Effects of testosterone on messenger ribonucleic acid and protein synthesis in rat seminal vesicle

In a previous report [Higgins et al. (1976) Biochem. J.158, 271–282] we described the effects of alterations in androgen status on the synthesis of two basic secretory proteins of the rat seminal vesicle. In the present paper we examine the effects of testosterone on the activity of mRNA in the seminal vesicle. Total cellular poly(A)-rich RNA was isolated and translated in a cell-free system prepared from wheat germ. Translation products were separated on denaturing polyacrylamide gels and the protein bands corresponding to the two basic secretory proteins were identified immunologically. Incorporation of radioactive methionine into these bands was taken as a measure of the individual mRNA activities. Total mRNA activity was estimated by radioactivity in total acid-precipitable material. The results show that 1 to 2 weeks after castration the activities of mRNA molecules for the basic secretory proteins were decreased 10–20-fold on a tissue basis. Testosterone given in vivo rapidly and substantially restores mRNA activity to normal. Since these changes correlate closely with variations in the rates of synthesis of the secretory proteins in whole cells it suggests that androgenic steroids control protein synthesis chiefly via mRNA availability. In this respect their action resembles those of other steroid hormones acting in other systems. However, these effects of testosterone on the mRNA molecules for the major secretory proteins could not be distinguished from those on total mRNA. Thus the proportion of the total mRNA population accounted for by the two specific mRNA molecules showed less than a 2-fold variation with androgen status. Similarly the two secretory proteins always accounted for 25–33% of general protein synthesis. This is in sharp contrast with the markedly differential effects of other steroid hormones controlling synthesis of major proteins in other well-studied systems. We interpret our results as indicating that testosterone regulates the mRNA population of the seminal vesicle as a whole.

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Developmental biochemistry of cottonseed embryogenesis and germination: changing messenger ribonucleic acid populations as shown by in vitro and in vivo protein synthesis

Biochemistry ◽

10.1021/bi00517a033 ◽

1981 ◽

Vol 20 (14) ◽

pp. 4162-4168 ◽

Cited By ~ 290

Author(s):

Leon Dure ◽

Sally C. Greenway ◽

Glenn A. Galau

Keyword(s):

Protein Synthesis ◽

Ribonucleic Acid ◽

Messenger Ribonucleic Acid ◽

In Vivo Protein Synthesis

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In vivo inhibition of cell-mediated and humoral immune responses to cellular antigens by SV-IV, a major protein secreted from the rat seminal vesicle epithelium

Journal of Reproductive Immunology ◽

10.1016/0165-0378(94)00900-r ◽

1995 ◽

Vol 28 (1) ◽

pp. 15-30 ◽

Cited By ~ 14

Author(s):

Caterina Romano-Carratelli ◽

Marilena Galdiero ◽

Immacolata Nuzzo ◽

Concetta Bentivoglio ◽

Raffaele Porta ◽

...

Keyword(s):

Immune Responses ◽

Seminal Vesicle ◽

Major Protein ◽

Humoral Immune ◽

Humoral Immune Responses ◽

Rat Seminal Vesicle

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Studies on the form and synthesis of messenger ribonucleic acid in the rat ventral prostate gland, including its tissue-specific stimulation by androgens

Biochemical Journal ◽

10.1042/bj1370513 ◽

1974 ◽

Vol 137 (3) ◽

pp. 513-524 ◽

Cited By ~ 27

Author(s):

W. Ian P. Mainwaring ◽

Peter A. Wilce ◽

Allan E. Smith

Keyword(s):

Prostate Gland ◽

Sodium Dodecyl ◽

Ventral Prostate ◽

Experimental Conditions ◽

Free System ◽

Cell Free System ◽

Messenger Ribonucleic Acid ◽

Selective Incorporation

1. When prostate polyribosomes are labelled with radioactive precursors in vivo and subsequently dissociated with sodium dodecyl sulphate, a heterogeneous 6–15S RNA species may be identified that possesses all of the distinctive properties of mRNA. 2. Apart from the selective incorporation of 5′-fluoro-orotic acid into this 6–15S RNA component, it is bound by nitrocellulose filters under experimental conditions where only poly(A)-rich species of RNA are specifically retained. Most importantly, however, only the 6–15S RNA fraction is capable of promoting the incorporation of amino acids into peptide linkage in an mRNA-depleted cell-free system derived from ascites-tumour cells. 3. With the development of a simpler method for labelling the total RNA fraction of the prostate gland in vitro, the poly(A)-enriched RNA fraction may be readily isolated by adsorption and elution from oligo(dT)-cellulose. The synthesis of the poly(A)-enriched 6–15S RNA fraction is stringently controlled by androgens in a highly tissue- and steroid-specific manner. 4. From an analysis of the proteins synthesized in the ascites cell-free system in the presence of the poly(A)-rich RNA fraction, it appears that protein synthesis in the prostate gland is stimulated in a rather general way, even during the earliest phases of the androgenic response. This conclusion may require modification when more specific means of analysis are available than those used in the present investigation. 5. The implications of these findings to the mechanism of action of androgens are discussed.

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Growth of Rat Seminal Vesicle Epithelial Cells in Culture: Neurotransmitters Are Required for Androgen-Regulated Synthesis of Tissue-Specific Secretory Proteins*

Endocrinology ◽

10.1210/endo-121-5-1678 ◽

1987 ◽

Vol 121 (5) ◽

pp. 1678-1688 ◽

Cited By ~ 26

Author(s):

E. MARGARET KINGHORN ◽

ANITA S. BATE ◽

STEPHEN J. HIGGINS

Keyword(s):

Epithelial Cells ◽

Seminal Vesicle ◽

Secretory Proteins ◽

Tissue Specific ◽

Cells In Culture ◽

Rat Seminal Vesicle

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Txe, an endoribonuclease of the enterococcal Axe–Txe toxin–antitoxin system, cleaves mRNA and inhibits protein synthesis

Microbiology ◽

10.1099/mic.0.045492-0 ◽

2011 ◽

Vol 157 (2) ◽

pp. 387-397 ◽

Cited By ~ 32

Author(s):

Elizabeth M. Halvorsen ◽

Julia J. Williams ◽

Azra J. Bhimani ◽

Emily A. Billings ◽

Paul J. Hergenrother

Keyword(s):

Protein Synthesis ◽

Multidrug Resistant ◽

Start Codon ◽

Pcr Analysis ◽

Free System ◽

Toxic Activity ◽

E Coli ◽

A Cell ◽

Vancomycin Resistant

The axe–txe operon encodes a toxin–antitoxin (TA) pair, Axe–Txe, that was initially identified on the multidrug-resistance plasmid pRUM in Enterococcus faecium. In Escherichia coli, expression of the Txe toxin is known to inhibit cell growth, and co-expression of the antitoxin, Axe, counteracts the toxic effect of Txe. Here, we report the nucleotide sequence of pS177, a 39 kb multidrug-resistant plasmid isolated from vancomycin-resistant Ent. faecium, which harbours the axe–txe operon and the vanA gene cluster. RT-PCR analysis revealed that the axe–txe transcript is produced by strain S177 as well as by other vancomycin-resistant enteroccoci. Moreover, we determine the mechanism by which the Txe protein exerts its toxic activity. Txe inhibits protein synthesis in E. coli without affecting DNA or RNA synthesis, and inhibits protein synthesis in a cell-free system. Using in vivo primer extension analysis, we demonstrate that Txe preferentially cleaves single-stranded mRNA at the first base after an AUG start codon. We conclude that Txe is an endoribonuclease which cleaves mRNA and inhibits protein synthesis.

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Changes in protein synthesis during the development of Xenopus laevis

Development ◽

10.1242/dev.51.1.137 ◽

1979 ◽

Vol 51 (1) ◽

pp. 137-153

Author(s):

J. E. M. Ballantine ◽

H. R. Woodland ◽

E. A. Sturgess

Keyword(s):

Protein Synthesis ◽

Translational Control ◽

Gene Activity ◽

Specific Gene ◽

Two Dimensional Gel Electrophoresis ◽

Free System ◽

Stage Of Development ◽

New Gene ◽

Made In

Patterns of protein synthesis during the development of Xenopus were studied by two-dimensional gel electrophoresis. Up to the end of the blastula stage we find no newly synthesized proteins which are not already made in the oocyte. The first new proteins are seen during gastrulation, and they increase in number during neurulation. Some of these are restricted to the ‘ectodermal’ region, and some to the ‘endodermal’ region of embryos divided into two parts. These new, region-specific proteins include α-actin. When the oocyte matures the number of detectable newly synthesized proteins decreases, reaching a minimum in the unfertilized egg. Some, such as β- and γ-actin, re-appear at the end of cleavage. This could not be shown to be a recovery artifact. The relation of the total mRNA to these changes in protein synthesis was studied by translation in the lysed reticulocyte cell-free system. The mRNAs that code for oocyte proteins that cease synthesis in the unfertilized egg and re-appear in blastulae are nevertheless detectable in total RNA made from eggs. These proteins therefore seem to cease and resume synthesis through translational control. mRNAs for new proteins first appear after gastrulation, just when these proteins are first detected in vivo. This strongly suggests, though it does not prove, that new gene activity is involved. It is therefore likely that region-specific gene activity is already present by the gastrula stage of development, and has an impact on the most abundant kinds of proteins made in the embryo.

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