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Blood, Vol. 92 No. 4 (August 15), 1998:
pp. 1324-1333
Mice Deficient for the Ecto-Nicotinamide Adenine Dinucleotide
Glycohydrolase CD38 Exhibit Altered Humoral Immune Responses
Debra A. Cockayne,
Tony Muchamuel,
J. Christopher Grimaldi,
Hélène Muller-Steffner,
Troy D. Randall,
Frances E. Lund,
Richard Murray,
Francis Schuber, and
Maureen C. Howard
From the Department of Immunology, DNAX Research Institute of
Molecular and Cellular Biology, Palo Alto, CA and the Laboratoire de
Chimie Bioorganique, Faculté de Pharmacie, Université Louis
Pasteur, Strasbourg-Illkirch, France.
CD38 is a membrane-associated ecto-nicotinamide adenine dinucleotide
(NAD+) glycohydrolase that is expressed on multiple
hematopoietic cells. The extracellular domain of CD38 can mediate the
catalysis of NAD+ to cyclic adenosine
diphosphoribose (cADPR), a Ca2+-mobilizing second
messenger, adenosine diphosphoribose (ADPR), and nicotinamide. In
addition to its enzymatic properties, murine CD38 has been shown to act
as a B-cell coreceptor capable of modulating signals through the B-cell
antigen receptor. To investigate the in vivo physiological function(s)
of this novel class of ectoenzyme we generated mice carrying a null
mutation in the CD38 gene. CD38 / mice showed a
complete loss of tissue-associated NAD+ glycohydrolase
activity, showing that the classical NAD+ glycohydrolases
and CD38 are likely identical. Although murine CD38 is expressed on
hematopoietic stem cells as well as on committed progenitors, we show
that CD38 is not required for hematopoiesis or lymphopoiesis. However,
CD38/ mice did exhibit marked deficiencies in
antibody responses to T-cell-dependent protein antigens and augmented
antibody responses to at least one T-cell-independent type 2 polysaccharide antigen. These data suggest that CD38 may play an
important role in vivo in regulating humoral immune responses.
© 1998 by The American Society of Hematology.
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