LFA-1-mediated leukocyte adhesion regulated by interaction of CD43 with LFA-1 and CD147. Export

@article{citeulike:1915534, abstract = {The activity of the lymphocyte-function associated antigen 1 (LFA-1; CD11a/CD18) must be tightly controlled during the onset of cellular immunity. It is well known that the sialoglycoprotein CD43 can influence LFA-1-mediated cell adhesion in an either anti- or pro-adhesive manner through mechanisms not well understood. By using a yeast-2-hybrid screen and co-immunoprecipitation we identified physical association of CD43 with two novel partners, LFA-1 itself and the Ig-family member CD147 (EMMPRIN, basigin), and characterized how these interactions are involved in LFA-1-mediated cell adhesion. Monoclonal antibodies (mAbs) to both CD43 and CD147 induced similar homotypic cell aggregation and adhesion of Jurkat T cells and U937 myeloid cells. Both CD43 and CD147 mAbs induced dynamic co-capping of LFA-1 together with the CD43 and the CD147 molecule to cell contact zones. However, in contrast to CD43, we were not able to co-immunoprecipitate LFA-1 with CD147, which indicates that CD43 interacts with CD147 and LFA-1 in two distinct but similarly reorganized complexes. Co-transfection of CD43 interfered with the CD147-induced cell adhesion and aggregation, and siRNA-mediated knock down of CD43 in human T cells resulted in enhanced LFA-1 activation induced via CD147 and also the T cell antigen receptor. These results indicate that triggering CD43 and the underlying signaling pathways enhance LFA-1 adhesiveness while CD43 also negatively regulates LFA-1 induction via other receptors by dynamic interaction with either LFA-1 or CD147.}, address = {Department of Molecular Immunology, Center for Physiology, Pathophysiology \& Immunology, Medical University of Vienna, Vienna, Austria.}, author = {Khunkaewla, Panida and Schiller, Herbert B B. and Paster, Wolfgang and Leksa, Vladim\'{\i}r and Cerm\'{a}k, Luk\'{a}\v{s} and And\v{e}ra, Ladislav and Ho\v{r}ej\v{s}\'{\i}, V\'{a}clav and Stockinger, Hannes}, citeulike-article-id = {1915534}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.molimm.2007.09.032}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/17996943}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=17996943}, day = {8}, doi = {10.1016/j.molimm.2007.09.032}, issn = {0161-5890}, journal = {Mol Immunol}, keywords = {cd43, lfa-1}, month = {November}, posted-at = {2007-11-14 19:34:50}, priority = {2}, title = {LFA-1-mediated leukocyte adhesion regulated by interaction of CD43 with LFA-1 and CD147.}, url = {http://dx.doi.org/10.1016/j.molimm.2007.09.032}, year = {2007} }

TY - JOUR ID - citeulike:1915534 L3 - citeulike-article-id:1915534 N2 - The activity of the lymphocyte-function associated antigen 1 (LFA-1; CD11a/CD18) must be tightly controlled during the onset of cellular immunity. It is well known that the sialoglycoprotein CD43 can influence LFA-1-mediated cell adhesion in an either anti- or pro-adhesive manner through mechanisms not well understood. By using a yeast-2-hybrid screen and co-immunoprecipitation we identified physical association of CD43 with two novel partners, LFA-1 itself and the Ig-family member CD147 (EMMPRIN, basigin), and characterized how these interactions are involved in LFA-1-mediated cell adhesion. Monoclonal antibodies (mAbs) to both CD43 and CD147 induced similar homotypic cell aggregation and adhesion of Jurkat T cells and U937 myeloid cells. Both CD43 and CD147 mAbs induced dynamic co-capping of LFA-1 together with the CD43 and the CD147 molecule to cell contact zones. However, in contrast to CD43, we were not able to co-immunoprecipitate LFA-1 with CD147, which indicates that CD43 interacts with CD147 and LFA-1 in two distinct but similarly reorganized complexes. Co-transfection of CD43 interfered with the CD147-induced cell adhesion and aggregation, and siRNA-mediated knock down of CD43 in human T cells resulted in enhanced LFA-1 activation induced via CD147 and also the T cell antigen receptor. These results indicate that triggering CD43 and the underlying signaling pathways enhance LFA-1 adhesiveness while CD43 also negatively regulates LFA-1 induction via other receptors by dynamic interaction with either LFA-1 or CD147. JF - Mol Immunol SN - 0161-5890 AD - Department of Molecular Immunology, Center for Physiology, Pathophysiology & Immunology, Medical University of Vienna, Vienna, Austria. TI - LFA-1-mediated leukocyte adhesion regulated by interaction of CD43 with LFA-1 and CD147. KW - cd43 KW - lfa-1 AU - Khunkaewla, Panida AU - Schiller, Herbert B AU - Paster, Wolfgang AU - Leksa, Vladimír AU - Cermák, Lukáš AU - Anděra, Ladislav AU - Hořejší, Václav AU - Stockinger, Hannes PY - 2007/11/08/ UR - http://dx.doi.org/10.1016/j.molimm.2007.09.032 ER -