Published online 24 November 2003 doi:10.1084/jem.20031428
© Rockefeller University Press,
0022-1007/2003/12/1699 $5.00
The Journal of Experimental Medicine, Volume 198, Number 11, 1699-1706
Identification of a Pre-BCR Lacking Surrogate Light Chain
Yu-wen Su,
Alexandra Flemming,
Thomas Wossning,
Elias Hobeika,
Michael Reth and
Hassan Jumaa
Institute for Biology III, Albert-Ludwigs University of Freiburg, and Max Planck Institute for Immunobiology, 79108 Freiburg, Germany
Address correspondence to Hassan Jumaa, Max Planck Institute for Immunobiology, Stuebeweg 51, D-79108 Freiburg, Germany. Phone: 49-761-5108437; Fax: 49-761-5108423; email: jumaa{at}immunbio.mpg.de
SLP-65-/- pre-B cells show a high proliferation rate in vitro. We have shown previously that 
5 expression and consequently a conventional pre-B cell receptor (pre-BCR) are essential for this proliferation. Here, we show that pre-B cells express a novel receptor complex that contains a µ heavy chain (µHC) but lacks any surrogate (SL) or conventional light chain (LC). This SL-deficient pre-BCR (SL-pre-BCR) requires Ig-
for expression on the cell surface. Anti-µ treatment of pre-B cells expressing the SL-pre-BCR induces tyrosine phosphorylation of substrate proteins and a strong calcium (Ca2+) release. Further, the expression of the SL-pre-BCR is associated with a high differentiation rate toward 
LC-positive cells. Given that B cell development is only partially blocked and allelic exclusion is unaffected in SL-deficient mice, we propose that the SL-pre-BCR is involved in these processes and therefore shares important functions with the conventional pre-BCR.
Key Words: B cell development • adaptor • signaling • proliferation • receptor
Y.-w. Su and A. Flemming contributed equally to this work.
Abbreviations used in this paper: BCR, B cell receptor; HC, heavy chain; LAT, linker for activation of T cells; LC, light chain; PLC, phospholipase C; PTK, protein tyrosine kinase; SL, surrogate light chain.
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