An estrogen-dependent polysomal protein binds to the 5′ untranslated region of the chicken vitellogenin mRNA

Liang, Haimin; Jost, Jean-Pierre

doi:10.1093/nar/19.9.2289

Cited by 28 publications

(12 citation statements)

References 38 publications

(27 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Coding region stability determinants have also been described in c-/os, tubulin, and interleukin-2 (IL-2) a-receptor mRNAs (Yen et al 1988a,b;Shyu et al 1989Shyu et al , 1990Kanamori et al 1990). Our results are also consistent with experiments describing trans-acting factors that influence the half-lives of specific mRNAs in intact cells (Schuler and Cole 1988;Casey et al 1989;Kuchka et al 1989;Mullner et al 1989;Stern and Gruissem 1989;Weber et al 1989;Wager and Assoian 1990;Bohjanen et al 1991;Brewer 1991;Liang and Jost 1991;Malter and Hong 1991).…”

Section: Discussionsupporting

confidence: 91%

Control of c-myc mRNA half-life in vitro by a protein capable of binding to a coding region stability determinant.

Bernstein

Herrick²,

Prokipcak³

et al. 1992

Genes Dev.

286

239

View full text Add to dashboard Cite

Polysome-associated c-tnyc mRNA is degraded relatively rapidly in cells and in an in vitro mRNA decay system containing extracts from cultured mammalian cells. Using this system, a competition/screening assay was devised to search for factors that bind to specific regions of polysome-associated c-myc mRNA and thereby alter its half-life. mRNA stability was first assayed in reactions containing exogenous competitor RNAs corresponding to portions of c-myc mRNA itself. The addition of a 182-nucleotide sense strand fragment from the carboxy-terminal portion of the c-myc-coding region destabilized c-myc mRNA by at least eightfold. This RNA fragment had no effect on the stability of other mRNAs tested. Moreover, c-myc mRNA was not destabilized in reactions containing unrelated competitor RNAs or sense strand RNA from the c-myc 5' region. Polysome-associated globin mRNA containing the c-myc-coding region segment in-frame was also destabilized in vitro by the 182-nucleotide RNA. As determined by UV-cross-linking experiments, the 182-nucleotide RNA fragment was recognized by and bound to an ~75-kD polysome-associated protein. On the basis of these data plus Northern blotting analyses of c-myc mRNA decay products, we suggest that the ~75-kD protein is normally bound to a c-myc-coding region determinant and protects that region of the mRNA from endonuclease attack. Possible links between the protective protein, translation, ribosome pausing, and c-myc mRNA turnover are discussed.

show abstract

Section: Discussionsupporting

confidence: 91%

Control of c-myc mRNA half-life in vitro by a protein capable of binding to a coding region stability determinant.

Bernstein

Herrick²,

Prokipcak³

et al. 1992

Genes Dev.

286

239

View full text Add to dashboard Cite

show abstract

“…UV crosslinking studies revealed a protein from cytosolic and polysomal fractions which binds to the 5' end of avian vitellogenin mRNA (33). However, since only polysomes were assayed for estrogen inducibility in that study, it is not known whether the protein was recruited from the cytosol or actually induced by estrogen.…”

Section: Resultsmentioning

confidence: 90%

An estrogen-inducible protein binds specifically to a sequence in the 3' untranslated region of estrogen-stabilized vitellogenin mRNA.

Dodson¹,

Shapiro²

1994

Mol. Cell. Biol.

View full text Add to dashboard Cite

The 3' untranslated region (3'-UTR) has been implicated in the estrogen stabilization of hepatic Xenopus laevis vitellogenin mRNA. We used RNA gel mobility shift assays to demonstrate that Xenopus liver contains a factor which binds with very high specificity to a segment of the 3'-UTR of vitellogenin B1 and B2 mRNAs. We detected a single high-affinity binding site in the vitellogenin mRNA 3'-UTR and localized the binding site to a 27-nucleotide region. Since binding was abolished by proteinase K digestion, at least a component of the factor is a protein. Following estrogen administration, binding was induced approximately four-to fivefold in extracts from liver polysomes. The hepatic vitellogenin mRNA-binding protein was found in both polysomes and cytosol. Since the protein was also estrogen inducible in cytosol, this represents a genuine induction, not simply recruitment of the cytosolic protein into polysomes. UV cross-linking studies with the 27-nucleotide recognition sequence revealed bands corresponding to bound proteins with apparent molecular weights of 71,000 and 141,000. This appears to be the first example of steroid hormone-inducible proteins binding to an mRNA 3'-UTR. Its induction by estrogen and its sequence-specific binding to a region of vitellogenin mRNA important in estrogen-mediated stabilization suggest that the protein may play a role in the regulation of mRNA stability.

show abstract

“…In fish and especially in rainbow trout the field is hardly explored and except work by Dr VaiUant [21] few metabolic activities in hepatocyte culture have been clearly demonstrated. In oviparous animals, the synthesis of VTG by hepatocytes represent a good system with which to study the mechanism of action of steroid hormones [31][32][33][34]. Most of these studies have used hepatocytes of either amphibians (especially Xenopus laevis) or birds (especially chickens), though some have been based on hepatocytes from fish [24,[35][36][37].…”

Section: Resultsmentioning

confidence: 99%

Vitellogenin synthesis in cultured hepatocytes; an in vitro test for the estrogenic potency of chemicals

Pelissero

Flouriot

Foucher

et al. 1993

The Journal of Steroid Biochemistry and Molecular Biology

266

108

View full text Add to dashboard Cite

Smnmary--We describe here an/n vitro technique to assess the estrogenic activity of chemicals. This technique is based on rainbow trout hepatocytes incubated in a basic medium free of any additional growth factors or estrogenic chemicals and uses the production of vitellogenin (VTG) as a marker for the estrogenic potency of the compounds tested. The system allows at least some of the metabolic transformations which are undertaken by the liver cells/n vivo and could therefore be used for xenobiotic compounds which exhibit estrogenic activities after liver metabolic transformation. A dose-response curve was always consistently obtained using estradiol-17fl (E2), with a mid point at around 100 nME 2 and a maximum response at around 1000nM. Established estrogens such as 17al ethynylestradiol (EE2) or diethylstilboestrol (DES) were also tested. EE 2 appeared to be equipotent with E2 and DES slightly less potent. E2 conjugates were, perhaps surprisingly, also very potent. Estradiol-3-sulfate was equipotent with E2 and estradiol-17fl-glucuronide approx. 10% as potent. Other steroids such as androgens and progesterone, though active in the bioassay, were 3 orders of magnitude less potent than E 2. Of the various steroids tested, only cortisol, at concentrations up to 50 #M, was completely inactive. Six different phytoestrogens were tested in the assay. All were weakly estrogenic, possessing approximately one thousanth the potency of E 2 (they were as potent as the androgens and progesterone). All six phytoestrogens, as well as the androgens and progesterone, were tested in the presence of tamoxifen. In all cases tamoxifen reduced the production of VTG significantly, demonstrating that the estrogenic action of all of these compounds was most likely mediated by the E 2 receptor. The potencies determined here may not reflect the situation/n vivo but can provide complementary results about the activity of chemicals which need an hepatic metabolization to be estrogenic. Hepatocyte cultures would profitably be developed in other species to sustain these results.

show abstract

An estrogen-dependent polysomal protein binds to the 5′ untranslated region of the chicken vitellogenin mRNA

Cited by 28 publications

References 38 publications

Control of c-myc mRNA half-life in vitro by a protein capable of binding to a coding region stability determinant.

Control of c-myc mRNA half-life in vitro by a protein capable of binding to a coding region stability determinant.

An estrogen-inducible protein binds specifically to a sequence in the 3' untranslated region of estrogen-stabilized vitellogenin mRNA.

Vitellogenin synthesis in cultured hepatocytes; an in vitro test for the estrogenic potency of chemicals

Contact Info

Product

Resources

About