title: Elastin as a matrikine.
abstract: The fact that elastin peptides, the degradation products of the extracellular matrix protein elastin, are chemotactic for numerous cell types, promote cell cycle progression and induce release of proteolytic enzymes by stromal and cancer cells, strongly suggests that their presence in tissues could contribute to tumour progression. Thus, elastin peptides qualify as matrikines, i.e. peptides originating from the fragmentation of matrix proteins and presenting biological activities. After a brief description of their origin, the biological activities of these peptides are reviewed, emphasising their potential role in cancer. The nature of their receptor and the signalling events it controls are also discussed. Finally, the structural selectivity of the elastin complex receptor is presented, leading to the concept of elastokine (matrikine originating from elastin fragmentation) and morpho-elastokine, i.e. peptides presenting a conformation similar to that of bioactive elastin peptides and mimicking their effects.
authors.affiliation: Université de Reims Champagne Ardenne, IFR53 Biomolécules, UFR Sciences Exactes et Naturelles, FRE CNRS 2534, Moulin de la Housse, BP 1039, 51687 Reims Cedex 2, France.
authors.forename: Laurent
authors.initials: L
authors.lastname: Duca
authors.forename: Nicolas
authors.initials: N
authors.lastname: Floquet
authors.forename: Alain J P
authors.initials: AJ
authors.lastname: Alix
authors.forename: Bernard
authors.initials: B
authors.lastname: Haye
authors.forename: Laurent
authors.initials: L
authors.lastname: Debelle
mesh_terms: D004549:Elastin / Q000378:metabolism*; D009369:Neoplasms / Q000378:metabolism; D010455:Peptides / Q000502:physiology*; D011956:Receptors, Cell Surface / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology*; D013329:Structure-Activity Relationship
chemical_list: D010455:Peptides; D011956:Receptors, Cell Surface; C054901:elastin-binding proteins; D004549:Elastin