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Science 6 November 1992:
Vol. 258. no. 5084, pp. 1001 - 1004
DOI: 10.1126/science.1279802
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Articles

Science, Vol 258, Issue 5084, 1001-1004
Copyright © 1992 by American Association for the Advancement of Science

articles

Tyrosine phosphorylation of CD22 during B cell activation

RJ Schulte, MA Campbell, WH Fischer, and BM Sefton

Molecular Biology and Virology Laboratory, Salk Institute, San Diego, CA 92186.

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.


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