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Recognition of Fibrinogen by Leukocyte Integrins
Author(s) -
UGAROVA TATIANA P.,
YAKUBENKO VALENTIN P.
Publication year - 2001
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2001.tb03523.x
Subject(s) - integrin , beta (programming language) , integrin alpha m , alpha (finance) , fibrinogen , cd18 , alpha v beta 3 , cd11c , microbiology and biotechnology , cell adhesion , receptor , biology , immunology , immune system , vitronectin , biochemistry , cell , medicine , phenotype , gene , construct validity , nursing , patient satisfaction , computer science , programming language
A bstract : Numerous studies have provided evidence that fibrinogen plays a multifaceted role in the immune and inflammatory response. The ability of fibrinogen to participate in the inflammatory response depends on its specific interaction with leukocyte cell surface adhesion receptors, integrins. Two leukocyte integrins, α M β 2 (CD11b/CD18, Mac‐1) and α X β 2 (CD11c/CD18, p150,95), are the main fibrinogen receptors expressed on neutrophils, monocytes, macrophages and several subsets of lymphocytes. The recognition site for α M β 2 has been previously mapped to the carboxyl‐terminal globular γC domains (γ143–411) and two sequences, γ190–202 (P1) and γ377–395 (P2), were implicated as the putative binding sites. We now demonstrate that a second leukocyte integrin, α X β 2 , which is highly homologous to α M β 2 , mediates adhesion of the α X β 2 ‐bearing cells to the D fragment and to the recombinant γ‐module, γ143–411. Within the γC domain, α X β 2 may recognize P1 and P2 sequences since synthetic peptides duplicating these sequences effectively inhibits adhesion of the α X β 2 ‐expressing cells to the D fragment. In addition, neutrophil inhibitory factor, NIF, a potent inhibitor of α X β 2 , also inhibited α X β 2 ‐mediated cell adhesion. These data suggest that recognition of the γC domain of fibrinogen by α M β 2 and α X β 2 may have common structural requirements.