Independently ligating CD38 and FcγRIIB relays a dominant negative signal to B cells

Alyce M. Oliver, J. Christopher Grimaldi, Maureen C. Howard, John F. Kearney

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

CD38 is expressed on a variety of hematopoietic cells and has a unique enzymatic activity that converts nicotinamide adenine dinucleotide (NAD) into cyclic ADP-ribose (cADPR) and then into ADPR. CD38 is expressed at increasingly higher levels on B cells at each stage of B cell differentiation, and is then down-regulated on germinal center B cells and mature plasma cells. Crosslinking of CD38 on the surface of mature, resting B cells induces B-cell proliferation, which is enhanced by co-signals such as IL-4 and LPS. CD38-induced proliferation is abrogated by FcγRIIB ligation and this inhibition can be effected by the addition of anti-FcγRII Ab midway through a 48 h in vitro culture indicating that it delivers a potent negative signal to CD38 activated B cells. The suppressive signal was shown to occur through the FcγRIIB because CD38-induced B-cell activation was not inhibited by the ligation of FcγRIIB in FcγRII-deficient B cells. These results indicate that FcγRIIB can act as a regulatory molecule that modulates CD38 signals in vivo.

Original languageEnglish (US)
Pages (from-to)113-119
Number of pages7
JournalHybridoma
Volume18
Issue number2
DOIs
Publication statusPublished - Jan 1 1999
Externally publishedYes

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ASJC Scopus subject areas

  • Immunology
  • Genetics

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