The ligand-binding domain of CD22 is needed for inhibition of the B cell receptor signal, as demonstrated by a novel human CD22-specific inhibitor compound

Journal of Experimental Medicine

Volumn 195, Issue 9, 2002, Pages 1207-1213

  Kelm, Soerge ^a   Gerlach, Judith ^c   Brossmer, Reinhard ^b   Danzer, Claus Peter ^c   Nitschke, Lars ^c  

^a UNIVERSITY OF BREMEN   (Germany)

^b UNIVERSITY OF HEIDELBERG   (Germany)

^c UNIVERSITY OF WÜRZBURG   (Germany)

Author keywords

B lymphocytes; Ca2+ flux; CD22; Sialic acid; Siglecs

Indexed keywords

B LYMPHOCYTE RECEPTOR; CD22 ANTIGEN; IMMUNOGLOBULIN M; SIALIC ACID;

ANIMAL CELL; ARTICLE; B LYMPHOCYTE; BINDING AFFINITY; CALCIUM CELL LEVEL; CALCIUM MOBILIZATION; CALCIUM TRANSPORT; CELL STIMULATION; CONTROLLED STUDY; DAUDI CELL; HUMAN; HUMAN CELL; LIGAND BINDING; MOLECULAR WEIGHT; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION;

ANIMALS; ANTIGENS, CD; ANTIGENS, CD22; ANTIGENS, DIFFERENTIATION, B-LYMPHOCYTE; BINDING SITES; CELL ADHESION MOLECULES; CELL LINE; HUMANS; IMMUNOGLOBULIN FC FRAGMENTS; KINETICS; LECTINS; LIGANDS; MICE; PROTEIN-TYROSINE-PHOSPHATASE; RECEPTORS, ANTIGEN, B-CELL; RECOMBINANT FUSION PROTEINS; SRC HOMOLOGY DOMAINS; TUMOR CELLS, CULTURED;

EID: 0037029667     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.20011783     Document Type: Article

References (28)

1. CD22 is a negative regulator or B-cell receptor signalling
2. Hyperresponsive B cells in CD22-deficient mice
3. CD22 regulates thymus-independent responses and the lifespan of B cells
4. CD22 is both a positive and negative regulator of B lymphocyte antigen receptor signal transduction: Altered signaling in CD22-deficient mice
5. A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP
6. Tuning antigen receptor signaling by CD22: Integrating cues from antigens and the microenvironment
7. New functions for the sialic acid-binding adhesion molecule CD22, a member of the growing family of Siglecs
8. Siglecs, sialic acids and innate immunity
9. Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily
10. The oligosaccharide binding specificities of CD22β, a sialic acid-specific lectin of B cells
11. The same epitope on CD22 of B lymphocytes mediates the adhesion of erythrocytes, T and B lymphocytes, neutrophils, and monocytes
12. CD22-mediated cell adhesion to cytokine-activated human endothelial cells. Positive and negative regulation by α2-6-sialylation of cellular glycoproteins
13. Masking and unmasking of the sialic acid-binding lectin activity of CD22 (Siglec-2) on B lymphocytes
14. A novel subset of murine B cells that expresses unmasked forms of CD22 is enriched in the bone marrow: Implications for B-cell homing to the bone marrow
15. Identification of CD22 ligands on bone marrow sinusoidal endothelium implicated in CD22-dependent homing of recirculating B cells
16. Crystal structure of the N-terminal domain of sialoadhesin in complex with 3′ sialyllactose at 1.85 A resolution
17. Localization of the putative sialic acid-binding site on the immunoglobulin superfamily cell-surface molecule CD22
18. Activation of B lymphocytes: Integrating signals from CD19, CD22 and FcγRIIb1
19. The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and α2-6 sialyltransferase, CD75, oil B cells
20. Sialic acid analogs and application for preparation of neoglycoconjugates
21. Functional groups of sialic acids involved in binding to siglecs (sialoadhesins) deduced from interactions with synthetic analogues
22. Transcription of the β-galactoside α2,6-sialyltransferase gene in B lymphocytes is directed by a separate and distinct promoter
23. CD22 associates with the human surface IgM-B-cell antigen receptor complex
24. Association of CD22 with the B cell antigen receptor
25. Regulation of CD45 engagement by the B-cell receptor CD22
26. Inhibition of the B cell by CD22: A requirement for Lyn
27. Interaction of CD22 with α2,6-linked sialoglyconjugates: Innate recognition of self to dampen B cell autoreactivity?
28. Sialic acid binding domains of CD22 are required for negative regulation of B cell receptor signaling