Journal
AMERICAN JOURNAL OF PHYSIOLOGY-LUNG CELLULAR AND MOLECULAR PHYSIOLOGY
Volume 282, Issue 2, Pages L259-L266Publisher
AMER PHYSIOLOGICAL SOC
DOI: 10.1152/ajplung.00214.2001
Keywords
asthma; Golgi enzymes; O-linked oligosaccharides
Categories
Funding
- NCI NIH HHS [KO8 CA88035] Funding Source: Medline
- NIAID NIH HHS [AI-35796, AI-33977, AI-38425] Funding Source: Medline
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We have investigated the importance of cell-surface serine- and/or threonine-linked oligosaccharide adhesion molecules synthesized by the Golgi enzyme core 2beta-1,6-N-acetylglucosaminyltransferase (C2Glc-NAcT) 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 C2Glc-NAcT-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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