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

Endocrinology ◽  
1987 ◽  
Vol 121 (5) ◽  
pp. 1678-1688 ◽  
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

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

1978 ◽  
Vol 174 (2) ◽  
pp. 543-551 ◽  
Author(s):  
Stephen J. Higgins ◽  
Joy M. Burchell
Keyword(s):  
Protein Synthesis ◽  
Seminal Vesicle ◽  
Steroid Hormones ◽  
Secretory Proteins ◽  
Total Acid ◽  
Free System ◽  
Messenger Ribonucleic Acid ◽  
Mrna Population ◽  
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.

scholarly journals INTRAMITOCHONDRIAL BAND-LIKE STRUCTURES IN THE EPITHELIAL CELLS OF THE RAT SEMINAL VESICLE

1970 ◽  
Vol 17 (1) ◽  
pp. 49-53
Author(s):  
MASAHIRO MURAKAMI ◽  
SHOJI GOHARA ◽  
MIZUHO NONAKA
Keyword(s):  
Epithelial Cells ◽  
Seminal Vesicle ◽  
Rat Seminal Vesicle

Neonatal seminal vesicle mesenchyme induces a new morphological and functional phenotype in the epithelia of adult ureter and ductus deferens

Development ◽  
1991 ◽  
Vol 111 (1) ◽  
pp. 145-158 ◽  
Author(s):  
G.R. Cunha ◽  
P. Young ◽  
S.J. Higgins ◽  
P.S. Cooke
Keyword(s):  
Epithelial Cells ◽  
Seminal Vesicle ◽  
Developmental Plasticity ◽  
Androgen Receptors ◽  
Seminal Vesicles ◽  
Neonatal Mouse ◽  
Secretory Proteins ◽  
Complete Spectrum ◽  
Ductus Deferens ◽  
Functional Phenotype

Mesenchyme from neonatal mouse and rat seminal vesicles (SVM) was grown in association with postnatal (adult) epithelial cells from the ureter (URE) and ductus deferens (DDE) in chimeric tissue recombinants composed of mouse mesenchyme and rat epithelium or vice versa. Functional cytodifferentiation was examined in these SVM + URE and SVM + DDE tissue recombinants with antibodies against major androgen-dependent seminal-vesicle-specific secretory proteins. Adult DDE and URE were induced to express seminal cytodifferentiation and produced the complete spectrum of major seminal vesicle secretory (SVS) proteins. The SVS proteins produced were specific for the species that provided the epithelium. In the case of SVM + URE recombinants, the URE, which normally lacks androgen receptors (AR), expressed AR. These results demonstrate that adult epithelial cells retain a developmental plasticity equivalent to their undifferentiated fetal counterparts and are capable of being reprogrammed to express a completely new morphological, biochemical and functional phenotype.

Isolation and culture of rat seminal vesicle epithelial cells

1983 ◽  
Vol 145 (2) ◽  
pp. 293-304 ◽  
Author(s):  
Abraham L. Kierszenbaum ◽  
Robert M. DePhilip ◽  
W.Austin Spruill ◽  
Ikumasa Takenaka
Keyword(s):  
Epithelial Cells ◽  
Seminal Vesicle ◽  
Rat Seminal Vesicle

Electron Microscopic Study of the Epithelium of the Seminal Vesicle of Aging Rats

1974 ◽  
Vol 32 ◽  
pp. 138-139
Author(s):  
V. F. Allison ◽  
G. C. Fink ◽  
G. W. Cearley
Keyword(s):  
Cell Growth ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Seminal Vesicle ◽  
Seminal Vesicles ◽  
Epithelial Layer ◽  
Epithelial Hyperplasia ◽  
Electron Microscopic ◽  
Aging Rats ◽  
Pseudostratified Epithelium

It is well known that epithelial hyperplasia (benign hypertrophy) is common in the aging prostate of dogs and man. In contrast, little evidence is available for abnormal epithelial cell growth in seminal vesicles of aging animals. Recently, enlarged seminal vesicles were reported in senescent mice, however, that enlargement resulted from increased storage of secretion in the lumen and occurred concomitant to epithelial hypoplasia in that species.The present study is concerned with electron microscopic observations of changes occurring in the pseudostratified epithelium of the seminal vescles of aging rats. Special attention is given to certain non-epithelial cells which have entered the epithelial layer.

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