CD22 ASSOCIATES WITH THE HUMAN SURFACE IGM-B-CELL ANTIGEN RECEPTOR COMPLEX

被引：187
作者：
LEPRINCE, C
DRAVES, KE
GEAHLEN, RL
LEDBETTER, JA
CLARK, EA
机构：
[1] UNIV WASHINGTON, DEPT MICROBIOL SC-42, SEATTLE, WA 98195 USA
[2] PURDUE UNIV, DEPT MED CHEM, W LAFAYETTE, IN 47907 USA
[3] BRISTOL MYERS SQUIBB RES INST, SEATTLE, WA 98121 USA
来源：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1993年 / 90卷 / 08期
关键词：
MEMBRANE IMMUNOGLOBULIN; B-LYMPHOCYTE; SIGNAL TRANSDUCTION; PHOSPHORYLATION;
D O I：
10.1073/pnas.90.8.3236
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
The B-cell surface molecule CD22, when cross-linked, modulates signaling through the surface IgM (sIgM)-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 antiserum 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 Igalpha/mb-1, Igbeta/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.
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页码：3236 / 3240
页数：5
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