface; C040072:chondrocalcin; C071927:perlecan; C076744:cytoplasmic linker protein 170; D006820:Hyaluronic Acid; D003094:Collagen; D020782:Matrix Metalloproteinases