Isolation and characterization of the potential receptor for wheat germ agglutinin from human neutrophils.

Abstract:

: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.

journal_name

Glycoconj J

journal_title

Glycoconjugate journal

authors

Solórzano C,Bouquelet S,Pereyra MA,Blanco-Favela F,Slomianny MC,Chavez R,Lascurain R,Zenteno E,Agundis C

doi

10.1007/s10719-006-8635-6

subject

Has Abstract

pub_date

2006-11-01 00:00:00

pages

591-8

issue

7-8

eissn

0282-0080

issn

1573-4986

journal_volume

23

pub_type

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