Publication Date:
1992-11-06
Description:
Ligation of the antigen receptor on B cells induces the rapid phosphorylation of tyrosine on a number of cellular proteins. A monoclonal antibody that recognized a tyrosine-phosphorylated cell surface protein that was present in activated B cells was generated. Amino acid sequence analysis showed that this 140-kilodalton protein was CD22, a B cell-specific cell surface glycoprotein and putative extracellular ligand of the protein tyrosine phosphatase CD45. Tyrosine phosphorylation of CD22 may be important in B cell signal transduction, possibly through regulation of the adhesiveness of activated B cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schulte, R J -- Campbell, M A -- Fischer, W H -- Sefton, B M -- CA 14195/CA/NCI NIH HHS/ -- CA17289/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 6;258(5084):1001-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology and Virology Laboratory, Salk Institute, San Diego, CA 92186.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1279802" target="_blank"〉PubMed〈/a〉
Keywords:
Antigens, CD/*metabolism
;
Antigens, Differentiation, B-Lymphocyte/*metabolism
;
B-Lymphocytes/*immunology
;
Burkitt Lymphoma
;
*Cell Adhesion Molecules
;
Chymotrypsin/metabolism
;
Humans
;
Immunoblotting
;
Immunosorbent Techniques
;
*Lectins
;
*Lymphocyte Activation
;
Peptide Mapping
;
Phosphorylation
;
Phosphotyrosine
;
Sialic Acid Binding Ig-like Lectin 2
;
Signal Transduction/physiology
;
Tumor Cells, Cultured
;
Tyrosine/*analogs & derivatives/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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