Molecular characterization of fusion regulatory protein-1 (FRP-1) that induces multinucleated giant cell formation of monocytes and HIV gp160-mediated cell fusion. FRP-1 and 4F2/CD98 are identical molecules.
1995; American Association of Immunologists; Volume: 155; Issue: 7 Linguagem: Inglês
10.4049/jimmunol.155.7.3585
ISSN1550-6606
AutoresShinji Ohgimoto, Nobutada Tabata, Shigeru Suga, Machiko Nishio, H Ohta, Masato Tsurudome, Hiroshi Komada, Mitsuo Kawano, Nobumoto Watanabe, Yasuhiko Ito,
Tópico(s)Virus-based gene therapy research
ResumoFusion regulatory protein (FRP)-1 regulates virus-mediated cell fusion and fusion of monocytes. Eleven of fifteen N-terminal amino acids of FRP-1 were the same as the amino acid sequence of 4F2/CD98 heavy chain. FRP-1 molecules were detected in Con A- or IL-2-stimulated lymphocytes, while FRP-1 was rare on resting lymphocytes. These properties of FRP-1 are similar to those of 4F2/CD98. Treatment of monocytes with anti-4F2/CD98 mAbs resulted in cell fusion, and other mAbs directed against 4F2/CD98 induced formation of multinucleated giant cells of Cd+U2ME-7 cells, a CD4+U937 cell line transfected with the HIV gp160 gene. Both anti-4F2/CD98 and anti-FRP-1 mAbs reacted with murine L929 cells expressing human 4F2/CD98 transiently or constitutively. When Newcastle disease virus (NDV)-infected L929 cells expressing human FRP-1/CD98 were incubated with mAb 4-5-1, an anti-FRP-1 mAb, multinucleated giant cells were induced; thus, FRP-1/CD98 molecules expressed in L929 cells are functional for fusion regulatory activity.
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