Proteinase 3 hydrolysis of peptides derived from human elastin exon 24.
In normal and pathological tissues, elastin-derived peptides proceed of elastin degradation by polymorphonuclear leukocyte proteases: elastase, cathepsin G and proteinase 3. They were demonstrated to have a chemotactic activity, to promote cell proliferation and protease release, . . .. To be biologically active, their structures, which reflect elastase specificity, must adopt a beta-turn conformation which accommodate to the cell surface-located elastin binding protein. In this study, we establish that human elastin exon 24-derived peptides containing at least two repeated VGVAPG sequences are hydrolyzed by the proteinase 3 (Pr3). As shown by mass spectrometry analyses, the demonstrated cleavage sites are in agreement with previously reported Pr3 substrate specificity and its lengthy substrate binding site. The characterization of the Pr3-generated products indicate that they contain at least one GXXPG sequence known to stimulate cellular effects after binding to the elastin receptor.
Lombard
C
C
Laboratoire de Biochimie Analytique et Synthèse Bioorganique, UFR Chimie-Biochimie, Bâtiment Chevreul, Université Lyon 1, Villeurbanne, France.
Bouchu
D
D
Wallach
J
J
Saulnier
J
J
D004549:Elastin / Q000737:chemistry*; D005091:Exons; D006801:Humans; D006868:Hydrolysis; D053146:Myeloblastin; D009504:Neutrophils / Q000201:enzymology*; D010455:Peptides / Q000737:chemistry*; D012697:Serine Endopeptidases / Q000737:chemistry*; D013379:Substrate Specificity
D010455:Peptides; D004549:Elastin; D012697:Serine Endopeptidases; D053146:Myeloblastin