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PMID: 9143697 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

CD22, a B lymphocyte-specific adhesion molecule that regulates antigen receptor signaling.

Annual review of immunology ·Vol. 15 ·1997-00-00 ·Pages 481-504

Tedder TF, Tuscano J, Sato S, Kehrl JH

Abstract

The development of B lymphocytes is a highly regulated process that depends in part on lineage-specific cell surface molecules. In addition, transmembrane signals generated through the B cell antigen receptor and other surface molecules regulate B cell responses to foreign antigens. Recent studies reveal CD22 to be a functionally significant receptor during these processes. CD22 is first expressed in the cytoplasm of pro-B and pre-B cells, and on the surface as B cells mature to become IgD+. CD22 is a member of the Ig superfamily that serves as an adhesion receptor for sialic acid-bearing ligands expressed on erythrocytes and all leukocyte classes. In addition to its potential role as a mediator of intercellular interactions, signal transduction through CD22 can activate B cells and modulate antigen receptor signaling in vitro. CD22 signaling is mediated via interactions with a number of kinases and phosphatases that bind the cytoplasmic domain through phosphorylated tyrosine residues located within consensus TAM and TIM motifs. The phenotype of CD22-deficient mice suggests that CD22 is primarily involved in the generation of mature B cells within the bone marrow, blood, and marginal zones of lymphoid tissues. Most notable in CD22-deficient mice is a significant diminution of surface Ig levels in these B cell subpopulations, which suggests that CD22 functions in vivo to adjust the signaling threshold of cell surface antigen receptors. A further understanding of CD22 function is required and may reveal roles for CD22 in disease susceptibility or the development of autoimmunity.

MeSH Terms
Amino Acid Sequence Animals Antigens, CD/chemistry,genetics,metabolism Antigens, Differentiation, B-Lymphocyte/chemistry,genetics,metabolism B-Lymphocytes/immunology Carbohydrate Sequence Cell Adhesion Molecules/chemistry,genetics,metabolism Chromosome Mapping Humans Lectins Ligands Mice Molecular Sequence Data Molecular Structure Receptors, Antigen, B-Cell/metabolism Sequence Homology, Amino Acid Sialic Acid Binding Ig-like Lectin 2 Signal Transduction
Chemicals
Antigens, CD Antigens, Differentiation, B-Lymphocyte CD22 protein, human Cd22 protein, mouse Cell Adhesion Molecules Lectins Ligands Receptors, Antigen, B-Cell Sialic Acid Binding Ig-like Lectin 2
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Tedder T F
Department of Immunology, Duke University Medical Center, Durham, North Carolina 27710, USA. tedde003@mc.duke.edu
Tuscano J
Sato S
Kehrl J H
Article Info
Journal
Annual review of immunology
Abbr.
Annu Rev Immunol
ISSN
0732-0582
Published
1997-00-00
Pages
481-504
Language
English
Region
United States
NLM ID
8309206
Subset
IM
Grants
NIAID NIH HHS · R01AI31678 · United States
NIAID NIH HHS · R01AI35987 · United States
NIAID NIH HHS · R01AI37180 · United States
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