Estrogen stabilizes vitellogenin mRNA against cytoplasmic degradation

Brock, Martin L.; Shapiro, David J.

doi:10.1016/0092-8674(83)90151-4

Cited by 429 publications

(189 citation statements)

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“…Hormonal regulation of mRNA stability has been documented in several systems. Estrogen, for instance, can stabilize vitellogenin mRNA in cultured Xenopus liver [39]. Prolactin has been shown to alter mRNA stability of casein in mammary cell cultures [40].…”

Section: Discussionmentioning

confidence: 99%

Steroid 5.ALPHA. Reductase mRNA Type I is Differentially Regulated by Androgens and Glucocorticoids in the Rat Liver

Awady¹,

El-Garf²,

El-Houssieny³

2004

Endocr J

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Abstract. Testosterone and 5a-dihydrotestosterone (DHT) are the principal male hormones (androgens) in mammals. The enzyme, steroid 5a reductase catalyzes the conversion of testosterone (T) to its biologically potent steroid (DHT) in androgen dependent tissues. Two 5a reductase isoenzymes have been identified in rat tissues. The type I isoenzyme has been shown to be predominately expressed in the rat liver, whereas androgen target tissues of the genital tract express mainly isoenzyme II. The effects of androgens and glucocorticoids on the abundance of steroid 5a reductase type I (5aR1) messenger RNA in the rat liver were examined. Steady state levels of 5aR1 mRNA decreased dramatically to 1.5% of control levels 14 days following adrenalectomy (ADX), whereas dexamethasone (Dex) administered (0.5 mg/ 100 g) to ADX animals enhanced the expression of 5aR1 to twice its' normal values within 40 hours. Bilateral orchiectomy induced, within eight days, the expression of 5aR1 mRNA in the rat liver to 1.75 fold the normal value while testosterone injection failed to reduce this enhanced expression in castrated animals. Addition of Dex (1 mM) to primary cultures of rat hepatocyte resulted in a five-and three-fold reduction in the mRNA expression of 5aR1 after 24 and 48 hours, respectively. DHT (0.5 mM) however, induced the expression of 5aR1 mRNA by two-and seven-fold 24 and 48 hours post-treatment, respectively. In vitro nuclear run-on analysis of the 5aR1 gene showed no correlation between the rate of synthesis and steady state levels of this mRNA either in the intact liver or in cultured hepatocytes. These results appear to suggest that glucocorticoids and androgens differentially regulate 5aR1 mRNA in the rat liver. Moreover, our findings appear to indicate that regulation of 5aR1 gene is primarily at the post-transcriptional level. TESTOSTERONE and dihydrotestosterone (DHT) are the major circulating androgens in humans and other vertebrates. Although each hormone displays potent effects in biological assays of androgen action, under specific conditions, each hormone displays properties that suggest roles in the modulation of specific functions. It is clear that DHT is crucial for the normal development of the male genitalia and of the prostate [1,2]. In contrast, testosterone appears to play essential roles in promoting spermatogenesis and Wollfian duct development, as well as gonadotropin regulation. The steroid 5a reductase enzyme plays an important physiological role in the conversion of testosterone to its bioactive and reduced derivatives; 5a dihydrotestosterone (DHT) in androgen dependent tissues [3]. To date, two steroid 5a reductase isoenzymes have been cloned and characterized in humans and rats. These isoenzymes are encoded by independent genes designated types I and II. In peripheral tissues such as the liver, type (I) 5a-reductase (5aR1) and reductive 3a-hydroxysteroid dehydrogenase (3a-HSD) isomers work consecutively to eliminate androgens and protect against hormone excess [4]. It has been postulated tha...

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Section: Discussionmentioning

confidence: 99%

Steroid 5.ALPHA. Reductase mRNA Type I is Differentially Regulated by Androgens and Glucocorticoids in the Rat Liver

Awady¹,

El-Garf²,

El-Houssieny³

2004

Endocr J

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“…One of the most poorly understood posttranscriptional controls is that which defines the stability of specific mRNA sequences. The importance of turnover rate in controlling mRNA abundance, and thus gene expression, is best illustrated by the observation that many of the mRNAs that encode the most highly abundant cell type-specific polypeptides are preferentially stabilized over other mRNAs present within the same cytoplasm (6,21,25,29,44).The stability of specific eucaryotic mRNAs has most often been determined by assaying for the presence of particular mRNAs after treating cells with the transcriptional inhibitor actinomycin D (4,13,25,34,43,46). However, this kind of analysis is subject to several possible artifacts.…”

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Differential stability of Drosophila embryonic mRNAs during subsequent larval development.

Winkles¹,

Grainger²

1985

The Journal of Cell Biology

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The relative stabilities of specific embryonic mRNAs that persist in Drosophila melanogaster larvae were determined using an approach that combined RNA density labeling with cell-free translation. Unlike the other methods commonly used to measure the decay of individual mRNAs, the density labeling approach does not depend on the use of transcriptional inhibitors or on the measurement of precursor pool specific activities. Using this approach, we have determined that different embryonic mRNA species persist for varying periods during subsequent development, with half-lives ranging from ~2 to ~30 h. The embryonic histone mRNAs are relatively unstable; they are no longer detectable by 9 h of larval development. By 41 h of larval development, 90% of the nonhistone mRNAs assayed have decayed considerably; computerized scanning densitometry of translation products indicates that these transcripts are not decaying as members of discrete half-life classes. The persisting mRNAs that remain are very long-lived; their in vitro translation products can still be detected after 91 h of larval development. We have tentatively identified the mRNAs that encode actin, tropomyosin, and tubulin as members of this stable mRNA population. Although embryonic mRNAs do fall into these three broad classes of stability, they appear to decay with a continuum of half-lives. Because the range of half-lives is so great, mRNA stability is probably an important factor controlling mRNA abundance during Drosophila development.The cytoplasmic abundance of a particular mRNA can be controlled at both the transcriptional and posttranscriptional levels. One of the most poorly understood posttranscriptional controls is that which defines the stability of specific mRNA sequences. The importance of turnover rate in controlling mRNA abundance, and thus gene expression, is best illustrated by the observation that many of the mRNAs that encode the most highly abundant cell type-specific polypeptides are preferentially stabilized over other mRNAs present within the same cytoplasm (6,21,25,29,44).The stability of specific eucaryotic mRNAs has most often been determined by assaying for the presence of particular mRNAs after treating cells with the transcriptional inhibitor actinomycin D (4,13,25,34,43,46). However, this kind of analysis is subject to several possible artifacts. In addition to a secondary effect on cellular protein synthesis (12,15,39,40) it has also been shown that actinomycin D treatment can both decrease the stability of total mRNA populations (41) and increase the half-life of specific mRNAs (9, 42). Also, if 1808 the actinomycin D "chase" does not begin immediately or is not completely effective, then the measured half-life of a mRNA species will appear longer than it actually is.The best experimental system to use for studying the differential stability of individual mRNAs would be one in which no transcriptional inhibition is necessary. For example, by measurement of the rate of radiolabel accumulation into specific mRNAs by usi...

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“…Estrogen stabilizes the mRNA encoding the egg yolk precursor protein, vitellogenin (11), and destabilizes albumin mRNA (12). Current evidence indicates that the first committed step in albumin mRNA decay is the activation of an endoribonuclease termed PMR-1 (polysomal ribonuclease 1) (13).…”

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confidence: 99%

Vigilin binding selectively inhibits cleavage of the vitellogenin mRNA 3′-untranslated region by the mRNA endonuclease polysomal ribonuclease 1

Cunningham

Dodson

Nagel

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

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In Xenopus, estrogen induces the stabilization of vitellogenin mRNA and the destabilization of albumin mRNA. These processes correlate with increased polysomal activity of a sequence-selective mRNA endonuclease, PMR-1, and a hnRNP K homology-domain RNA-binding protein, vigilin. Vigilin binds to a region of the vitellogenin mRNA 3 -untranslated region (3 -UTR) implicated in estrogen-mediated stabilization. The vigilin-binding site in the vitellogenin B1 mRNA 3 -UTR contains two consensus PMR-1 cleavage sites. The availability of purified PMR-1 and recombinant vigilin made it possible to test the hypothesis that RNA-binding proteins interact with cis-acting elements to stabilize target mRNAs by blocking cleavage by site-specific mRNA endonucleases. Vigilin binds to the vitellogenin mRNA 3 -UTR site with at least 30-fold higher affinity than it exhibits for the albumin mRNA segment containing the mapped PMR-1 cleavage sites. This differential binding affinity correlates with differential in vitro susceptibility of the protein-RNA complexes to cleavage by PMR-1. Whereas recombinant vigilin has no detectable protective effect on PMR-1 cleavage of albumin mRNA, it retards in vitro cleavage of the vitellogenin mRNA 3 -UTR by purified PMR-1. The PMR-1 sites in the vitellogenin mRNA 3 -UTR are functional because they are readily cleaved in vitro by purified PMR-1. These results provide direct evidence for differential susceptibility to endonuclease-mediated mRNA decay resulting from the differential affinity of a RNAbinding protein for cis-acting stability determinants.

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Estrogen stabilizes vitellogenin mRNA against cytoplasmic degradation

Cited by 429 publications

References 32 publications

Steroid 5.ALPHA. Reductase mRNA Type I is Differentially Regulated by Androgens and Glucocorticoids in the Rat Liver

Steroid 5.ALPHA. Reductase mRNA Type I is Differentially Regulated by Androgens and Glucocorticoids in the Rat Liver

Differential stability of Drosophila embryonic mRNAs during subsequent larval development.

Vigilin binding selectively inhibits cleavage of the vitellogenin mRNA 3′-untranslated region by the mRNA endonuclease polysomal ribonuclease 1

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