Ferrocyanide enhancement of concanavalin A-ferritin and cationized ferritin staining blood cell surface glycoconjugates

1979 ◽  
Vol 11 (4) ◽  
pp. 379-389 ◽  
Author(s):  
Richard T. Parmley ◽  
Francis R. Denys ◽  
Celestino J. Alvarez
Keyword(s):  
Cell Surface ◽  
Blood Cell ◽  
Concanavalin A ◽  
Cationized Ferritin ◽  
Cell Surface Glycoconjugates

Differential redistribution of lectin receptor classes on clonal rat myotubes and myoblasts

1986 ◽  
Vol 83 (1) ◽  
pp. 181-196
Author(s):  
J.T. Sawyer ◽  
R.A. Akeson
Keyword(s):  
Cell Surface ◽  
Concanavalin A ◽  
Wheat Germ ◽  
Lens Culinaris ◽  
Qualitative Change ◽  
Soybean Agglutinin ◽  
Plant Lectins ◽  
Lectin Receptor ◽  
Lens Culinaris Agglutinin ◽  
Cell Surface Glycoconjugates

To evaluate the relative mobilities of cell surface glycoconjugates during myogenesis we have studied the redistribution of fluorescein-conjugated plant lectins on L6 rat myogenic cells. Previous experiments had demonstrated that the receptors for the lectins soybean agglutinin (SBA), wheat germ agglutinin, concanavalin A and Lens culinaris agglutinin all were relatively uniformly distributed on both myoblasts and myotubes, and that SBA receptors were capable of rapid redistribution on myotubes but not myoblasts at 4 degrees C (Sawyer & Akeson, 1983). Here we show that when SBA-labelled myoblasts are incubated at 37 degrees C, or for extended times at 4 degrees C, the lectin aggregates as on myotubes. So it appears that SBA-binding components show a quantitative rather than qualitative change in their mobility during L6 differentiation. In addition, the redistribution of the three other lectins on myoblasts and myotubes was either less prominent (i.e. showing fewer apparent surface clusters) or occurred less rapidly than with SBA. None of these three lectins showed striking differences in mobility between myoblasts and myotubes. Thus, it appears that SBA binds to a subset of surface glycoconjugates that is relatively highly mobile, and that this mobility is specifically enhanced with differentiation.

scholarly journals Relative mobility of con A and anionic receptor sites on the cell surface of lymphocytes. A quantitative-cytochemical study.

1978 ◽  
Vol 26 (6) ◽  
pp. 468-477 ◽  
Author(s):  
D K Bhalla ◽  
M E Perotti ◽  
W A Anderson
Keyword(s):  
Cell Surface ◽  
Concanavalin A ◽  
Human Peripheral Blood ◽  
Peripheral Blood Lymphocytes ◽  
Cationized Ferritin ◽  
Reaction Products ◽  
Cytochemical Study ◽  
Receptor Sites ◽  
Normal Human Peripheral Blood ◽  
Concanavalin A Receptors

Events following the binding of Concanavalin A and cationized ferritin to the surface of normal human peripheral blood lymphocytes were followed using ultracytochemical methods. In this paper, we described a technique involving microdensitometry, which was employed in order to make a comparative cytochemical quantitation of the dense horseradish peroxidase-diaminobenzidine reaction products representing the states of Concanavalin A receptors under various conditions of distribution and redistribution. The technique presents a direct approach to the analysis of various probes that are currently being employed for studying the nature and distribution of various cell surface components. An attempt was also made to analyze the distribution of anionic sites, and their lateral redistribution is compared with the mobility of Concanavalin A receptors. The data presented suggests an independent mobility of receptors for Concanavalin A and cationized ferritin.

Perfluorocarbon attenuates response of concanavalin A-stimulated mononuclear blood cells without altering ligand-receptor interaction

2004 ◽  
Vol 287 (1) ◽  
pp. L210-L216 ◽  
Author(s):  
Dirk Haufe ◽  
Thomas Luther ◽  
Matthias Kotzsch ◽  
Lilla Knels ◽  
Thea Koch
Keyword(s):  
Cell Surface ◽  
Concanavalin A ◽  
Blood Cells ◽  
Cell Activation ◽  
Receptor Interaction ◽  
Surface Binding ◽  
Cellular Activation ◽  
Flow Cytofluorometry ◽  
Anti Inflammatory ◽  
Mononuclear Blood Cells

Intrapulmonary application of perfluorocarbons (PFC) in acute lung injury is associated with anti-inflammatory effects. A direct impact on leukocytic function may be involved. To further elucidate PFC effects on cellular activation, we compared in an in vitro model the response of concanavalin A (ConA)-stimulated lymphocytes and monocytes exposed to perfluorohexane. We hypothesized that perfluorohexane attenuates the action of the lectin ConA by altering stimulant-receptor interaction on the cell surface. Mononuclear blood cells were stimulated by incubation with ConA in the presence of different amounts of perfluorohexane. The response of lymphocytes and monocytes was determined by means of IL-2 secretion and tissue factor (TF) expression, respectively. The influence of perfluorohexane on cell-surface binding of fluorescence-labeled ConA was studied using flow cytofluorometry and fluorescence microscopy. Perfluorohexane itself did not induce a cellular activation but significantly inhibited both monocytic TF expression and, to a far greater extent, IL-2 secretion of ConA-stimulated mononuclear blood cells. The effect of perfluorohexane was due neither to an alteration of cell viability nor to a binding of the stimulant. The amount of cell surface-bound ConA was not altered by perfluorohexane, and the overall pattern of ConA receptor rearrangement did not differ between controls and treated cells. In the present study, we provide further evidence for an anti-inflammatory effect of PFC that might be beneficial in states of pulmonary hyperinflammation. A PFC-induced alteration of stimulant-receptor interaction on the surface membrane does not seem to be the cause of attenuated cell activation.

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