Journal article
The Lectin-like Domain of Thrombomodulin Confers Protection from Neutrophil-mediated Tissue Damage by Suppressing Adhesion Molecule Expression via Nuclear Factor κB and Mitogen-activated Protein Kinase Pathways
Abstract
Thrombomodulin (TM) is a vascular endothelial cell (EC) receptor that is a cofactor for thrombin-mediated activation of the anticoagulant protein C. The extracellular NH(2)-terminal domain of TM has homology to C-type lectins that are involved in immune regulation. Using transgenic mice that lack this structure (TM(LeD/LeD)), we show that the lectin-like domain of TM interferes with polymorphonuclear leukocyte (PMN) adhesion to ECs by …
Authors
Conway EM; Van de Wouwer M; Pollefeyt S; Jurk K; Van Aken H; De Vriese A; Weitz JI; Weiler H; Hellings PW; Schaeffer P
Journal
Journal of Experimental Medicine, Vol. 196, No. 5, pp. 565–577
Publisher
Rockefeller University Press
Publication Date
September 2, 2002
DOI
10.1084/jem.20020077
ISSN
0022-1007
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Amino Acid SequenceAnimalsBase SequenceCell AdhesionEndothelium, VascularFemaleInflammationIntercellular Adhesion Molecule-1LectinsLipopolysaccharidesMaleMiceMice, Mutant StrainsMice, TransgenicMitogen-Activated Protein KinasesMolecular Sequence DataNF-kappa BNeutrophilsProtein Structure, TertiaryThrombomodulin