Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have previously isolated an estrogen-inducible secretory protein, lactotransferrin (LTF), and a cDNA to its messenger RNA from the uterus of mice. In this report we determined that the level of LTF mRNA is minimal in the seminal vesicles of normal mice. In contrast, expression of LTF mRNA in the seminal vesicles of developmentally estrogenized males was both constitutive and estrogen inducible. The results suggested that this alteration may be an example of atypical gene expression after hormonal manipulation early in development.
Mol Endocrinol 1988 Dec
PMID:Prenatal exposure of male mice to diethylstilbestrol alter the expression of the lactotransferrin gene in seminal vesicles. 321 64

The seminal vesicles of the rat synthesise large amounts of androgen-regulated secretory proteins. Indirect immunofluorescence cytochemistry and immunoblotting with monospecific polyclonal antibodies against three of the major secretory proteins (II, S and F) have been used to investigate the tissue distribution, subcellular localisation, androgen-regulation and developmental profile of secretory protein synthesis. There was no evidence for regional specialisation of the seminal vesicle epithelium; every epithelial cell synthesizes all three proteins via a classical secretory involving storage in secretory vesicles. Proteins S and II are contained within the same secretory vesicles. The time course of deinduction of proteins S and F after castration and their reinduction by testosterone closely followed that for their specific mRNAs described previously. During development, proteins S and F first appear between 10 and 15 days after birth. A protein immunologically related to seminal vesicle protein II is present in the lateral and dorsal lobes of the prostatic complex.
Mol Cell Endocrinol 1986 Nov
PMID:Tissue distribution, developmental profile and hormonal regulation of androgen-responsive secretory proteins of rat seminal vesicles studied by immunocytochemistry. 353 39

The androgen dependence of a highly abundant mRNA found in the rat dorsolateral prostate and seminal vesicles has been investigated using a complementary DNA clone from a rat dorsal prostate library. The 1.5 kilobase (kb) mRNA codes for a 52 000 Da translation product which is processed to 49 000 Da in the presence of microsomal membranes. This product appears to correspond to the previously described SVS II protein secreted by rat seminal vesicles and can be immunoprecipitated with anti-SVS II antiserum. Dot hybridization assays indicated that the mRNA is abundant in the dorsal and lateral prostate glands and in seminal vesicles but not in the ventral prostate, coagulating gland or other non-accessory sex tissues. Castration of mature male rats reduces the 1.5 kb mRNA 10-fold in the seminal vesicles and 7-fold in the dorsolateral prostate in 9 days. Androgen administration to one-week castrates returned the mRNA level to normal in both tissues within 48 h. The levels of the 1.5 kb mRNA are very similar in the dorsolateral prostate and seminal vesicles at maturity but distinct patterns of developmental regulation of this gene exist in the two tissues. Between 3 and 6 weeks of age, the level of the 1.5 kb mRNA increases approximately 3-fold in the dorsolateral prostate while the increase in the seminal vesicles is more than 600-fold.
Mol Cell Endocrinol 1986 Oct
PMID:Effect of androgens on mRNA for a secretory protein of rat dorsolateral prostate and seminal vesicles. 375 73

Rapid coagulation of seminal fluid in rats, guinea pigs, and several other mammalian species including certain non-human primates is responsible for the post-coital formation of copulatory plugs in the vagina. The clotting of rodent seminal plasma results from coagulation of certain proteins derived from the seminal vesicles by enzymes secreted mainly by the coagulating (anterior prostate) gland. Several lines of evidence indicate that the clotting enzymes of coagulating gland secretions are transglutaminases, and that the extreme insolubility of the seminal clot in rodents is due to transglutaminase-catalyzed formation of epsilon(gamma-glutamyl)lysine cross-links between polypeptide chains. Various features of the apparently unique forms of transglutaminases produced by rat coagulating gland and the actions of these enzymes on vesicular secretory and other proteins are discussed. The aliphatic polyamines spermidine and spermine are incorporated covalently into the proteins of the clot as the corresponding N-mono-epsilon-(gamma-glutamyl)- and N,N-bis(gamma-glutamyl)-adducts during the enzymatic coagulation process. At the greater than millimolar concentrations at which cross-spermidine and spermine are present in normal rat seminal plasma, these polyamines attenuate the formation of hard clots in reconstituted rat semen coagulation systems, seemingly by competing with lysyl residues in vesicular secretion proteins as transglutaminase amine donor substrates, and thus preventing formation of epsilon-(gamma-glutamyl)lysine cross-bridges. It is proposed that in those species such as the rat and man in which seminal plasma contains large amounts of spermidine and(or) spermine of prostatic origin, the seminal polyamines may serve to stop blockage of the urethra by preventing too explosive a rate of seminal clot formation during the ejaculatory process.
Mol Cell Biochem 1984
PMID:Transglutaminases and the clotting of mammalian seminal fluids. 614 53

Cells isolated enzymically from seminal vesicles and epididymides of normal and castrated rats were shown by electron microscopy to be intact and representative of the tissue. The cells synthesize and secrete tissue-specific proteins. Short-term incorporation of [3H]uridine and [35S]methionine was measured to determine the effects of castration on RNA and protein synthesis. Epididymal cells and tissue incorporated uridine at similar rates which were unaltered by castration. Similarly castration failed to diminish uridine incorporation by seminal vesicle cells and tissue. Therefore, androgens may principally control RNA degradation. A similar situation pertained to methionine incorporation by epididymal cells and tissue so here too control may be via protein degradation. In contrast, castration greatly decreased methionine incorporation by seminal vesicle tissue but not by isolated cells. Isolated cells were more active than in tissue, particularly those from castrated rats, and may be released from stromal-epithelial interactions and controls.
Mol Cell Endocrinol 1981 Aug
PMID:Isolation of cells from rat seminal vesicles and epididymis and their use in studying androgen action. 616

Combined treatment of adult male rats with the LHRH agonist, [D-Ser(TBU)6, des-Gly-NH2(10)]LHRH ethylamide, and a non-steroid antiandrogen, RU 23908, led to a rapid and marked atrophy of the ventral prostate and seminal vesicles. Treatment with the LHRH agonist decreased androgen secretion and thus facilitated the action of the antiandrogen in androgen-dependent tissues. Such a combined treatment could be useful in the treatment of androgen-dependent pathologies in man, particularly in prostatic adenocarcinoma and possibly benign prostatic hyperplasia.
Mol Cell Endocrinol 1981 Jan
PMID:Additive inhibitory effects of treatment with an LHRH agonist and an antiandrogen on androgen-dependent tissues in the rat. 625 2

The effects of a GnRH antagonist analogue (N-acetyl-Ala1,D-p-Cl-Phe2,D-Trp3,6-GnRH, Ant.) and a GnRH antiserum (A/S) on the development of pituitary-testicular function were studied in immature (23/24-31/32-day-old) rats. In another experiment the Ant. treatment was combined with bromocriptine (BR)-induced hypoprolactinaemia. Ant. and A/S decreased serum and pituitary levels of LH and FSH, and BR those of Prl (P less than 0.01-0.05). Testicular testosterone (T) and progesterone (P) contents were significantly decreased only by Ant. (P less than 0.01). Ant. decreased the weights of the testes, ventral prostates and seminal vesicles, as well as testicular LH, FSH and Prl receptors (R) (P less than 0.01-0.05). BR decreased LH-R but had no effect on Prl-R. Both Ant. and A/S decreased available pituitary GnRH-R (P less than 0.01), but free testicular GnRH-R were reduced only by Ant. BR increased GnRH receptors in the pituitaries. It is concluded that Ant.-induced low gonadotropin levels in immature animals inhibit the developmental increase of testicular weight, gonadotropin and Prl-R, steroidogenesis and androgen action on accessory sex glands. Hypoprolactinaemia had an additive inhibitory effect to the antigonadal effects of Ant. The testis tissue of immature (23/24-day-old) animals already contains GnRH-R. In general, developing animals are clearly very sensitive to the antigonadal actions of Ant. and BR, whereas the effect of GnRH-A/S is less pronounced than in adults.
Mol Cell Endocrinol 1984 Feb
PMID:Pituitary-testicular function in immature rats after treatment with GnRH antagonist, GnRH antiserum and bromocriptine. 632 70

Nafazatrom, an antithrombotic and antimetastatic agent containing a pyrazolone functionality, is a reducing substrate for the peroxidase activity of prostaglandin H (PGH) synthase. Nafazatrom inhibits the hydroperoxide-dependent oxidation of phenylbutazone, stimulates the reduction of 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid, and is oxidized by microsomal or purified enzyme preparations from ram seminal vesicles. Consonant with the effects of other peroxidase-reducing substrates, nafazatrom stimulates the oxygenation of arachidonic acid to prostaglandin endoperoxides by the cyclooxygenase component of PGH synthase. In addition, nafazatrom causes an elevation in the levels of 6-keto-prostaglandin F1 alpha, the non-enzymatic hydrolysis product of prostacyclin (PGI2) biosynthesized from arachidonic acid by ram seminal vesicle microsomes. Elevation of PGI2 biosynthetic capacity by nafazatrom occurs under conditions in which prostaglandin endoperoxide biosynthesis is maximal, suggesting that nafazatrom has a stimulatory effect on the conversion of prostaglandin endoperoxides to PGI2. Nafazatrom has no effect on the ability of ram seminal vesicle microsomes to convert PGH2 to PGI2 but protects microsomal PGI2 synthase from inactivation by 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid. Nafazatrom stimulates PGI2 biosynthesis in ram seminal vesicle microsomes by acting as a substrate for the peroxidase-catalyzed reduction of hydroperoxy fatty acids that are irreversible inactivators of PGI2 synthase. Several other compounds, including dipyridamole and triiodothyronine, exert similar effects. This may contribute to the reported ability of nafazatrom and related compounds to elevate the levels of bioassayable PGI2 in vivo and to the antithrombotic and antimetastatic activities of nafazatrom.
Mol Pharmacol 1984 Sep
PMID:Mechanism of the stimulation of prostaglandin H synthase and prostacyclin synthase by the antithrombotic and antimetastatic agent, nafazatrom. 643 40

The seminal vesicles of male rat secrete tissue-specific proteins under androgenic control. The effects of testosterone on the rough endoplasmic reticulum (RER) and Golgi-system of this tissue have been quantified using specific antibodies. Castration was followed within 2 weeks by a 10-fold reduction in RER-specific membrane protein. This was reversed by testosterone commencing about 4 h after exposure to the hormone. Five individual major RER antigens were separately quantified; these changed coordinately in response to androgen. No hormone-induced changes were seen in Golgi-specific membrane protein. Hormonal effects on mRNAs for two major secretory proteins were also measured using hybridisation to specific cDNA probes. The cellular concentrations of the two mRNAs changed by at least 1000-fold during hormonal treatment. A detailed examination of the time-course of induction by testosterone failed to show any temporal distinction between effects on mRNA and RER.
Mol Cell Endocrinol 1984 Aug
PMID:Androgen regulation of specific mRNAs, endoplasmic reticulum and Golgi-system. 646 50

The fibromuscular stroma (FMS) separated from the seminal vesicles of adult guinea pigs incorporated [35S]methionine into a 12 500 X g soluble fraction in vitro. Incorporation decreased 60% in tissues from 7-day castrates with no further change up to 21 days post-castration. Administration of 5 alpha-dihydrotestosterone prevented this decrease. Castration did not appear to increase the degradation of newly synthesized protein, or to alter the distribution between soluble and particulate subcellular fractions. Using SDS-PAGE and fluorography to quantitate [35S]methionine incorporation into specific proteins, three protein classes were identified which responded differentially to castration: (1) bands at 110 000 and 24 000 Mr decreased by 95%; (2) bands at 58 000 and 97 000 Mr were unchanged; (3) multiple bands decreased in proportion to total incorporation. Administration of 5 alpha-dihydrotestosterone could not fully maintain, at control levels, the synthesis of the 110 000 and 24 000 Mr bands. These results demonstrate that the FMS of the guinea pig seminal vesicle can serve as a useful model system for studying hormonally regulated functions of male sex accessory stromal tissue.
Mol Cell Endocrinol 1984 Dec
PMID:Androgen regulation of protein synthesis in the seminal vesicle fibromuscular stroma. 651 May 50


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