Wheat germ agglutinin induces NADPH-oxidase activity in human neutrophils by interaction with mobilizable receptors

Authors
Citation
A. Karlsson, Wheat germ agglutinin induces NADPH-oxidase activity in human neutrophils by interaction with mobilizable receptors, INFEC IMMUN, 67(7), 1999, pp. 3461-3468
Citations number
52
Categorie Soggetti
Immunology
Journal title
INFECTION AND IMMUNITY
ISSN journal
00199567 → ACNP
Volume
67
Issue
7
Year of publication
1999
Pages
3461 - 3468
Database
ISI
SICI code
0019-9567(199907)67:7<3461:WGAINA>2.0.ZU;2-1
Abstract
Wheat germ agglutinin (WGA), a lectin,vith specificity for N-acetylglucosam ine and sialic acid, was investigated with respect to its ability to activa te the NADPH-oxidase of in vivo-exudated neutrophils (obtained from a skin chamber), and the activity was compared to that of peripheral blood neutrop hils. The exudate cells responded to WGA, by both releasing reactive oxygen species into the extracellular milieu and producing oxygen metabolites int racellularly. The peripheral blood cells were unresponsive. To mimic the in vivo-exuded neutrophils with regards to receptor exposure, peripheral bloo d neutrophils were induced to mobilize their granules and vesicles to varyi ng degrees (in vitro priming), prior to challenge with WGA. The oxidative r esponse to WGA increased with increasing levels of granule mobilization, an d the receptor(s) could be shown to reside in the secretory vesicles and/or the gelatinase granules in resting neutrophils. Several WGA-binding glycop roteins were detected in subcellular fractions containing these organelles. The extra- and intracellular NADPH-oxidase responses showed differences in sialic acid dependency, indicating that these two responses are mediated b y different receptor structures.