Format

Send to

Choose Destination
See comment in PubMed Commons below
J Exp Med. 1993 Aug 1;178(2):469-78.

A complex of glycoproteins is associated with VpreB/lambda 5 surrogate light chain on the surface of mu heavy chain-negative early precursor B cell lines.

Author information

1
Basel Institute for Immunology, Switzerland.

Abstract

Monoclonal antibodies (mAbs) have been made specific for the pre-B cell-specific proteins VpreB and lambda 5 which together form the surrogate light (L) chain. mAbs specific for VpreB protein identified the 16-kD molecule associated on precursor B cell lines with lambda 5 protein as the product of the VpreB gene. Surrogate L chain was detectable even in the absence of mu heavy (H) chain on the surface of early precursor cell lines such as pro-B cell lines where all immunoglobulin (Ig) loci are in the germline configuration, as well as early pre-B cell lines where Ig H chain loci are DHJH rearranged in reading frame I or III, which does not allow the expression of a DHJHC mu protein. A complex of glycoproteins (200, 130, 105, and 65-35 kD) was identified as coprecipitated with the Vpreb/lamba 5 surrogate L chain in mu H chain-negative precursor B cell lines. The 130-kD protein was most strongly labeled with iodine and most consistently detected in noncovalent association with surrogate L chain. This protein turned out to be a N-linked glycoprotein with a 100-kD protein core and isoelectric point 5.8, indicating that it is distinct from CD43 and the BP-1/6C3 antigen. The surface deposition of the surrogate L chain in association with the newly identified glycoproteins suggests that the surrogate L chain may function as a receptor even before the association with mu H chain in early precursor B cells.

PMID:
8340754
PMCID:
PMC2191143
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Support Center