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Publication : Core 2 oligosaccharides mediate eosinophil and neutrophil peritoneal but not lung recruitment.

First Author  Broide DH Year  2002
Journal  Am J Physiol Lung Cell Mol Physiol Volume  282
Issue  2 Pages  L259-66
PubMed ID  11792630 Mgi Jnum  J:107833
Mgi Id  MGI:3622362 Doi  10.1152/ajplung.00214.2001
Citation  Broide DH, et al. (2002) Core 2 oligosaccharides mediate eosinophil and neutrophil peritoneal but not lung recruitment. Am J Physiol Lung Cell Mol Physiol 282(2):L259-66
abstractText  We have investigated the importance of cell-surface serine- and/or threonine-linked oligosaccharide adhesion molecules synthesized by the Golgi enzyme core 2 beta-1,6-N-acetylglucosaminyltransferase (C2GlcNAcT) in mediating eosinophil trafficking to the lung in studies utilizing C2GlcNAcT-I-deficient mice. The number of bronchoalveolar eosinophils, the number of lung eosinophils, and airway responsiveness to methacholine were not significantly different in C2GlcNAcT-I-deficient compared with wild-type mice sensitized and challenged by inhalation with ovalbumin. C2GlcNAcT-I-deficient mice do not demonstrate defects in neutrophil trafficking to the lung in response to lipopolysaccharide (LPS). In contrast, ragweed-sensitized C2GlcNAcT-I-deficient mice exhibit significantly reduced eosinophil trafficking to the peritoneal cavity in response to ragweed peritoneal challenge. C2GlcNAcT-I-deficient mice also have significantly reduced neutrophil trafficking to the peritoneal cavity in response to LPS challenge. Overall, these studies demonstrate an important role for serine/threonine-linked oligosaccharides synthesized by the Golgi enzyme C2GlcNAcT-I in eosinophil and neutrophil trafficking to the peritoneum but not for eosinophil or neutrophil trafficking to the lung.
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