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Oxidative functions of polymorphonuclear neutrophils (PMNs), which play a deciding role in the phagocytosis process, are stimulated by extracellular matrix proteins such as type I collagen. Previous studies have demonstrated the involvement of a DGGRYY sequence located within the a1 chain C-terminal telopeptide in type I collagen-induced PMN activation, but so far the mechanism has not been completely elucidated. | ễFEBS Journal Involvement of lysine 1047 in type I collagen-mediated activation of polymorphonuclear neutrophils Stéphane Jaisson1 2 Herve Sartelet3 Corinne Perreau1 Charlotte Blanchevoye3 Roselyne Garnotel1 2 and Philippe Gillery1 2 1 Laboratory of Biochemistry and Molecular Biology Faculty of Medicine University of Reims Champagne Ardenne UMR CNRS n 6237 France 2 Laboratory of Pediatric Research and Biology American Memorial Hospital CHU of Reims France 3 Laboratory of Biochemistry Faculty of Sciences University of Reims Champagne Ardenne UMR CNRS n 6237 France Keywords carbamylation lysine polymorphonuclear neutrophils reactive oxygen species type I collagen Correspondence S. Jaisson Laboratoire de Biochimie Medicale et Biologie Moleculaire CNRS UMR 6237 Faculte de Medecine 51 Rue Cognacq-Jay F-51095 Reims France Fax 33 3 26 78 38 82 Tel 33 3 26 78 75 63 E-mail stephane.jaisson@univ-reims.fr Received 8 February 2008 revised 21 March 2008 accepted 18 April 2008 doi 10.1111 j.1742-4658.2008.06474.x Oxidative functions of polymorphonuclear neutrophils PMNs which play a deciding role in the phagocytosis process are stimulated by extracellular matrix proteins such as type I collagen. Previous studies have demonstrated the involvement of a DGGRYY sequence located within the a1 chain C-terminal telopeptide in type I collagen-induced PMN activation but so far the mechanism has not been completely elucidated. We have recently demonstrated that collagen carbamylation i.e. post-translational binding of cyanate to lysine e-NH2 groups impairs PMN oxidative functions suggesting the potential involvement of lysine residues in this process. The present study was devoted to the identification of lysine residues involved in the collagen-induced activation of PMNs. The inhibition of PMN activation by collagen in the presence of 6-amino-hexanoic acid a structural analogue of lysine residues confirmed the involvement of specific lysine residues. Modification of lysine residues by .
