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Blood, Vol. 95 No. 3 (February 1), 2000:
pp. 965-972
Switch in the protein tyrosine phosphatase associated with human
CD100 semaphorin at terminal B-cell differentiation stage
Christian Billard,
Stéphanie Delaire,
Emmanuel Raffoux,
Armand Bensussan, and
Laurence Boumsell
From Unit 448, INSERM, Faculté de Médecine Henri Mondor,
Créteil, France.
Human CD100, the first semaphorin identified in the immune system,
is a transmembrane protein involved in T-cell activation. In the
present study, we showed that activation of peripheral blood or
tonsillar B lymphocytes induced the expression of CD100 in
CD38+CD138 cell populations,
including in CD148+ subpopulations, thus expressing a
memory B-cell-like phenotype. Using an in vitro enzymatic assay, we
found that protein tyrosine phosphatase (PTP) activities
were immunoprecipitated with CD100 in these cell populations, which
were isolated by cell sorting, as well as in most B-cell
lines representing various stages of B-cell differentiation.
Immunodepletion and Western blotting experiments demonstrated that CD45
was the PTP associated with CD100 in cell lines displaying pre-B,
activated B, and pre-plasma cell phenotypes. CD45 also accounted for
PTP activity immunoprecipitated with CD100 in
CD38+CD138 cells sorted after activation
of peripheral blood or tonsillar B lymphocytes. In contrast, no
CD100-CD45 association was observed in plasma cell lines corresponding
to the terminal B-cell differentiation stage. CD148, the other
transmembrane PTP known to be implicated in lymphocyte signaling
pathways, was either only partly involved in the CD100-associated PTP
activity or not expressed in plasma cell lines, indicating the
association of CD100 with another main PTP. Our data show that CD100 is
differentially expressed and can functionally associate with distinct
PTPs in B cells depending on their activation and maturation state.
They also provide evidence for a switch in the CD100-associated PTP at
terminal stage of B-cell differentiation.

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