Gene Review:
CD22 - CD22 molecule
Homo sapiens
Synonyms:
B-cell receptor CD22, B-lymphocyte cell adhesion molecule, BL-CAM, SIGLEC-2, SIGLEC2, ...
- The immunophenotype of splenic lymphoma with villous lymphocytes and its relevance to the differential diagnosis with other B-cell disorders. Matutes, E., Morilla, R., Owusu-Ankomah, K., Houlihan, A., Catovsky, D. Blood (1994)
- A bispecific recombinant immunotoxin, DT2219, targeting human CD19 and CD22 receptors in a mouse xenograft model of B-cell leukemia/lymphoma. Vallera, D.A., Todhunter, D.A., Kuroki, D.W., Shu, Y., Sicheneder, A., Chen, H. Clin. Cancer Res. (2005)
- Association of CD22 with the B cell antigen receptor. Peaker, C.J., Neuberger, M.S. Eur. J. Immunol. (1993)
- Detection of membrane and intracellular antigens by flow cytometry following ORTHO PermeaFix fixation. Pizzolo, G., Vincenzi, C., Nadali, G., Veneri, D., Vinante, F., Chilosi, M., Basso, G., Connelly, M.C., Janossy, G. Leukemia (1994)
- CD22, a B lymphocyte-specific adhesion molecule that regulates antigen receptor signaling. Tedder, T.F., Tuscano, J., Sato, S., Kehrl, J.H. Annu. Rev. Immunol. (1997)
- Toxin-labeled monoclonal antibodies. Kreitman, R.J. Current pharmaceutical biotechnology. (2001)
- CD22-mediated cell adhesion to cytokine-activated human endothelial cells. Positive and negative regulation by alpha 2-6-sialylation of cellular glycoproteins. Hanasaki, K., Varki, A., Powell, L.D. J. Biol. Chem. (1995)
- Antitumor efficacy of a combination of CMC-544 (inotuzumab ozogamicin), a CD22-targeted cytotoxic immunoconjugate of calicheamicin, and rituximab against non-Hodgkin's B-cell lymphoma. DiJoseph, J.F., Dougher, M.M., Kalyandrug, L.B., Armellino, D.C., Boghaert, E.R., Hamann, P.R., Moran, J.K., Damle, N.K. Clin. Cancer Res. (2006)
- Characterization of RFB4-Pseudomonas exotoxin A immunotoxins targeted to CD22 on B-cell malignancies. Mansfield, E., Pastan, I., FitzGerald, D.J. Bioconjug. Chem. (1996)
- CD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase C-gamma(1) upon B cell activation. Law, C.L., Sidorenko, S.P., Chandran, K.A., Zhao, Z., Shen, S.H., Fischer, E.H., Clark, E.A. J. Exp. Med. (1996)
- cDNA cloning of the B cell membrane protein CD22: a mediator of B-B cell interactions. Wilson, G.L., Fox, C.H., Fauci, A.S., Kehrl, J.H. J. Exp. Med. (1991)
- Sialoadhesin, a macrophage sialic acid binding receptor for haemopoietic cells with 17 immunoglobulin-like domains. Crocker, P.R., Mucklow, S., Bouckson, V., McWilliam, A., Willis, A.C., Gordon, S., Milon, G., Kelm, S., Bradfield, P. EMBO J. (1994)
- CD22 regulates B cell receptor-mediated signals via two domains that independently recruit Grb2 and SHP-1. Otipoby, K.L., Draves, K.E., Clark, E.A. J. Biol. Chem. (2001)
- A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP. Doody, G.M., Justement, L.B., Delibrias, C.C., Matthews, R.J., Lin, J., Thomas, M.L., Fearon, D.T. Science (1995)
- Identification and characterization of plasma cells in normal human bone marrow by high-resolution flow cytometry. Terstappen, L.W., Johnsen, S., Segers-Nolten, I.M., Loken, M.R. Blood (1990)
- Regulation of CD45 engagement by the B-cell receptor CD22. Sgroi, D., Koretzky, G.A., Stamenkovic, I. Proc. Natl. Acad. Sci. U.S.A. (1995)
- Natural ligands of the B cell adhesion molecule CD22 beta carry N-linked oligosaccharides with alpha-2,6-linked sialic acids that are required for recognition. Powell, L.D., Sgroi, D., Sjoberg, E.R., Stamenkovic, I., Varki, A. J. Biol. Chem. (1993)
- Distinct endocytic mechanisms of CD22 (Siglec-2) and Siglec-F reflect roles in cell signaling and innate immunity. Tateno, H., Li, H., Schur, M.J., Bovin, N., Crocker, P.R., Wakarchuk, W.W., Paulson, J.C. Mol. Cell. Biol. (2007)
- The B cell coreceptor CD22 associates with AP50, a clathrin-coated pit adapter protein, via tyrosine-dependent interaction. John, B., Herrin, B.R., Raman, C., Wang, Y.N., Bobbitt, K.R., Brody, B.A., Justement, L.B. J. Immunol. (2003)
- Analysis of tyrosine phosphorylation-dependent interactions between stimulatory effector proteins and the B cell co-receptor CD22. Yohannan, J., Wienands, J., Coggeshall, K.M., Justement, L.B. J. Biol. Chem. (1999)
- Myelin-associated glycoprotein binding to gangliosides. Structural specificity and functional implications. Schnaar, R.L., Collins, B.E., Wright, L.P., Kiso, M., Tropak, M.B., Roder, J.C., Crocker, P.R. Ann. N. Y. Acad. Sci. (1998)
- The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and alpha 2-6 sialyltransferase, CD75, on B cells. Stamenkovic, I., Sgroi, D., Aruffo, A., Sy, M.S., Anderson, T. Cell (1991)
- The B-cell adhesion molecule CD22 is cross-species reactive and recognizes distinct sialoglycoproteins on different functional T-cell sub-populations. Sgroi, D., Stamenkovic, I. Scand. J. Immunol. (1994)
- Expression and structure of CD22 in acute leukemia. Boué, D.R., LeBien, T.W. Blood (1988)
- CD19 regulates intrinsic B lymphocyte signal transduction and activation through a novel mechanism of processive amplification. Fujimoto, M., Poe, J.C., Hasegawa, M., Tedder, T.F. Immunol. Res. (2000)
- Constitutive endocytosis and degradation of CD22 by human B cells. Shan, D., Press, O.W. J. Immunol. (1995)
- CD19 and CD22 regulate a B lymphocyte signal transduction pathway that contributes to autoimmunity. Tedder, T.F., Sato, S., Poe, J.C., Fujimoto, M. The Keio journal of medicine. (2000)
- CD22 cross-linking generates B-cell antigen receptor-independent signals that activate the JNK/SAPK signaling cascade. Tuscano, J.M., Riva, A., Toscano, S.N., Tedder, T.F., Kehrl, J.H. Blood (1999)
- CD22-mediated stimulation of T cells regulates T-cell receptor/CD3-induced signaling. Aruffo, A., Kanner, S.B., Sgroi, D., Ledbetter, J.A., Stamenkovic, I. Proc. Natl. Acad. Sci. U.S.A. (1992)
- A single N-linked glycosylation site is implicated in the regulation of ligand recognition by the I-type lectins CD22 and CD33. Sgroi, D., Nocks, A., Stamenkovic, I. J. Biol. Chem. (1996)
- Human circulating specific antibody-forming cells after systemic and mucosal immunizations: differential homing commitments and cell surface differentiation markers. Quiding-Järbrink, M., Lakew, M., Nordström, I., Banchereau, J., Butcher, E., Holmgren, J., Czerkinsky, C. Eur. J. Immunol. (1995)
- Haptoglobin interacts with the human mast cell line HMC-1 and inhibits its spontaneous proliferation. El-Ghmati, S.M., Arredouani, M., Van Hoeyveld, E.M., Ceuppens, J.L., Stevens, E.A. Scand. J. Immunol. (2002)
- Cytokine response of B lymphocytes from splenic lymphoma with villous lymphocytes: correlation with TNF-RII (p75) and CD11c expression. Treton, D., Valensi, F., Troussard, X., Gras, G., Flandrin, G., Galanaud, P., Richard, Y. Hematology and cell therapy. (1996)