Dual regulation of ligand binding by CD11b I domain. Inhibition of intercellular adhesion and monocyte procoagulant activity by a factor X-derived peptide.

The Journal of Biological Chemistry
M MesriD C Altieri

Abstract

The role of coagulation factor X as a ligand for CD11b/CD18 (Mac-1, alphaMbeta2) in leukocyte adhesion was investigated. A factor X peptide, (G)L238YQAKRFKV246(G), blocked ligand binding to CD11b/CD18 and prevented monocyte procoagulant activity. This peptide also inhibited monocytic THP-1 cell adhesion to tumor necrosis factor alpha-stimulated endothelium and blocked neutrophil migration through tumor necrosis factor alpha-activated endothelial cell monolayers. In contrast, other factor X-derived peptides were ineffective. Radiolabeled peptide (G)LYQAKRFKV(G) bound specifically and saturably to isolated recombinant CD11b I domain. Functionally, the factor X sequence (G)LYQAKRFKV(G) dose-dependently inhibited THP-1 cell attachment to intercellular adhesion molecule 1 (ICAM-1) transfectants (IC50 = approximately 50 microg/ml), indistinguishably from anti-CD18 monoclonal antibodies 60.3 and IB4. In contrast, peptide (G)LYQAKRFKV(G) failed to reduce binding of 125I-fibrinogen to immobilized CD11b I domain, which was abolished by the fibrinogen-derived peptide KYG190WTVFQKRLDGSV202. By Lineweaver-Burke analysis, peptide (G)LYQAKRFKV(G) inhibited factor X binding to CD11b/CD18 in a noncompetitive fashion, and intact factor X did not...Continue Reading

References

Mar 1, 1993·The Journal of Cell Biology·R C LandisN Hogg
May 1, 1994·The Journal of Experimental Medicine·G GrandalianoH E Abboud
Jan 1, 1995·Annual Review of Cell and Developmental Biology·M A SchwartzM H Ginsberg

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Citations

Feb 25, 2015·Journal of Molecular Recognition : JMR·Xin FuX Frank Zhang
Jan 30, 2004·Biophysical Journal·Elena B Lomakina, Richard E Waugh
Feb 13, 1999·The Journal of Biological Chemistry·D D HuJ W Smith

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