Sulfotransferases of two specificities function in the reconstitution of high endothelial cell ligands for L-selectin.

Journal Article

L-selectin, a lectin-like receptor, mediates rolling of lymphocytes on high endothelial venules (HEVs) in secondary lymphoid organs by interacting with HEV ligands. These ligands consist of a complex of sialomucins, candidates for which are glycosylation- dependent cell adhesion molecule 1 (GlyCAM-1), CD34, and podocalyxin. The ligands must be sialylated, fucosylated, and sulfated for optimal recognition by L-selectin. Our previous structural characterization of GlyCAM-1 has demonstrated two sulfation modifications, Gal-6-sulfate and GlcNAc-6-sulfate in the context of sialyl Lewis x. We now report the cloning of a Gal-6-sulfotransferase and a GlcNAc-6-sulfotransferase, which can modify GlyCAM-1 and CD34. The Gal-6-sulfotransferase shows a wide tissue distribution. In contrast, the GlcNAc-6-sulfotransferase is highly restricted to HEVs, as revealed by Northern analysis and in situ hybridization. Expression of either enzyme in Chinese hamster ovary cells, along with CD34 and fucosyltransferase VII, results in ligand activity, as detected by binding of an L-selectin/IgM chimera. When coexpressed, the two sulfotransferases synergize to produce strongly enhanced chimera binding.

Full Text

Duke Authors

Cited Authors

  • Bistrup, A; Bhakta, S; Lee, JK; Belov, YY; Gunn, MD; Zuo, FR; Huang, CC; Kannagi, R; Rosen, SD; Hemmerich, S

Published Date

  • May 17, 1999

Published In

Volume / Issue

  • 145 / 4

Start / End Page

  • 899 - 910

PubMed ID

  • 10330415

International Standard Serial Number (ISSN)

  • 0021-9525

Language

  • eng

Conference Location

  • United States