test_moissonnage_selune
type: Agent

Isolation and characterization of the potential receptor for wheat germ agglutinin from human neutrophils
type: Distribution
access URL: https://hal.science/hal-00086491
format: HTML
issued: 2026-05-09T15:24:14.089541
modified: 2026-05-09T15:24:14.072502

Isolation and characterization of the potential receptor for wheat germ agglutinin from human neutrophils
type: Dataset
contact point: Organization
  fn: CCSD
keyword: oxidative-burst
keyword: sdvbbmlife-sciences-q-biobiochemistry-molecular-biology
keyword: journal-articles
keyword: neutrophils
keyword: infoeu-reposemanticsarticle
keyword: proteomic
keyword: lectins
keyword: glcnac
keyword: wga
landing page: 0282-0080
description: Neutrophils participate in host protection and central to this process is the regulation of oxidative mechanisms. We purified by affinity chromatography the receptor for the GlcNAc-specific WGA from CD14+CD16+ cell lysates (WGAr). The receptor is a 141 kDa glycoprotein constituted by two subunits of 78 and 63 kDa. It is mainly composed of Ser, Asx, and Gly, and, in a minor proportion, His, Cys, and Pro. Its glycan portion contains GlcNAc, Gal, and Man; NeuAc and GalNAc were identified in a minor proportion. The amino acid sequence of the WGA receptor was predicted from tryptic peptides by MALDI-TOF, both subunits showed homology with cytokeratin type II (26 and 29% for the 78 and 63 kDa subunits, respectively); the 78 kDa subunit showed also homology with the human transferrin receptor (24%). Antibodies against WGAr induce higher oxidative burst than WGA, determined by NBT reduction; however, this effect was inhibited (p<0.05) with GlcNAc suggesting that WGAr participates as mediator in signal transduction in neutrophils.
issued: 2026-05-09T15:24:14.083903
language: en
modified: 2026-05-09T15:24:14.083907