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

David H. Broide, Marina Miller, Diego Castaneda, Jyothi Nayar, Jae Youn Cho, Mark Roman, Lesley G. Ellies, P. Sriramarao

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

We have investigated the importance of cell-surface serine- and/or threonine-linked oligosaccharide adhesion molecules synthesized by the Golgi enzyme core 2 β-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.

Original languageEnglish (US)
Pages (from-to)L259-L266
JournalAmerican Journal of Physiology - Lung Cellular and Molecular Physiology
Volume282
Issue number2 26-2
DOIs
StatePublished - 2002

Keywords

  • Asthma
  • Golgi enzymes
  • O-linked oligosaccharides

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