Elastin as a matrikine.
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.
Duca
Laurent
L
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.
Floquet
Nicolas
N
Alix
Alain J P
AJ
Haye
Bernard
B
Debelle
Laurent
L
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
D010455:Peptides; D011956:Receptors, Cell Surface; C054901:elastin-binding proteins; D004549:Elastin