Characterization of expression of glycan ligands for Siglec-F in normal mouse lungs.
Sialic acid-binding immunoglobulin-like lectin (Siglec)-F, an inhibitory receptor on mouse eosinophils, preferentially recognizes the glycan ligand 6'-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, also known 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, and spleen 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.
Guo
Jin P
JP
Division of Allergy and Clinical Immunology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland, USA.
Brummet
Mary E
ME
Myers
Allen C
AC
Na
Ho Jeong
HJ
Rowland
Elizabeth
E
Schnaar
Ronald L
RL
Zheng
Tao
T
Zhu
Zhou
Z
Bochner
Bruce S
BS
D000818:Animals; D000888:Antibodies, Anti-Idiotypic; D000911:Antibodies, Monoclonal / Q000378:metabolism; D061067:Antibodies, Monoclonal, Humanized; D015214:Antigens, Differentiation, Myelomonocytic / Q000378:metabolism*; D001483:Base Sequence; D017931:DNA Primers / Q000235:genetics; D005260:Female; D008024:Ligands; D008168:Lung / Q000276:immunology* / Q000378:metabolism*; D008297:Male; D051379:Mice; D008810:Mice, Inbred C57BL; D018345:Mice, Knockout; D000069444:Omalizumab; D011134:Polysaccharides / Q000276:immunology* / Q000378:metabolism*; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D020545:Respiratory Mucosa / Q000276:immunology / Q000378:metabolism; D063265:Sialic Acid Binding Immunoglobulin-like Lectins; D012799:Sialyltransferases / Q000172:deficiency / Q000235:genetics / Q000378:metabolism; D015238:Sulfotransferases / Q000235:genetics / Q000378:metabolism; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase; D000097811:Carbohydrate Sulfotransferases
D000888:Antibodies, Anti-Idiotypic; D000911:Antibodies, Monoclonal; D061067:Antibodies, Monoclonal, Humanized; D015214:Antigens, Differentiation, Myelomonocytic; D017931:DNA Primers; D008024:Ligands; D000069444:Omalizumab; D011134:Polysaccharides; D012333:RNA, Messenger; D011993:Recombinant Fusion Proteins; D063265:Sialic Acid Binding Immunoglobulin-like Lectins; D012799:Sialyltransferases; D015238:Sulfotransferases; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase; D000097811:Carbohydrate Sulfotransferases; C443130:Siglecf protein, mouse
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