2. Academic Validation
  3. Novel sulfated lymphocyte homing receptors and their control by a Core1 extension beta 1,3-N-acetylglucosaminyltransferase

Novel sulfated lymphocyte homing receptors and their control by a Core1 extension beta 1,3-N-acetylglucosaminyltransferase

  • Cell. 2001 Jun 29;105(7):957-69. doi: 10.1016/s0092-8674(01)00394-4.
J C Yeh 1,  N Hiraoka,  B Petryniak,  J Nakayama,  L G Ellies,  D Rabuka,  O Hindsgaul,  J D Marth,  J B Lowe,  M Fukuda
Affiliations

Affiliation

  • 1 Glycobiology Program, Cancer Research Center, The Burnham Institute, La Jolla, CA 92037, USA.
PMID: 11439191 DOI: 10.1016/s0092-8674(01)00394-4
Abstract

L-selectin mediates lymphocyte homing by facilitating lymphocyte adhesion to addressins expressed in the high endothelial venules (HEV) of secondary lymphoid organs. Peripheral node addressin recognized by the MECA-79 antibody is apparently part of the L-selectin ligand, but its chemical nature has been undefined. We now identify a sulfated extended core1 mucin-type O-glycan, Gal beta 1-->4(sulfo-->6)GlcNAc beta 1-->3Gal beta 1-->3GalNAc, as the MECA-79 epitope. Molecular cloning of a HEV-expressed core1-beta 1,3-N-acetylglucosaminyltransferase (Core1-beta 3GlcNAcT) enabled the construction of the 6-sulfo sialyl Lewis x on extended core1 O-glycans, recapitulating the potent L-selectin-mediated, shear-dependent adhesion observed with novel L-selectin ligands derived from core2 beta1,6-N-acetylglucosaminyltransferase-I null mice. These results identify Core1-beta 3GlcNAcT and its cognate extended core1 O-glycans as essential participants in the expression of the MECA-79-positive, HEV-specific L-selectin ligands required for lymphocyte homing.

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