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. 1995 Oct 15;311(Pt 2):629–636. doi: 10.1042/bj3110629

Human lymphocyte activation is associated with the early and high-level expression of the endogenous lectin CSL at the cell surface.

J P Zanetta 1, J Wantyghem 1, S Kuchler-Bopp 1, A Badache 1, M Aubery 1
PMCID: PMC1136046  PMID: 7487906

Abstract

Lymphocytes undergo activation in response to antigens, cytokines, lectins and antibodies interacting with specific cell-surface molecules or through substances influencing signal transduction pathways. This study shows that human T- and B-cells stimulated using phorbol esters or plant lectins express early (2 h using phorbol esters and 24 h using plant lectins) a high level of a polyvalent carbohydrate-binding protein, the cerebellar soluble lectin (CSL), which is in part externalized. The lectin, immunologically related to CDw70, interacts with specific glycoprotein ligands of the lymphocyte surface, including CD3 on T-cells and CD24 on B-cells. Major changes in phosphorylations associated with activation appear as largely CSL-dependent since they are specifically inhibited by anti-CSL Fab fragments. It is suggested that the lectin induces the clustering of specific cell-surface glycoproteins and plays the role of an endogenous amplifier of activation signals.

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