Role of adherent cells in immune responses to phytohemagglutinin and concanavalin A

Arala-Chaves, M.P.; Hope, L.; Korn, Joseph H.; Fudenberg, H. Hugh

doi:10.1002/eji.1830080202

Cited by 24 publications

(11 citation statements)

References 18 publications

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“…These results confirm, and in the case of LBL-I11 and WFA, extend to purified T cells the findings of others [ l , 2, 44-48]. It is unclear whether accessory cells are essential for mitogen-induced T cell proliferation [12][13][14]. We found that the response of T cells to La, WFA, SBA and LBL-I11 was either somewhat increased or unchanged as compared to that of the original PBL preparation (Fig.…”

Section: Discussionsupporting

confidence: 94%

“…Similarly, it is not clear whether cellcell interactions are essential for T cell triggering by lectins or whether single cells can be activated . The role of accessory cells and various types of growth factors is presently under intense investigation [12][13][14][15][16]. There are some indications that the membrane glycoprotein components are involved in mitogenesis, since treatment of the cells with proteases inhibited lectin-induced proliferation, and a glycoprotein -but not a glycolipid fraction -isolated from the plasma membranes of the lymphocytes also inhibited proliferation [17,181.…”

Section: Introductionmentioning

confidence: 99%

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Interaction of lectins with human T lymphocytes mitogenic properties, inhibitory effects, binding to the cell membrane and to isolated surface glycopeptides

et al. 1980

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The mode of interaction of twelve lectins with human T lymphocytes was investigated. In order to establish possible differences between mitogenic and nonmitogenic lectins, they were studied for their capacity to induce or inhibit DNA synthesis. Their interaction with intact T cells was studied by immunofluorescence and "Cr release. Further, lectins conjugated to Sepharose were investigated with regard to their capacity to bind surface glycopeptides from T cell lysates. Operationally, the lectins could be divided into three groups: (a) mitogenic lectins; (b) lectins inhibitory for lymphocyte mitogenesis as induced by leucoagglutinin (La) from Phaseolus vulgaris; and (c) nonmitogenic lectins which were noninhibitory in this La system. Six lectins were nonmitogenic. For two or possibly three of these, lack of mitogenicity was due to complete or partial failure to bind to the lymphocytes. This explanation could not account for lack of mitogenicity of the other three nonmitogenic lectins. Only two of the lectins utilized inhibited La-induced mitogenesis. However, when the lectins were compared with regard to their capacity to bind surface glycopeptides from T cell lysates, important differences between mitogenic and nonmitogenic lectins were seen. As revealed by polyacrylamide gel electrophoresis in sodium dodecyl sulfate and autoradiography, the mitogenic lectins bound a larger number of surface glycopeptides (15-20) than the nonmitogenic lectins (3-10). More importantly, five distinct glycopeptides (gp 135 K, 125 K, 105 K, 95 K and 43 K) were bound by all mitogenic lectins but not by the nonmitogenic lectins. It remains to be established whether these glycopeptides are present on the T cells which are susceptible to the mitogenic action of the lectins and whether it is the interaction of the lectins with one or several of them which triggers mitogenicity.

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Section: Discussionsupporting

confidence: 94%

Section: Introductionmentioning

confidence: 99%

Interaction of lectins with human T lymphocytes mitogenic properties, inhibitory effects, binding to the cell membrane and to isolated surface glycopeptides

et al. 1980

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“…Monocyte augmentation of lymphocyte proliferation has been documented with cells grown in suspension or soft agar culture, and cells stimulated with either mitogen or antigen (2)(3)(4)(5)(6)(7)(8)(9)(10)(11). These data, demonstrating the need for both a stimulating mitogen and a growth-supporting accessory cell, suggest a possible requirement for multiple independent signals for optimal T cell proliferation.…”

Section: From the University Of Texas System Cancer Center M D Andmentioning

confidence: 99%

Effect of interleukin 1 on human thymocytes and purified human T cells.

Maizel¹,

Mehta²,

Ford³

et al. 1981

The Journal of Experimental Medicine

100

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Human Interleukin 1 (IL-1) purified by molecular weight fractionation, isoelectric focusing, and gel electrophoresis has been tested on human thymocytes and highly purified human T cells. IL-1 prepared in this manner could not support the long-term growth of T cells yet would augment lectin-stimulated mitogenesis. The IL-1 preparations were shown to possess the lectin-augmenting activity at dilutions containing less than 1 ng of the measurable protein. These data are in agreement with the model that IL-1 stimulates production of IL-2 from lectin-stimulated lymphocytes.

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“…The interaction of different functional cell subsets is a normal requirement for mitogenic stimulation (Arala-Chaves et al, 1978), but as a consequence, only a proportion of cells are likely to respond in the early stages, even with polyclonal activators. Methods of investigation that depend on the use of radioactive probes, or on the measurement of the fluorescence of cell suspensions, provide a measure of cell response that is averaged over all those present.…”

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confidence: 99%

Flow cytometric detection of membrane potential changes in murine lymphocytes induced by concanavalin A

Tatham¹,

Delves²

1984

Biochemical Journal

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The effect of the mitogenic lectin concanavalin A on the membrane potential of murine lymphocytes was investigated by observing the fluorescence of cells stained with carbocyanine and oxonol dyes. We describe a rapid and reliable method for detecting lectin-induced membrane potential changes in individual cells by flow cytometric analysis of oxonol fluorescence. By 10min after addition of lectin to suspensions of isolated cells from lymph node, 7-15% of the cells have responded by releasing oxonol dye, indicating a membrane hyperpolarization. The dose onset of this response is similar to that for mitogenesis, which was assessed by measuring [3H]thymidine incorporation. The effect is abolished by a-methyl mannoside (100mM), which prevents concanavalin A from binding to the cells, but not by fucose (100mM). When cells are treated with lectin in medium from which Ca2+ has been omitted or to which quinine (0.5mM) has been added, a membrane depolarization is observed. Since these are conditions under which activation of plasma membrane Ca2+-dependent K+ channels is prevented, these findings support the view that the early hyperpolarization of these cells is brought about by an increase in intracellular free [Ca2+].

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Role of adherent cells in immune responses to phytohemagglutinin and concanavalin A

Cited by 24 publications

References 18 publications

Interaction of lectins with human T lymphocytes mitogenic properties, inhibitory effects, binding to the cell membrane and to isolated surface glycopeptides

Interaction of lectins with human T lymphocytes mitogenic properties, inhibitory effects, binding to the cell membrane and to isolated surface glycopeptides

Effect of interleukin 1 on human thymocytes and purified human T cells.

Flow cytometric detection of membrane potential changes in murine lymphocytes induced by concanavalin A

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