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CD22 associates with the human surface IgM-B-cell antigen receptor complex.
Proc Natl Acad Sci U S A. 1993 Apr 15; 90(8):3236-40.PN

Abstract

The B-cell surface molecule CD22, when cross-linked, modulates signaling through the surface IgM (sIgM)-B-cell receptor (BCR) complex. Here we analyzed the basis of this interaction between CD22 and the human sIgM complex. After lysis of B cells or B-cell lines in digitonin, CD22 coimmunoprecipitated a kinase activity that in vitro-phosphorylated two polypeptides of 150 and 130 kDa on tyrosine residues. By immunoblot analysis with a rabbit anti-serum specific for a synthetic peptide of CD22, we found these proteins to be CD22 itself. Furthermore, the phosphorylated 150-kDa CD22 was found in the sIgM-BCR complex maintained by digitonin, along with Ig alpha/mb-1, Ig beta/B29, and a 75-kDa polypeptide precipitated by an antiserum specific to protein-tyrosine kinase PTK72. CD22 is likely to be an important signaling partner in the sIgM-BCR complex since it is very rapidly and strikingly phosphorylated after sIgM is cross-linked and since it contains the antigen recognition homology I (ARHI) motif, present in other antigen receptor molecules.

Authors+Show Affiliations

Department of Microbiology, University of Washington, Seattle 98195.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

8475064

Citation

Leprince, C, et al. "CD22 Associates With the Human Surface IgM-B-cell Antigen Receptor Complex." Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no. 8, 1993, pp. 3236-40.
Leprince C, Draves KE, Geahlen RL, et al. CD22 associates with the human surface IgM-B-cell antigen receptor complex. Proc Natl Acad Sci U S A. 1993;90(8):3236-40.
Leprince, C., Draves, K. E., Geahlen, R. L., Ledbetter, J. A., & Clark, E. A. (1993). CD22 associates with the human surface IgM-B-cell antigen receptor complex. Proceedings of the National Academy of Sciences of the United States of America, 90(8), 3236-40.
Leprince C, et al. CD22 Associates With the Human Surface IgM-B-cell Antigen Receptor Complex. Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3236-40. PubMed PMID: 8475064.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - CD22 associates with the human surface IgM-B-cell antigen receptor complex. AU - Leprince,C, AU - Draves,K E, AU - Geahlen,R L, AU - Ledbetter,J A, AU - Clark,E A, PY - 1993/4/15/pubmed PY - 1993/4/15/medline PY - 1993/4/15/entrez SP - 3236 EP - 40 JF - Proceedings of the National Academy of Sciences of the United States of America JO - Proc Natl Acad Sci U S A VL - 90 IS - 8 N2 - The B-cell surface molecule CD22, when cross-linked, modulates signaling through the surface IgM (sIgM)-B-cell receptor (BCR) complex. Here we analyzed the basis of this interaction between CD22 and the human sIgM complex. After lysis of B cells or B-cell lines in digitonin, CD22 coimmunoprecipitated a kinase activity that in vitro-phosphorylated two polypeptides of 150 and 130 kDa on tyrosine residues. By immunoblot analysis with a rabbit anti-serum specific for a synthetic peptide of CD22, we found these proteins to be CD22 itself. Furthermore, the phosphorylated 150-kDa CD22 was found in the sIgM-BCR complex maintained by digitonin, along with Ig alpha/mb-1, Ig beta/B29, and a 75-kDa polypeptide precipitated by an antiserum specific to protein-tyrosine kinase PTK72. CD22 is likely to be an important signaling partner in the sIgM-BCR complex since it is very rapidly and strikingly phosphorylated after sIgM is cross-linked and since it contains the antigen recognition homology I (ARHI) motif, present in other antigen receptor molecules. SN - 0027-8424 UR - https://www.unboundmedicine.com/medline/citation/8475064/CD22_associates_with_the_human_surface_IgM_B_cell_antigen_receptor_complex_ L2 - http://www.pnas.org/cgi/pmidlookup?view=long&pmid=8475064 DB - PRIME DP - Unbound Medicine ER -