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(Received for publication, November 21, 1996, and in revised form, March 26, 1997)
From the Transcription factors of the Stat gene family are
selectively activated by many hormones and cytokines. Stat5 originally
was cloned as a prolactin-stimulated DNA-binding protein, but is also activated by non-lactogenic cytokines in many cell types. The recent
identification of two distinct Stat5 genes, which encode a 94-kDa
Stat5a and a 92-kDa Stat5b as well as several lower molecular weight
isoforms, suggests additional complexity and combinatorial possibilities for transcriptional regulation. We now report a biochemical analysis of prolactin activation of Stat proteins in Nb2
lymphocytes, which was associated with: 1) rapid tyrosine phosphorylation of Stat5a, Stat5b, a COOH-terminally truncated 80-kDa
Stat5 form, Stat1
Volume 272, Number 22,
Issue of May 30, 1997
pp. 14098-14103
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
Intramural Research Support Program,
Laboratory of
Biochemistry and Metabolism, NIDDK, National Institutes of Health,
Bethesda, Maryland 20892, and the ** United States Food and Drug
Administration, Center for Biologic Evaluation and Research, Division
of Cytokine Biology, Bethesda, Maryland 20814
, and Stat3; 2) rapid and selective formation of
Stat5a/b heterodimers, without involvement of Stat1 or Stat3; 3)
marked serine, but not threonine phosphorylation of Stat5a and Stat5b;
and 4) the appearance of two qualitatively distinct Stat5 protein
complexes, which discriminated between oligonucleotides corresponding
to the prolactin response elements of the 
-casein and interferon
regulatory factor-1 gene promoters. Collectively, our analyses showed
that Stat5a and Stat5b respond similarly to prolactin receptor
activation, but also suggested that the two genes have evolved unique
properties that may contribute to the specificity of receptors that
utilize Stat5 signaling proteins.
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