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CD22 is a functional ligand for SH2 domain-containing protein-tyrosine phosphatase-1 in primary T cells

Sathish, Jean Gerard, Walters, Jenna, Luo, Jin Cai, Johnson, Kenneth G., LeRoy, Frances Gertrude, Brennan, Paul, Kim, Kwang P., Gygi, Steven P., Neel, Benjamin G. and Matthews, Reginald James 2004. CD22 is a functional ligand for SH2 domain-containing protein-tyrosine phosphatase-1 in primary T cells. Journal of Biological Chemistry 279 (46) , pp. 47783-47791. 10.1074/jbc.M402354200

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Abstract

The intracellular Src homology 2 (SH2) domain-containing protein-tyrosine phosphatase (SHP-1) has been characterized as a negative regulator of T cell function, contributing to the definition of T cell receptor signaling thresholds in developing and peripheral mouse T lymphocytes. The activation of SHP-1 is achieved through the engagement of its tandem SH2 domains by tyrosine-phosphorylated proteins; however, the identity of the activating ligand(s) for SHP-1, within mouse primary T cells, is presently unresolved. The identification of SHP-1 ligand(s) in primary T cells would provide crucial insight into the molecular mechanisms by which SHP-1 contributes to in vivo thresholds for T cell activation. Here we present a combination of biochemical and yeast genetic analyses indicating CD22 to be a T cell ligand for the SHP-1 SH2 domains. Based on these observations we have confirmed that CD22 is indeed expressed on mouse primary T cells and capable of associating with SHP-1. Significantly, CD22-deficient T cells demonstrate enhanced proliferation in response to anti-CD3 or allogeneic stimulation. Furthermore, the co-engagement of CD3 and CD22 results in a raising of TCR signaling thresholds hence demonstrating a previously unsuspected functional role for CD22 in primary T cells.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Subjects: R Medicine > R Medicine (General)
ISSN: 1083-351X
Last Modified: 04 Jun 2017 01:31
URI: http://orca-mwe.cf.ac.uk/id/eprint/302

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