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Blood, Vol. 93 No. 12 (June 15), 1999:
pp. 4336-4346
The Human ( L+µ ) proB Complex: Cell
Surface Expression and Biochemical Structure of a Putative Transducing
Receptor
Bénédicte Lemmers,
Laurent Gauthier,
Valérie Guelpa-Fonlupt,
Michel Fougereau, and
Claudine Schiff
From the Centre d'Immunologie de Marseille-Luminy, Marseille,
France.
The surrogate light chain ( L) associates with µ and Ig -Ig
chains to form the preB-cell receptor that plays a critical role in
early B-cell differentiation. Discrepancies exist in human concerning
the existence of L+µ proB cells and
the biochemical structure of such a proB-cell complex remains elusive.
Among new antihuman VpreB monoclonal antibodies (MoAbs), 5 of the
  isotype bound to recombinant and native VpreB protein with high
affinity. They recognized 4 discrete epitopes, upon which 2 were in the
extra-loop fragment. Such MoAbs detected the L at the cell surface
of either preB or on both proB and preB cells. The previously reported
SLC1/SLC2 MoAbs recognize a conformational epitope specific for the
µ/L association in accordance with their preB-cell reactivity.
Using the proB/preB 4G7 MoAb, L cell surface expression was detected
on normal bone marrow, not only on
CD34CD19+ preB but also on
CD34+CD19+ proB cells. Futhermore, this
MoAb identified L+µ fresh proB
leukemic cells of the TEL/AML1 type. Biochemical studies showed that,
at the proB stage, the L is associated noncovalently with two
proteins of 105 and 130 kD. Triggering of this complex induces
intracellular Ca2+ flux, suggesting that the L may be
involved in a new receptor at this early step of the B-cell differentiation.
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