scholarly journals A comparative study of the localization of wheat-germ agglutinin and its potential receptors in wheat grains

1982 ◽  
Vol 206 (3) ◽  
pp. 571-576 ◽  
Author(s):  
R C Miller ◽  
D J Bowles
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Soluble Form ◽  
Wheat Seed ◽  
Endosperm Tissue ◽  
Wheat Grains ◽  
Embryo Tissue ◽  
Reversible Association ◽  
Germination And Growth

Wheat-germ agglutinin is located only in the embryo of a dry wheat seed and not in the endosperm tissue. This distribution remains unaltered for up to 96 h of germination and growth. The lectin is found not only in a freely soluble form but also in reversible association with particulate subcellular components. There appear to be no poly-peptides that can be solubilized with sonication and aqueous buffers from the embryo tissue that can interact with the agglutinin. This suggests that in vivo the lectin remains uncomplexed to endogenous glycoconjugates or is only able to bind to glycosylated integral membrane polypeptides. Alternatively the potential endogenous receptor(s) to wheat-germ agglutinin may not contain a polypeptide. Although the lectin is not present in the endosperm, seven polypeptides able to interact in a reversible way with wheat-germ agglutinin could be purified from that tissue.

Internalization of wheat germ agglutinin (WGA) by rat pancreatic cells in vivo and in vitro

1996 ◽  
Vol 98 (2) ◽  
pp. 165-172 ◽  
Author(s):  
Christian Wirth ◽  
Jörg Schwuchow ◽  
Ludwig Jonas
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Pancreatic Cells

In vivo uptake of wheat germ agglutinin-horseradish peroxidase conjugates into neuronal gerl and lysosomes

1980 ◽  
Vol 188 (2) ◽  
pp. 465-472 ◽  
Author(s):  
Clive G. Harper ◽  
Jacqueline O. Gonatas ◽  
Anna Stieber ◽  
Nicholas K. Gonatas
Keyword(s):  
Horseradish Peroxidase ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
In Vivo Uptake

scholarly journals Immunocytochemical localization of wheat germ agglutinin in wheat.

1982 ◽  
Vol 92 (3) ◽  
pp. 753-764 ◽  
Author(s):  
M Mishkind ◽  
N V Raikhel ◽  
B A Palevitz ◽  
K Keegstra
Keyword(s):  
Wheat Germ Agglutinin ◽  
Direct Contact ◽  
Fungal Pathogens ◽  
Adventitious Roots ◽  
Wheat Germ ◽  
Wheat Embryos ◽  
Secondary Antibodies ◽  
Germination And Growth ◽  
Subcellular Level ◽  
Adult Plants

Immunocytological techniques were developed to localize the plant lectin, wheat germ agglutinin (WGA), in the tissues and cells of wheat plants. In a previous study we demonstrated with a radioimmunoassay that the lectin is present in wheat embryos and adult plants both in the roots and at the base of the stem. We have now found, using rhodamine, peroxidase, and ferritin-labeled secondary antibodies, that WGA is located in cells and tissues that establish direct contact with the soil during germination and growth of the plant In the embryo, WGA is found in the surface layer of the radicle, the first adventitious roots, the coleoptile, and the scutellum. Although found throughout the coleorhiza and epiblast, it is at its highest levels within the cells at the surface of these organs. In adult plants, WGA is located only in the caps and tips of adventitious roots. Reaction product for WGA was not visualized in embryonic or adult leaves or in other tissues of adult plants. At the subcellular level, WGA is located at the periphery of protein bodies, within electron-translucent regions of the cytoplasm, and at the cell wall-protoplast interface. Since WGA is found at potential infection sites and is known to have fungicidal properties, it may function in the defense against fungal pathogens.

scholarly journals Wheat Germ Agglutinin Induces NADPH-Oxidase Activity in Human Neutrophils by Interaction with Mobilizable Receptors

1999 ◽  
Vol 67 (7) ◽  
pp. 3461-3468 ◽  
Author(s):  
Anna Karlsson
Keyword(s):  
Sialic Acid ◽  
Nadph Oxidase ◽  
Peripheral Blood ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Human Neutrophils ◽  
Extracellular Milieu ◽  
Blood Neutrophils

ABSTRACT Wheat germ agglutinin (WGA), a lectin with specificity forN-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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