scholarly journals Wheat germ agglutinin, concanavalin A, and lens culinalis agglutinin block the inhibitory effect of nerve growth factor on cell-free phosphorylation of Nsp100 in PC12h cells.

1989 ◽  
Vol 14 (1) ◽  
pp. 87-93 ◽  
Author(s):  
Seiichi Hashimoto ◽  
Akihiko Hagino
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Concanavalin A ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Inhibitory Effect ◽  
Nerve Growth ◽  
Pc12h Cells

scholarly journals Alteration of binding properties and cytoskeletal attachment of nerve growth factor receptors in PC12 cells by wheat germ agglutinin.

1982 ◽  
Vol 94 (3) ◽  
pp. 710-717 ◽  
Author(s):  
R D Vale ◽  
E M Shooter
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Pc12 Cells ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Binding Properties ◽  
Nerve Growth ◽  
Total Binding ◽  
Ngf Receptor ◽  
Triton X

Incubation of PC12 cells preloaded with 125I-nerve growth factor (NGF) reveals rapidly and slowly dissociating binding components indicative of a heterogeneous population of receptors. If the cells are previously exposed to wheat germ agglutinin (WGA) for 30 min, NGF now binds to an apparently homogeneous receptor population which exhibit slow dissociation kinetics. Total binding is also reduced by 50%. If WGA is added subsequent to 125I-NGF, total binding is not diminished, but rapidly dissociating receptors occupied with NGF are all converted to the slowly dissociating form. This conversion of receptors occurs rapidly, reaching completion within 2 min at 37 degrees or 4 degrees C, and is unaffected by metabolic energy poisons, suggesting that WGA-induced slowly dissociating receptors are not the product of internalization. The effects of the lectin are blocked by the sugar N-acetyl-D-glucosamine, and the lectin-induced slowly dissociating receptors are converted back to rapidly dissociating receptors by addition of this same sugar. WGA also affects the association of the NGF receptor with the Triton X-100 cytoskeleton. Greater than 90% of bound 125I-NGF becomes associated with Triton X-100 insoluble cytoskeletons in the presence of the lectin, compared with less than 20% before lectin addition. Cytoskeleton association of the NGF receptor by WGA shows similar kinetics as the conversion of rapidly to slowly dissociating receptors. This interaction may be involved in the alteration of NGF-receptor binding properties produced by this lectin.

scholarly journals Receptor-mediated gonadotropin action in the ovary. Inhibitory actions of concanavalin A and wheat-germ agglutinin on gonadotropin-stimulated cyclic AMP and progesterone responses in ovarian cells

1981 ◽  
Vol 200 (1) ◽  
pp. 153-159 ◽  
Author(s):  
S Azhar ◽  
K M Menon
Keyword(s):  
Cyclic Amp ◽  
Concanavalin A ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Carbohydrate Chain ◽  
Inhibitory Effect ◽  
Dolichos Biflorus ◽  
Acetylneuraminic Acid ◽  
Ovarian Cells ◽  
Proline Incorporation

Pretreatment of ovarian cells with concanavalin A and wheat-germ agglutinin blocked the gonadotropin-induced cyclic AMP and progesterone responses and this effect was time- and concentration-dependent. Basal production of either cyclic AMP or progesterone, however, was not affected by treatment of cells with lectin. The effect of concanavalin A on gonadotropin-mediated cyclic AMP and progesterone responses was blocked by alpha-methyl D-mannoside and alpha-methyl d-glucoside. Similarly the inhibitory effect of wheat-germ agglutinin was reversed by N-acetyl-D-glucosamine. Pretreatment of ovarian cells with concanavalin A or wheat-germ agglutinin had no effect on protein synthesis in the ovary as monitored by [3H]proline incorporation studies. Concanavalin A and wheat-germ agglutinin did not affect steroid production in response to dibutyryl cyclic AMP and 8-bromo cyclic AMP, indicating that the inhibitory action of lectin was occurring at a step before cyclic AMP formation. Lectins specific for L-fucose, D-galactose and N-acetyl-D-galactosamine, gorse seed agglutinin, peanut agglutinin and Dolichos biflorus agglutinin respectively, did not interfere with gonadotropin-induced cyclic AMP and progesterone responses. The present studies suggest that gonadotropin receptors may be glycoprotein in nature or closely associated with glycoprotein structures with the carbohydrate chain containing N-acetyl-D-glucosamine, mannose and possibly N-acetylneuraminic acid.

scholarly journals Nerve growth factor stimulates tyrosine phosphorylation of paxillin in PC12h cells

FEBS Letters ◽  
1995 ◽  
Vol 362 (2) ◽  
pp. 201-204 ◽  
Author(s):  
Muhammad Ashraf Khan ◽  
Nobuaki Okumura ◽  
Masato Okada ◽  
Shin Kobayashi ◽  
Hachiro Nakagawa
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Tyrosine Phosphorylation ◽  
Nerve Growth ◽  
Pc12h Cells
Sign in / Sign up

Export Citation Format

Share Document