Published online before print September 11, 2008
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* Université Paris 13, EA 3406, Service de biochimie, APHP, Hôpital Avicenne, Cedex, France;
CNRS FRE 2937, Institut Lwoff, Villejuif, France;
Unité Mixte de Recherche (UMR), Centre National de la Recherche Scientifique (CNRS) 6101, and Laboratoire dHématologie, Centre Hospitalier Universitaire (CHU) Dupuytren and Faculté de Médecine, Université de Limoges, France; and
Forschungszentrum für Umwelt und Gesundheit (GSF), Institute of Clinical Molecular Biology and Tumor Genetics, Munich, Germany
2 Correspondence: Service de biochimie, Hôpital Avicenne, 125 route de Stalingrad, 93009 Bobigny Cedex, France. E-mail: remi.fagard{at}avc.aphp.fr
Alternate splicing of STAT1 produces two isoforms:
, known as the active form, and β, previously shown to act as a dominant-negative factor. Most studies have dealt with STAT1
, showing its involvement in cell growth control and cell death. To examine the specific function of either isoform in cell death, a naturally STAT1-deficient human B cell line was transfected to express STAT1
or STAT1β. STAT1
, expressed alone, enhanced cell death, potentiated the fludarabine-induced apoptosis, and enhanced the nuclear location, the phosphorylation, and the transcriptional activity of p53. Unexpectedly, STAT1β, expressed alone, induced cell death through a mechanism that was independent of the nuclear function of p53. Indeed, in STAT1β-expressing B cells, p53 was stricktly cytoplasmic where it formed clusters, and there was no induction of the transcriptional activity of p53. These data reveal a novel role of STAT1β in programmed cell death, which is independent of p53.
Key Words: B lymphocytes p53 fludarabine