Majority of RNA which co-purifies with unactivated rat hepatic glucocorticoid-receptor complexes is nonspecific and not receptor-associated

Holland, Lené J.; Diehl, Edward E.; Colburn, Richard.; Schmidt, Thomas J.

doi:10.1016/0022-4731(90)90245-n

Cited by 2 publications

(1 citation statement)

References 31 publications

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“…Fraction 4 in Figure 1 corresponds to fraction 26 in an earlier report (Holland & Wangh, 1987). RNA was resolved in 1.2% agarose gels containing formaldehyde with sample buffer as described (Holland et al, 1990) and was transferred to Genescreen (Holland & Wangh, 1984). In some cases, the membrane was exposed to 254-nm UV light (580 mW/cm2, 15 cm for 3 min) and baked under vacuum for 2 h at 80 °C.…”

Section: Methodsmentioning

confidence: 99%

Xenopus liver ferritin H subunit: cDNA sequence and mRNA production in the liver following estrogen treatment

Holland¹,

Wall²,

Bhattacharya³

1991

Biochemistry

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In vitro translation of liver mRNA from estrogen-treated Xenopus frogs yields two abundant polypeptides in the range of 20 kDa. DNA clones for one of these translation products were isolated and shown to be complementary to mRNA for the heavy subunit of ferritin. The predicted Xenopus amino acid sequence shares about 86% identity with the ferritin heavy chain from bullfrogs and about 70% identity with the comparable mammalian and avian proteins. Clone identity was confirmed by hybridization selection followed by in vitro translation into translation products of 19.5-20 kDa. The nearly full-length cDNA clone, termed XlferH1, comprises 868 nucleotides plus 22 adenosines of the poly(A) tail, including 134 nucleotides of the 5'-untranslated region, a 528-base coding region for 176 amino acids, and a 206-nucleotide 3'-untranslated region. The clone lacks 22 nucleotides from the 5' end of the mRNA. The level of ferritin mRNA in the liver of estrogen-treated frogs was determined over time. The amount of this mRNA relative to total RNA decreased about 3-fold 14 days after estradiol-17 beta was administered. However, the hormone also elevated total RNA in the liver about 24-fold. Hence, the total ferritin mRNA content of the liver increased to about 8 times its initial amount. This pattern of gene expression was very similar to that for serum retinol binding protein. The estrogen induction of these two mRNAs appeared to parallel the overall stimulation of hepatic RNA synthesis.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Methodsmentioning

confidence: 99%

Xenopus liver ferritin H subunit: cDNA sequence and mRNA production in the liver following estrogen treatment

Holland¹,

Wall²,

Bhattacharya³

1991

Biochemistry

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Coordinate Regulation of Fibrinogen Subunit Messenger RNA Levels by Glucocorticoids in Primary Cultures ofXenopusLiver Parenchymal Cells

Bhattacharya

Holland

1991

Molecular Endocrinology

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Fibrinogen synthesis is specifically induced by a synthetic glucocorticoid, dexamethasone, in primary liver parenchymal cell cultures of the frog Xenopus laevis. Here we demonstrate that this increase in the level of fibrinogen protein production is accompanied by an induction in the three mRNAs coding for the fibrinogen subunits, designated A alpha, B beta, and gamma. The stimulation of fibrinogen mRNA levels appears to be mediated by the glucocorticoid receptor, because 1) the dose-response relationship parallels the reported affinity of dexamethasone for the Xenopus glucocorticoid receptor; and 2) the induction is blocked by RU 486, a potent antiglucocorticoid. All three subunit mRNA levels are induced coordinately by the hormone. The response is characterized by a detectable increase as early as 2-4 h after dexamethasone addition, continuing to a final 10- to 30-fold increase over basal levels by 60 h. The induction is specific for the fibrinogen mRNAs; total cellular RNA content and the levels of other mRNAs are unaffected by the hormone. Dexamethasone-mediated stimulation of A alpha and B beta mRNA production occurs in the absence of protein synthesis, whereas increased production of gamma mRNA is completely blocked under the same conditions. Thus, the A alpha and B beta genes are probably regulated at least in part by direct transcriptional activation by glucocorticoid-receptor complexes. Induction of the gamma gene is dependent on newly synthesized or labile proteins, which could be required for either transcription or posttranscriptional processes. These data suggest that different proteins are involved in regulation of the three fibrinogen genes.

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Majority of RNA which co-purifies with unactivated rat hepatic glucocorticoid-receptor complexes is nonspecific and not receptor-associated

Cited by 2 publications

References 31 publications

Xenopus liver ferritin H subunit: cDNA sequence and mRNA production in the liver following estrogen treatment

Xenopus liver ferritin H subunit: cDNA sequence and mRNA production in the liver following estrogen treatment

Coordinate Regulation of Fibrinogen Subunit Messenger RNA Levels by Glucocorticoids in Primary Cultures ofXenopusLiver Parenchymal Cells

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