scholarly journals Sequence complementarity between the 5'-terminal regions of mRNAs for rat mitochondrial cytochrome P-450c27/25 and a growth hormone-inducible serine protease inhibitor. A possible gene overlap.

1992 ◽  
Vol 267 (4) ◽  
pp. 2421-2428 ◽  
Author(s):  
R M Shayiq ◽  
N G Avadhani
Keyword(s):  
Growth Hormone ◽  
Protease Inhibitor ◽  
Serine Protease ◽  
Serine Protease Inhibitor ◽  
Mitochondrial Cytochrome ◽  
Sequence Complementarity ◽  
Gene Overlap

scholarly journals Modulation of the Growth Hormone Response of the Serine Protease Inhibitor 2.1 Gene by Cytokines in Rat Hepatocytes

1999 ◽  
Vol 45 (4, Part 2 of 2) ◽  
pp. 85A-85A
Author(s):  
S A Berry ◽  
P L Bergad ◽  
S J Schwarzenberg ◽  
S Amarasinghe ◽  
H C Towle
Keyword(s):  
Growth Hormone ◽  
Protease Inhibitor ◽  
Serine Protease ◽  
Rat Hepatocytes ◽  
Serine Protease Inhibitor ◽  
Growth Hormone Response ◽  
Hormone Response

scholarly journals Growth hormone rapidly activates rat serine protease inhibitor 2.1 gene transcription and induces a DNA-binding activity distinct from those of Stat1, -3, and -4.

1995 ◽  
Vol 15 (1) ◽  
pp. 12-18 ◽  
Author(s):  
M J Thomas ◽  
A M Gronowski ◽  
S A Berry ◽  
P L Bergad ◽  
P Rotwein
Keyword(s):  
Gene Expression ◽  
Growth Hormone ◽  
Protease Inhibitor ◽  
Protein Binding ◽  
Serine Protease ◽  
Dna Sequences ◽  
Gene Promoter ◽  
Serine Protease Inhibitor ◽  
Gh Treatment ◽  
Gh Receptor

Transcriptional regulation by growth hormone (GH) represents the culmination of signal transduction pathways that are initiated by the cell surface GH receptor and are targeted to the nucleus. Recent studies have demonstrated that the activated GH receptor can stimulate Stat1, a cytoplasmic transcription factor that becomes tyrosine phosphorylated and translocates to the nucleus, where it can interact with specific DNA sequences to modulate gene expression. GH also has been found to induce protein binding to a portion of the rat serine protease inhibitor (Spi) 2.1 gene promoter that is required for GH-induced transcription of Spi 2.1. Using GH-deficient hypophysectomized rats as a model, we show that GH treatment rapidly and potently induces both nuclear Spi 2.1 mRNA expression in the liver and specific nuclear protein binding to a 45-bp segment of the Spi 2.1 gene promoter. A GH-inducible gel-shifted complex appears within 15 min of systemic hormone administration and can be inhibited by an antiphosphotyrosine monoclonal antibody but is not blocked by a polyclonal antiserum to Stat1, Stat3, or Stat4, even though the nucleotide sequence contains two gamma interferon-activated sequence-like elements that could interact with STAT proteins. By Southwestern (DNA-protein) blot analysis, approximately 41- and 35-kDa GH-inducible proteins were detected in hepatic nuclear extracts with the Spi 2.1 DNA probe. Thus, a GH-activated signaling pathway stimulates Spi 2.1 gene expression through a unique mechanism that does not appear to involve known members of the STAT family of transcription factors.

Discoordinate hormonal and ontogenetic regulation of four rat serpin genes

1992 ◽  
Vol 262 (5) ◽  
pp. C1144-C1148 ◽  
Author(s):  
S. J. Schwarzenberg ◽  
J. B. Yoon ◽  
S. Seelig ◽  
C. J. Potter ◽  
S. A. Berry
Keyword(s):  
Growth Hormone ◽  
Protease Inhibitor ◽  
Serine Protease ◽  
Serine Protease Inhibitor ◽  
Age Group ◽  
Serum Growth Hormone ◽  
Physiological Conditions ◽  
Specific Mrnas ◽  
Alpha 1 Antitrypsin ◽  
Inhibitor Genes

To understand the roles of four highly homologous rat hepatic serine protease inhibitor genes (Spi 2.1, Spi 2.2, Spi 2.3, and alpha 1-antitrypsin), we measured the hepatic content of their specific mRNAs under several physiological conditions. Spi 2.1 and 2.3 mRNAs, which are regulated by growth hormone, paralleled serum growth hormone levels developmentally. Only Spi 2.1 mRNA decreased with starvation, while Spi 2.2, 2.3, and alpha 1-antitrypsin mRNAs did not change. Despite the close homology of the Spi genes to mouse contrapsin, which is regulated by testosterone, none of the serine protease inhibitor mRNAs examined here was dependent on androgens for expression. Spi 2.2 mRNA displayed a unique ontogenetic regulation, with a rise in hepatic content at day 19 to levels five times that of any other age group. These studies confirm the importance of growth hormone in the regulation of Spi 2.1 and 2.3 mRNAs and suggest that Spi 2.2 mRNA may be regulated by metabolic alterations occurring in the weaning period.

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