De Toekomstige Verhoudingen Tussen Ontwikkelde En Onderontwikkelde Gebieden Op Lange termijn

Zimmerman, L. J.

doi:10.1007/bf01423992

Cited by 1 publication

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“…The existence of triggering receptors has also been postulated by others, Thus, using similar techniques, MitchelI and Bowers found 6 high-molecular weight glycoproteins on rat lymph node cells believed to be of importance for the induction of proliferation by oxidizing agents [63]. Similarly, the mitogenic properties of some anti-lymphocyte antisera have been found to be correlated to the presence of antibodies against a 48 kD component on human lymphocytes [64].…”

Section: Discussionmentioning

confidence: 89%

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: Discussionmentioning

confidence: 89%