Characterization of expression of glycan ligands for Siglec-F in normal mouse lungs

Jin P. Guo, Mary E. Brummet, Allen C. Myers, Ho Jeong Na, Elizabeth Rowland, Ronald L. Schnaar, Tao Zheng, Zhou Zhu, Bruce S. Bochner

Research output: Contribution to journalArticlepeer-review

24 Scopus citations


Sialic acid-binding immunoglobulin-like lectin (Siglec)-F, an inhibitory receptor on mouse eosinophils, preferentially recognizes the glycan ligand 69-sulfated sialyl Lewis X, but little is known about the requirements for its lung expression. RT-PCR and immunohistochemistry were used to detect and localize the sulfotransferase keratin sulfate galactose 6-O sulfotransferase (KSGal6ST, alsoknown as carbohydrate sulfotransferase 1; gene name, Chst1) that is putatively required for 6′-sulfated Sialyl Lewis X synthesis. RT-PCR detected the greatest constitutive expression of Chst1 in lung, liver, andspleen tissue.Immunohistochemistry localized the expression of KSGal6ST in lung tissue primarily to airway epithelium. Siglec-F-Ig fusion protein selectively bound in a similar pattern, and was unaffected in lung tissue treated with methanol or deficient in Type 2 α2,3 sialyltransferase (St3gal2), but was eliminated by proteinase K or sialidase, and was absent in tissue deficient in the Type 3 α2,3 sialyltransferase (St3gal3). Binding of the Siglec-F-Ig fusion protein was similar in pattern to, and completely blocked by, a plant lectin recognizing α2,3-linked sialic acid. Thus, α2,3-linked sialic acid-containing glycoprotein Siglec-F ligands and the enzymes required for their synthesis are constitutively expressed in murine lungs, especially by airway epithelium. St3gal3, but not St3gal2, is required for constitutive Siglec-F ligand synthesis. The survival of eosinophils entering the lung may be shortened by encountering these Siglec-F sialoside ligands.

Original languageEnglish (US)
Pages (from-to)238-243
Number of pages6
JournalAmerican journal of respiratory cell and molecular biology
Issue number2
StatePublished - Feb 1 2011


  • Eosinophil
  • Glycan ligand
  • Lung epithelium
  • Sialic acid
  • Sialyltransferase

ASJC Scopus subject areas

  • Molecular Biology
  • Pulmonary and Respiratory Medicine
  • Clinical Biochemistry
  • Cell Biology


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