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

Artikel i vetenskaplig tidskrift
Författare Anna Karlsson
Publicerad i Infection and immunity
Volym 67
Nummer/häfte 7
Sidor 3461-8
ISSN 0019-9567
Publiceringsår 1999
Publicerad vid Institutionen för invärtesmedicin, Avdelningen för reumatologi och inflammationsforskning
Sidor 3461-8
Språk en
Länkar www.ncbi.nlm.nih.gov/entrez/query.f...
Ämnesord Enzyme Activation, drug effects, Humans, NADPH Oxidase, metabolism, Neutrophils, enzymology, Oxygen, metabolism, Reactive Oxygen Species, metabolism, Receptors, Cell Surface, metabolism, Signal Transduction, Wheat Germ Agglutinins, pharmacology
Ämneskategorier Immunologi inom det medicinska området

Sammanfattning

Wheat germ agglutinin (WGA), a lectin with specificity for N-acetylglucosamine and sialic acid, was investigated with respect to its ability to activate the NADPH-oxidase of in vivo-exudated neutrophils (obtained from a skin chamber), and the activity was compared to that of peripheral blood neutrophils. The exudate cells responded to WGA, by both releasing reactive oxygen species into the extracellular milieu and producing oxygen metabolites intracellularly. The peripheral blood cells were unresponsive. To mimic the in vivo-exuded neutrophils with regards to receptor exposure, peripheral blood neutrophils were induced to mobilize their granules and vesicles to varying degrees (in vitro priming), prior to challenge with WGA. The oxidative response to WGA increased with increasing levels of granule mobilization, and the receptor(s) could be shown to reside in the secretory vesicles and/or the gelatinase granules in resting neutrophils. Several WGA-binding glycoproteins 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 by different receptor structures.

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