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Activation of Stat-3 Is Involved in the Induction of Apoptosis After
Ligation of Major Histocompatibility Complex Class I
Molecules on Human Jurkat T Cells
Søren Skov,
Mette Nielsen,
Søren Bregenholt,
Niels Ødum, and
Mogens H. Claesson
From the Laboratory of Experimental Immunology, Department of
Medical Anatomy, the Panum Institute, University of
Copenhagen, Copenhagen, Denmark.
Activation of Janus tyrosine kinases (Jak) and Signal transducers
and activators of transcription (Stat) after ligation of major
histocompatibility complex class I (MHC-I) was explored in
Jurkat T cells. Cross-linking of MHC-I mediated tyrosine
phosphorylation of Tyk2, but not Jak1, Jak2, and Jak3. In addition, the
transcription factor Stat-3 was tyrosine phosphorylated in the
cytoplasma and subsequently translocated to the cell nucleus. Data
obtained by electrophoretic mobility shift assay suggested that the
activated Stat-3 protein associates with the human serum-inducible
element (hSIE) DNA-probe derived from the interferon-
activated site (GAS) in the c-fos promoter, a common DNA sequence for
Stat protein binding. An association between hSIE and Stat-3 after
MHC-I ligation was directly demonstrated by precipitating Stat-3 from
nuclear extracts with biotinylated hSIE probe and avidin-coupled
agarose. To investigate the function of the activated Stat-3, Jurkat T cells were transiently transfected with a Stat-3 isoform lacking the
transactivating domain. This dominant-negative acting Stat-3 isoform
significantly inhibited apoptosis induced by ligation of MHC-I. In
conclusion, our data suggest the involvement of the Jak/Stat signal
pathway in MHC-I-induced signal transduction in T cells.
Blood, Vol. 91 No. 10 (May 15), 1998:
pp. 3566-3573
© 1998 by The American Society of Hematology.
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