Regulation of CD45 engagement by the B-cell receptor CD22

Détails

ID Serval
serval:BIB_5F86CACABD6B
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Regulation of CD45 engagement by the B-cell receptor CD22
Périodique
Proceedings of the National Academy of Sciences of the United States of America
Auteur(s)
Sgroi  D., Koretzky  G. A., Stamenkovic  I.
ISSN
0027-8424 (Print)
Statut éditorial
Publié
Date de publication
1995
Volume
92
Numéro
9
Pages
4026-4030
Notes
PT - Journal Article PT - Research Support, Non-U.S. Gov't PT - Research Support, U.S. Gov't, P.H.S
Résumé
The B-cell receptor CD22 binds sialic acid linked alpha-2-6 to terminal galactose residues on N-linked oligosaccharides associated with several cell-surface glycoproteins. The first of these sialoglycoproteins to be identified was the receptor-linked phosphotyrosine phosphatase CD45, which is required for antigen/CD3-induced T-cell activation. In the present work, we examine the effect of interaction between the extracellular domain of CD45 and CD22 on T-cell activation. Using soluble CD22-immunoglobulin fusion proteins and T cells expressing wild-type and chimeric CD45 forms, we show that engagement of CD45 by soluble CD22 can modulate early T-cell signals in antigen receptor/CD3-mediated stimulation. We also show that addition of sialic acid by beta-galactoside alpha-2,6-sialyltransferase to the CD22 molecule abrogates interactions between CD22 and its ligands. Together, these observations provide direct evidence for a functional role of the interaction between the extracellular domain of CD45 and a natural ligand and suggest another regulatory mechanism for CD22-mediated ligand engagement
Mots-clé
Antigens,CD/metabolism/Antigens,CD22/Antigens,CD45/Antigens,Differentiation,B-Lymphocyte/B-Lymphocytes/immunology/Calcium/Cell Adhesion Molecules/Cell Line/Humans/Inositol Phosphates/Isoenzymes/Kinetics/Lectins/Phospholipase C/Phosphorylation/Phosphotyrosine/Receptor-CD3 Complex,Antigen,T-Cell/Sialyltransferases/Tyrosine/analogs & derivatives/analysis
Pubmed
Web of science
Open Access
Oui
Création de la notice
29/01/2008 19:34
Dernière modification de la notice
20/08/2019 15:17
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