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*
Department of Neuroimmunology, Max-Planck Institute of Neurobiology, D-82152 Martinsried, Germany; and
Department of Neurology, Klinikum Grosshadern, Munich, Germany
The B7 family of costimulatory molecules likely includes members
distinct from B7.1 (CD80) and B7.2 (CD86). After stimulation with
IFN-
or TNF-
, human myoblasts selectively express BB-1, but not
B7.1 or B7.2. BB-1 is detected by anti-BB-1, a mAb cross-reacting
with B7.1 (but not B7.2) and an as yet undefined costimulatory
molecule. The absence of B7.1 and B7.2 in BB-1-positive myoblasts was
confirmed by RT-PCR. The molecule detected by anti-BB-1 is
functional, because anti-BB-1 mAb and CTLA4Ig (but not
anti-B7.1- or anti-B7.2-specific mAbs) completely inhibit Ag
presentation by cytokine-induced myoblasts to HLA-DR-matched
Ag-specific CD4+ T cell lines. Stimulation of myoblasts
with IL-4 induces B7.1 and B7.2, as well as BB-1, but with different
time kinetics. Stimulation of CD40-positive myoblasts with
anti-CD40 mAb selectively induces BB-1, whereas stimulation with
CD40L-transfected mouse L cells induces BB-1 and B7.1, with different
kinetics. To assess whether BB-1 is expressed in muscle tissue, we
investigated 23 muscle biopsy specimens from patients with
polymyositis, dermatomyositis, inclusion body myositis, Duchenne
muscular dystrophy, and nonmyopathic controls by immunohistochemistry
and confocal laser microscopy. We found that, in all inflammatory
myopathy cases, but not in normal muscle, many muscle fibers strongly
react with anti-BB-1. In contrast, muscle fibers did not react with
B7.1- or B7.2-monospecific mAbs in any of the pathologic specimens or
in normal muscle. Our results demonstrate that human muscle cells can
be induced to selectively express BB-1, a functional costimulatory
molecule distinct from B7.1 and B7.2. This molecule may play an
important role in the immunobiology of muscle.
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