Sialyltransferase ST3Gal-IV controls CXCR2-mediated firm leukocyte arrest during inflammation

Frommhold D, Ludwig A, Bixel MG, Zarbock A, Babushkina I, Weissinger M, Cauwenberghs S, Ellies L, Marth J, Beck Sickinger A, Sixt MK, Lange Sperandio B, Zernecke A, Brandt E, Weber C, Vestweber D, Ley K, Sperandio M. 2008. Sialyltransferase ST3Gal-IV controls CXCR2-mediated firm leukocyte arrest during inflammation. The Journal of Experimental Medicine. 205(6), 1435–1446.

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Frommhold, David; Ludwig, Andreas; Bixel, M Gabriele; Zarbock, Alexander; Babushkina, Inna; Weissinger, Melitta; Cauwenberghs, Sandra; Ellies, Lesley G; Marth, Jamey D; Beck-Sickinger, Annette G; Chatterjee, KrishnenduIST Austria ; Lange-Sperandio, Bärbel
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Abstract
Recent in vitro studies have suggested a role for sialylation in chemokine receptor binding to its ligand (Bannert, N., S. Craig, M. Farzan, D. Sogah, N.V. Santo, H. Choe, and J. Sodroski. 2001. J. Exp. Med. 194:1661-1673). This prompted us to investigate chemokine-induced leukocyte adhesion in inflamed cremaster muscle venules of alpha2,3 sialyltransferase (ST3Gal-IV)-deficient mice. We found a marked reduction in leukocyte adhesion to inflamed microvessels upon injection of the CXCR2 ligands CXCL1 (keratinocyte-derived chemokine) or CXCL8 (interleukin 8). In addition, extravasation of ST3Gal-IV(-/-) neutrophils into thioglycollate-pretreated peritoneal cavities was significantly decreased. In vitro assays revealed that CXCL8 binding to isolated ST3Gal-IV(-/-) neutrophils was markedly impaired. Furthermore, CXCL1-mediated adhesion of ST3Gal-IV(-/-) leukocytes at physiological flow conditions, as well as transendothelial migration of ST3Gal-IV(-/-) leukocytes in response to CXCL1, was significantly reduced. In human neutrophils, enzymatic desialylation decreased binding of CXCR2 ligands to the neutrophil surface and diminished neutrophil degranulation in response to these chemokines. In addition, binding of alpha2,3-linked sialic acid-specific Maackia amurensis lectin II to purified CXCR2 from neuraminidase-treated CXCR2-transfected HEK293 cells was markedly impaired. Collectively, we provide substantial evidence that sialylation by ST3Gal-IV significantly contributes to CXCR2-mediated leukocyte adhesion during inflammation in vivo.
Publishing Year
Date Published
2008-06-02
Journal Title
The Journal of Experimental Medicine
Volume
205
Issue
6
Page
1435 - 1446
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Frommhold D, Ludwig A, Bixel MG, et al. Sialyltransferase ST3Gal-IV controls CXCR2-mediated firm leukocyte arrest during inflammation. The Journal of Experimental Medicine. 2008;205(6):1435-1446. doi:10.1084/jem.20070846
Frommhold, D., Ludwig, A., Bixel, M. G., Zarbock, A., Babushkina, I., Weissinger, M., … Sperandio, M. (2008). Sialyltransferase ST3Gal-IV controls CXCR2-mediated firm leukocyte arrest during inflammation. The Journal of Experimental Medicine. Rockefeller University Press. https://doi.org/10.1084/jem.20070846
Frommhold, David, Andreas Ludwig, M Gabriele Bixel, Alexander Zarbock, Inna Babushkina, Melitta Weissinger, Sandra Cauwenberghs, et al. “Sialyltransferase ST3Gal-IV Controls CXCR2-Mediated Firm Leukocyte Arrest during Inflammation.” The Journal of Experimental Medicine. Rockefeller University Press, 2008. https://doi.org/10.1084/jem.20070846.
D. Frommhold et al., “Sialyltransferase ST3Gal-IV controls CXCR2-mediated firm leukocyte arrest during inflammation,” The Journal of Experimental Medicine, vol. 205, no. 6. Rockefeller University Press, pp. 1435–1446, 2008.
Frommhold D, Ludwig A, Bixel MG, Zarbock A, Babushkina I, Weissinger M, Cauwenberghs S, Ellies L, Marth J, Beck Sickinger A, Sixt MK, Lange Sperandio B, Zernecke A, Brandt E, Weber C, Vestweber D, Ley K, Sperandio M. 2008. Sialyltransferase ST3Gal-IV controls CXCR2-mediated firm leukocyte arrest during inflammation. The Journal of Experimental Medicine. 205(6), 1435–1446.
Frommhold, David, et al. “Sialyltransferase ST3Gal-IV Controls CXCR2-Mediated Firm Leukocyte Arrest during Inflammation.” The Journal of Experimental Medicine, vol. 205, no. 6, Rockefeller University Press, 2008, pp. 1435–46, doi:10.1084/jem.20070846.

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