Activation of human neutrophils by type I collagen. Requirement of two different sequences

Author:

Monboisse J C1,Bellon G1,Randoux A1,Dufer J2,Borel J P1

Affiliation:

1. Laboratory of Biochemistry, CNRS URA 610, UFR Medicine, 51 rue Cognacq-Jay, F51095 Reims Cedex, France.

2. Laboratory of Hematology, Institut Jean Godinot, 45 rue Cognacq-Jay, F51062 Reims Cedex, France.

Abstract

Contact between type I collagen purified from several species and human polymorphonuclear neutrophils (PMNs) triggers the production of O2.- by these cells. The activity of collagen is located in the alpha 1(I)-CB6 cyanogen bromide-cleaved (CB)-peptide, which is the C-terminal CB-peptide of the alpha 1(I) chain. Experiments based on the competitive inhibition of O2.- production by simultaneous incubation of PMNs with type I collagen and synthetic peptides identical to the conserved sequences of this collagen demonstrated that the binding of collagen to PMNs and the subsequent activation of these cells depend on the simultaneous presence of two sequences: Arg-Gly-Asp [residues 915, 916 and 917 of the complete alpha 1(I) chain, located in the helical part] Asp-Gly-Gly-Arg-Tyr-Tyr (residues 1034-1039, located in the C-terminal non-helical telopeptide).

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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