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(Received for publication, July 7, 1995; and in revised form, August 8,
1995) A growth hormone (GH)-inducible nuclear factor (GHINF) from rat
liver has been purified to near homogeneity. On SDS-polyacrylamide gel
electrophoresis and UV-cross-linking, a major band of mass
Volume 270,
Number 42,
Issue of October 20, 1995 pp. 24903-24910
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
-Activated Sites
93 kDa
and a minor band of
70 kDa are detected in the purified fraction.
DNase I footprinting using purified GHINF yields a protected region of
-149/-115 on the rat serine protease inhibitor 2.1 (Spi
2.1) promoter encompassed within the growth hormone response element
(GHRE). Mutational analysis demonstrated that GHINF binds
synergistically to two
-interferon-activated sites (GAS) within
the GHRE, with the 3` element being the pivotal binding domain.
Functional assays show that both GAS elements are necessary for full GH
response. GHINF has no immunoreactivity with either a C-terminal Stat1
antibody or an N-terminal Stat3 antibody, while cross-reacting with a
C-terminal Stat5 monoclonal antibody. GHINF will bind to two GAS
elements from the Stat5 binding region of the
-casein gene. These
studies indicate that GHINF is a Stat5-related factor binding
synergistically to two GAS elements to activate Spi 2.1 transcription.
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