RP105 is associated with MD-1 and transmits an activation signal in human B cells.

RP105 was originally discovered as a mouse B-cell surface molecule that transmits an activation signal. The signal leads to resistance against irradiation-induced apoptosis and massive B-cell proliferation. Recently, we found that mouse RP105 is associated with another molecule, MD-1. We have isolated here the human MD-1 cDNA. We show that ...
human MD-1 is also associated with human RP105 and has an important role in cell surface expression of RP105. We also describe a monoclonal antibody (MoAb) that recognizes human RP105. Expression of RP105 is restricted to CD19(+) B cells. Histological studies showed that RP105 is expressed mainly on mature B cells in mantle zones. Germinal center cells are either dull or negative. RP105 is thus a novel human B-cell marker that is preferentially expressed on mature B cells. Moreover, the anti-RP105 MoAb activates B cells, leading to increases in cell size, expression of a costimulatory molecule CD80, and DNA synthesis. The B-cell activation pathway using RP105 is conserved in humans.
Mesh Terms:
Amino Acid Sequence, Animals, Antibodies, Monoclonal, Antigens, CD, Antigens, Surface, B-Lymphocytes, Base Sequence, Chickens, Cloning, Molecular, DNA, Complementary, Germinal Center, Humans, Lymphocyte Activation, Lymphoma, Macromolecular Substances, Membrane Glycoproteins, Membrane Proteins, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Palatine Tonsil, Recombinant Fusion Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Signal Transduction, Species Specificity, Tumor Cells, Cultured
Blood
Date: Oct. 15, 1998
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