Spontaneous and concanavalin A-induced production of leukocyte migration inhibition factor by human peripheral blood lymphocytes

1983 ◽  
Vol 95 (6) ◽  
pp. 831-833
Author(s):  
G. S. Aitmatova ◽  
L. V. Koval'chuk

1982 ◽  
Vol 208 (1) ◽  
pp. 69-75 ◽  
Author(s):  
G Blackledge ◽  
B Vose ◽  
A J Morris ◽  
D Crowther ◽  
J T Gallagher

The binding of fluorescein-conjugated lentil lectin and concanavalin A to the surface membrane of human peripheral blood lymphocytes was studied by flow cytometry. The lymphocytes bound 3-fold more lentil lectin molecules compared with concanavalin A molecules and lentil lectin binding approached saturation at a much lower concentration than did that of concanavalin A. Lentil lectin identified two groups of lymphocytes: a low-binding T-cell fraction and a high-binding B-cell-enriched fraction. Concanavalin A did not discriminate between these populations in unseparated lymphocytes. Competition studies indicated that lentil lectin and concanavalin A were bound to different sites on the lymphocyte surface, although about 50% of lentil lectin sites were in close proximity to concanavalin A sites.



1979 ◽  
Vol 36 (1) ◽  
pp. 31-44
Author(s):  
D.K. Bhalla ◽  
C.V. Hunt ◽  
S.P. Kapur ◽  
W.A. Anderson

The capping of Concanavalin A (Con A) receptors induced by Con A was studied using human peripheral blood lymphocytes. The effects of Con A dose (5–100 micrograms/ml), pretreatment at 4 degrees C, unbound Con A, extracellular Ca2+ and Mg2+ and vinblastine were evaluated using Con A-horseradish peroxidase and electron microscopy. Lymphocytes incubated with Con A at 4 degrees C and fixed with glutaraldehyde exhibited Con A-horseradish peroxidase around the entire cell periphery. After raising the temperature to 37 degrees C, the Con A-horseradish peroxidase moved to form a cap at one pole of the cell and subsequently underwent endocytosis. Capping of Con A receptors induced by Con A at 37 degrees C was observed only at low Con A concentrations in the presence of unbound Con A and extracellular Ca2+ and Mg2+. Increased capping was found after pretreatment of cells with Con A at 4 degrees C, removing unbound Con A and/or removing extracellular Ca2+ and Mg2+, and by treatment with vinblastine. Following removal of both unbound Con A and extracellular Ca2+ and Mg2+, the percentage of capped cells at 37 degrees C was the same as on pretreatment at 4 degrees C under the same conditions. While pretreatment at 4 degrees C caused the breakdown of microtubules, removal of unbound Con A and/or extracellular Ca2+ and Mg2+ had no morphological effect on microtubules or microfilaments. Following exposure of lymphocytes to vinblastine and removal of unbound Con A, capping of Con A receptors by Con A was observed in over 90% of cells at all Con A dosages. However, when cells were exposed to vinblastine in the presence of unbound Con A the formation of Con A caps was either partially or completely inhibited.



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