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At least 991 records · Page 55Linked to original sources
PubMed1990

Time course of quantitative morphological changes of the autophagic-lysosomal compartment of murine seminal vesicle epithelial cells under the influence of vinblastine.

Changes of the autophagic-lysosomal compartment (ALC) of the murine seminal vesicle epithelial cells were monitored by electron microscopic morphometry during 36 h following a single 10 mg/kg bw dose of vinblastine sulfate (VBL), a widely used tool to cause an accumulation of the autophagic vacuoles (AVs). Three morphologically distinct subcompartments of the ALC, i.e. early autophagic vacuoles (AV1) being presumably prelysosomal autophagosomes, advanced AVs (AV2) containing material under degradation and dense bodies (DB) were defined. The ALC and its subcompartments expanded after VBL in a two-phase reaction. The first subcompartments to react significantly were AV1 and AV2 (at 30 min) followed by DBs with a 30 min delay. The ALC then ceased to grow until the 90th min when a second expansion phase started peaking around 8 h with a cytoplasmic volume fraction 15 times larger than in the untreated control. This second growth was entirely brought about by the expansion of the two AV subcompartments. After 8 h the volume fraction of both AV1 and AV2 decreased to cause a gradual regression of the ALC. AV1, however, already ceased to expand as early as after 6 h, i.e. during the last 2 h of the expansion phase of the ALC. Comparison of this time curve with the one we previously measured in mouse liver shows considerable differences between the two cell types. The growth curves of the AV subcompartments in our experiment along with others' kinetic data obtained in steady state cells not treated with VBL show that segregation (= formation of AV1) is possibly stimulated by VBL in our system.

Animals↗
PubMed1994

Inhibitory effects of transforming growth factor-beta 1 on androgen-induced development of neonatal mouse seminal vesicles in vitro.

The effects of transforming growth factor-beta 1 (TGF beta 1) on the development of seminal vesicles (SVs) of neonatal mice were investigated in vitro. SVs from 0-day-old male mice were cultured for 2-8 days in serum-free, chemically defined medium with or without 5 alpha-dihydrotestosterone (DHT) at 10(-8) M in the presence or absence of TGF beta 1. Before culture, SVs from 0-day-old mice had no epithelial branches. SVs cultured in medium with DHT formed numerous epithelial branches after day 2 of culture, whereas epithelial branching did not occur in SVs cultured without DHT. The addition of TGF beta 1 (10 ng/ml) to DHT-containing medium almost completely inhibited the formation of epithelial branches. However, the removal of TGF beta 1 from DHT-containing medium on day 2 or 4 of culture initiated the formation of epithelial branches. TGF beta 1 (10 ng/ml) decreased [3H]thymidine labeling indices of both epithelium and mesenchyme of SVs cultured in medium with DHT during 8 days of culture, an effect that was reversed after the removal of TGF beta 1 from the medium on day 2 or 4 of culture. In contrast, TGF beta 1 (10 ng/ml) did not affect the labeling indices of either epithelium or mesenchyme of SVs cultured in medium without DHT. TGF beta 1 (10 ng/ml) also suppressed the normal increase in protein and DNA contents of SVs cultured in medium with DHT, whereas it did not reduce protein or DNA contents of SVs cultured in medium without DHT. The present study indicates that androgen-dependent growth of the SV can be reversibly inhibited by TGF beta 1, whereas androgen-independent growth of the SV is insensitive to TGF beta 1.

Androgens↗
PubMed1981

Evidence for the presence of specific prolactin binding protein in rat seminal vesicle fluid.

The presence of a specific prolactin binding in rat seminal vesicle fluid has been demonstrated. The binding phenomenon was saturable and pH dependent, the optimum pH being 7.2. The prolactin binding protein (PBP, 1800 x g supernatant) was characterized by a single order affinity binding sites with an association constant (Ka) 1.52 x 10(7) mol-1. The specificity of the prolactin binding was demonstrated by the fact that other proteohormones such as rFSH, rLH, rTSH and hTSH failed to inhibit the binding of labelled hormone to PBP, while unlabelled oPRL gave a dose-response inhibition curve. Among the rats in the age group 45 to 180 days, PBP obtained from animals of 90 day old showed a maximum binding of radioiodinated rPRL. Following castration for five days the percent binding of 125I-rPRL to PBP decreased markedly. The treatment of castrated rats with testosterone propionate for five days returned the 125I-rPRL binding to near intact values. Following a centrifugation of 1800 x g supernatant at 360 000 x g for 3 h, prolactin binding activity still remained in the supernatant thus implicating that the binding protein is in a soluble state.

Age Factors↗
PubMed1989

Effects of autonomic drugs on intraluminal pressure and excretion of rat seminal vesicles in vivo.

The effects of intravenously administered autonomic drugs on the intraluminal pressure and the excretion volume of the seminal vesicles in rats were studied. Both alpha 1-adrenergic and cholinergic stimulants produced a rapid increase in pressure and fluid excretion. alpha 1-Adrenergic stimulants elicited a sharp and single increase in pressure, while cholinergic stimulants caused a sharp increase with multiple peaks.

Adrenergic alpha-Agonists↗
PubMed1988

Scanning-electron-microscopical study of the seminal vesicle, coagulating gland, ampullary gland and ventral prostate in the golden hamster.

A study of the internal surfaces of the seminal vesicle, coagulating gland, ampullary gland and ventral prostate of the golden hamster was carried out by scanning electron microscopy. The internal surface of each of these glands was found to display characteristic features in topography and in arrangements of the microvilli. The features are useful in the identification of these glandular tissues in situ.

Animals↗
PubMed1980

Immunohistochemical demonstration of VIP, [Met5]-and [Leu5]-enkephalin immunoreactive nerve fibres in the human prostate and seminal vesicles.

The distribution of nerves containing immunoreactivity for the VIP and enkephalins has been demonstrated in the human prostate and seminal vesicles using the immunoperoxidase bridge. VIP-containing nerves were detected in both organs studied mainly in association with the epithelium, while nerves containing ELI seemed to be related to smooth muscle. Compared with the distribution of adrenergic and cholinergic nerves in the prostate marked differences in the density of the innervation were detected. The possible nature of these peptide-containing nerves is discussed.

Acetylcholinesterase↗
PubMed1991

17R(18S)epoxyeicosatetraenoic acid, a cytochrome P-450 metabolite of 20:5n-3 in monkey seminal vesicles, is metabolized to novel prostaglandins.

Eicosapentaenoic acid (20:5n-3) is metabolized by cytochrome P-450w3 of monkey seminal vesicles to 17R(18S)epoxy-5,8,11,14-eicosatetraenoic acid (17R(18S)EpETE). PGH synthase is abundant in this tissue. Racemic 17(18)EpETE was therefore investigated as a substrate of PGH synthase. The main products were identified as two diastereoisomers of 17(18)epoxyprostaglandin E2, which were formed in a 4:5 ratio. The structures were confirmed by authentic material. The natural epoxide enantiomer can thus be metabolized to novel 17R(18S)epoxyprostaglandins.

Animals↗
PubMed1986

Endocytosis in guinea pig seminal vesicle epithelial cells cultivated in chemically defined medium.

We have developed a chemically defined monolayer culture system for guinea pig seminal vesicle epithelial cells (SVEP). The cells appeared as a polarized monolayer with apical microvilli, tight junctions and desmosome-like junctions, and often dilated intercellular spaces. SVEP expressed epithelial-specific cytokeratins as detected immunocytochemically. Growth was obtained during the first week of culture. In this period, the cells were exposed to unconjugated horseradish peroxidase (HRP), a ricin-peroxidase conjugate (Ri-HRP), or cationized ferritin (CF). HRP was endocytosed without binding to the SVEP surface (fluid-phase endocytosis) and was found mainly in multivesicular endosomes and lysosomes. Ri-HRP and CF, however, were endocytosed following binding to the cell surface. Initially these markers were present in multivesicular endosomes, but later also in smaller tubular and vesicular endosomes, some Golgi-associated elements (but not Golgi stacks), and lysosomes. We conclude that our SVEP culture system may be useful in further studies, on e.g. hormonal regulation of endocytosis and other processes of importance for SVEP maintenance and modulation of the seminal fluid in vivo.

Animals↗
PubMed1991

Biological functions of the water-insoluble fraction of mouse seminal vesicle fluid. I. Suppression of the blastogenic response of lymphocytes.

The effects of the water-insoluble fraction of mouse seminal vesicle fluid (WIF-SVF) on lymphocytes was investigated to clarify its role in reproductive immunity. WIF-SVF inhibited the blastogenic response of T-cells to concanavalin-A (Con-A), but it did not inhibit the blastogenic response of B-cells to lipopolysaccharide (LPS). Pretreatment of splenocytes with WIF-SVF did not suppress the blastogenic response of splenocytes to Con-A when treated cells were washed prior to culture. WIF-SVF did not inhibit the proliferation of Con-A activated splenocytes, the response of listeria-immune splenocytes to listerial antigen, or the proliferation of IL 2-dependent HT-2 cells, or the growth of tumour cells (Yac 1 cells, Ehrlich ascites carcinoma cells, EL-4 cells). A listerial antigen-specific immune response was not induced after mice were immunized with both listerial antigen and WIF-SVF. WIF-SVF is mainly composed of protein and its suppressive activity was enhanced by heating at 100 degrees C. These results suggest that WIF-SVF inhibits the responsiveness of T-cells to antigens or mitogens non-specifically at the initial stage.

Animals↗
PubMed1981

Blockade of 5-hydroxytryptamine-induced responses of rat seminal vesicle by lithium-possible mediation through calcium exchange..

Effect of lithium on the contractile responses of rat isolated seminal vesicle to 5-hydroxytryptamine (5-HT) were investigated by varying the Ca++ and Mg++ concentrations of the incubation medium in the absence and presence of EDTA. Preparations incubated in excess Ca++ (4.2 mM) or in Ca++-free Krebs solution showed decrease in sensitivity to 5-HT, whereas the responses to 5-HT were potentiated in Mg++-free incubation media and reduced in media containing excess Mg++. Rezerpinization failed to induce supersensitivity to 5-HT in any Mg++ concentration in the medium. However, reserpinized tissue in Mg++-free solution with EDTA showed increased sensitivity to 5-HT. Li+ inhibited responses to 5-HT. The inhibitory action of Li+ was augmented in medium lacking in Ca++ and was antagonized in media containing excess Ca++ (4.2mM). Li+ reduced the sensitivity and decreased maximum responses to 5-HT in any Mg++ concentration in the medium. In the presence of EDTA, the inhibition observed with Li+ in excess Mg++ (3.6 mM) medium was comparatively much less in both non-reserpinized and reserpinized preparations. Thus Li+ may be inhibiting responses to 5-Ht by block of influx of Ca++ or delayed efflux of Ca++ or inhibition of uptake of Ca++ or a combination of two or more of these effects.

Animals↗
PubMed2003

Expression study of three secretory proteins (prostatic secretory protein of 94 amino acids, probasin, and seminal vesicle secretion II) in dysplastic and neoplastic rat prostates.

BACKGROUND: Prostatic secretory protein of 94 amino acids (PSP94), probasin, and seminal vesicle secretion II (SVSII) are the three major proteins secreted by the lateral lobe of the rat prostate gland. Among these proteins, rodent PSP94 but not probasin and SVSII has a human homologue and it is also a major secretory protein of the human prostate, in addition to prostatic acid phosphatase and prostate-specific antigen. METHODS: In this study, we examined and compared the mRNA expression of these three secretory markers in three rat models of prostate cancer including the sex steroid-induced dysplasia (prostatic intraepithelial neoplasia or PIN) in Noble (Nb) rat model, an androgen-independent Nb rat prostatic tumor (AIT) and Dunning rat prostatic adenocarcinomas (both androgen-dependent and -independent) by in situ hybridization (ISH), reverse transcriptase-polymerase chain reaction (RT-PCR), and immunohistochemistry. RESULTS: The transcripts for the three markers were highly expressed in the secretory epithelium of normal lateral prostate (LP). Their hybridization signals became reduced in the epithelial cells in the low-grade PINs and significantly weakened or lost in the high-grade PINs induced in the LP. Interestingly, we observed that some dysplastic cells located at the basal compartment of the PIN lesions, and nests of outpouching epithelial cells in the vicinity of PINs, expressed positive hybridization signals of three markers. In the adenocarcinoma, signals of probasin but not PSP94 and SVSII were detected. No hybridization signals were detected in both Dunning and AIT tumors. By RT-PCR, transcripts for these proteins were still detected but significantly reduced in the Dunning tumors, whereas in the AIT tumor, only SVSII transcripts were detected. Immunohistochemistry of PSP94 also showed a reduced staining in the PIN lesions, but no immunoreactivity was seen in the rat prostatic tumors. CONCLUSIONS: The mRNA expression of the three prostatic secretory markers were decreased in the hormone-induced PINs and in two rat prostatic tumors, indicating that the androgen-regulated secretory differentiation was impaired during the development of the premalignant lesion and further reduced in advanced tumors. The abnormal expression pattern of these secretory markers and androgen receptor (AR) in the basal compartment of the PIN lesions suggests that there is a population of cell types with secretory phenotype appearing in the basal cell layer during the early malignant transformation of the prostatic epithelium.

Adenocarcinoma↗