{"volume":15,"publist_id":"2178","date_updated":"2021-01-12T07:53:25Z","type":"journal_article","extern":1,"intvolume":"        15","author":[{"last_name":"Moser","first_name":"Markus","full_name":"Moser, Markus"},{"first_name":"Martina","full_name":"Bauer, Martina","last_name":"Bauer"},{"last_name":"Schmid","full_name":"Schmid, Stephan","first_name":"Stephan"},{"full_name":"Ruppert, Raphael","first_name":"Raphael","last_name":"Ruppert"},{"last_name":"Schmidt","first_name":"Sarah","full_name":"Schmidt, Sarah"},{"last_name":"Sixt","id":"41E9FBEA-F248-11E8-B48F-1D18A9856A87","full_name":"Michael Sixt","first_name":"Michael K","orcid":"0000-0002-6620-9179"},{"last_name":"Wang","first_name":"Hao","full_name":"Wang, Hao-Ven"},{"first_name":"Markus","full_name":"Sperandio, Markus","last_name":"Sperandio"},{"last_name":"Fässler","first_name":"Reinhard","full_name":"Fässler, Reinhard"}],"doi":"10.1038/nm.1921","_id":"3950","title":"Kindlin-3 is required for β2 integrin-mediated leukocyte adhesion to endothelial cells","quality_controlled":0,"publication":"Nature Medicine","publication_status":"published","issue":"3","abstract":[{"text":"Integrin activation is essential for the function of all blood cells, including platelets and leukocytes. The blood cell-specific FERM domain protein Kindlin-3 is required for the activation of the beta1 and beta3 integrins on platelets. Impaired activation of beta1, beta2 and beta3 integrins on platelets and leukocytes is the hallmark of a rare autosomal recessive leukocyte adhesion deficiency syndrome in humans called LAD-III, characterized by severe bleeding and impaired adhesion of leukocytes to inflamed endothelia. Here we show that Kindlin-3 also binds the beta2 integrin cytoplasmic domain and is essential for neutrophil binding and spreading on beta2 integrin-dependent ligands such as intercellular adhesion molecule-1 and the complement C3 activation product iC3b. Moreover, loss of Kindlin-3 expression abolished firm adhesion and arrest of neutrophils on activated endothelial cells in vitro and in vivo, whereas selectin-mediated rolling was unaffected. Thus, Kindlin-3 is essential to activate the beta1, beta2 and beta3 integrin classes, and loss of Kindlin-3 function is sufficient to cause a LAD-III-like phenotype in mice.","lang":"eng"}],"citation":{"short":"M. Moser, M. Bauer, S. Schmid, R. Ruppert, S. Schmidt, M.K. Sixt, H. Wang, M. Sperandio, R. Fässler, Nature Medicine 15 (2009) 300–305.","ama":"Moser M, Bauer M, Schmid S, et al. Kindlin-3 is required for β2 integrin-mediated leukocyte adhesion to endothelial cells. <i>Nature Medicine</i>. 2009;15(3):300-305. doi:<a href=\"https://doi.org/10.1038/nm.1921\">10.1038/nm.1921</a>","mla":"Moser, Markus, et al. “Kindlin-3 Is Required for Β2 Integrin-Mediated Leukocyte Adhesion to Endothelial Cells.” <i>Nature Medicine</i>, vol. 15, no. 3, Nature Publishing Group, 2009, pp. 300–05, doi:<a href=\"https://doi.org/10.1038/nm.1921\">10.1038/nm.1921</a>.","ieee":"M. Moser <i>et al.</i>, “Kindlin-3 is required for β2 integrin-mediated leukocyte adhesion to endothelial cells,” <i>Nature Medicine</i>, vol. 15, no. 3. Nature Publishing Group, pp. 300–305, 2009.","ista":"Moser M, Bauer M, Schmid S, Ruppert R, Schmidt S, Sixt MK, Wang H, Sperandio M, Fässler R. 2009. Kindlin-3 is required for β2 integrin-mediated leukocyte adhesion to endothelial cells. Nature Medicine. 15(3), 300–305.","chicago":"Moser, Markus, Martina Bauer, Stephan Schmid, Raphael Ruppert, Sarah Schmidt, Michael K Sixt, Hao Wang, Markus Sperandio, and Reinhard Fässler. “Kindlin-3 Is Required for Β2 Integrin-Mediated Leukocyte Adhesion to Endothelial Cells.” <i>Nature Medicine</i>. Nature Publishing Group, 2009. <a href=\"https://doi.org/10.1038/nm.1921\">https://doi.org/10.1038/nm.1921</a>.","apa":"Moser, M., Bauer, M., Schmid, S., Ruppert, R., Schmidt, S., Sixt, M. K., … Fässler, R. (2009). Kindlin-3 is required for β2 integrin-mediated leukocyte adhesion to endothelial cells. <i>Nature Medicine</i>. Nature Publishing Group. <a href=\"https://doi.org/10.1038/nm.1921\">https://doi.org/10.1038/nm.1921</a>"},"date_created":"2018-12-11T12:06:04Z","month":"02","page":"300 - 305","year":"2009","status":"public","publisher":"Nature Publishing Group","day":"22","date_published":"2009-02-22T00:00:00Z"}