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PubMed2006

Magnetic resonance imaging of seminal vesicle cyst associated with ipsilateral urinary anomalies.

BACKGROUND: Seminal vesicle cysts rarely cause symptoms. Data on long-term follow-up from childhood to adulthood are lacking. The study analyzed the magnetic resonance imaging (MRI) and follow-up results of this condition. METHODS: From 1991 to 1996, seminal vesicle cyst was diagnosed in 13 boys (mean age, 12 years; range, 7-15 years), six of whom had long-term follow-up data. The clinical symptoms and MRI findings at diagnosis and at follow-up were analyzed. RESULTS: The seminal vesicle cyst was on the right side in six patients and on the left in seven. The size varied, ranging from 1.0 x 1.3 x 1.4 to 4.4 x 3.1 x 3.6 cm. All showed high signal intensity on T2-weighted images but variable signal intensity on T1-weighted images. Associated urinary tract anomalies included renal anomalies (dysplasia in 2 patients, agenesis in 11), ectopic ureteral orifice (11), hydroureter (6), and vertebral anomalies (2). One of the six patients with follow-up had repeated urinary tract infection and underwent surgical resection of the cyst 8 years after the diagnosis. The other five had no symptoms during the follow-up period. Three of the six patients had repeat MRI after a median of 11 years, which showed slight cyst enlargement and increased T1-weighted signal intensity. CONCLUSION: Most seminal vesicle cysts were asymptomatic and did not change during long-term follow-up. MRI is a powerful tool for detecting seminal vesicle cysts and in delineating associated congenital anomalies of the urogenital tract.

Adolescent↗
PubMed1989

[Prolactin and specific binding of testosterone in cultured cells of the seminal vesicle of Gobius niger L].

Cultured seminal vesicle cells of Gobius niger L., precultured for about 15 days, are tested for their Testosterone-binding capacity. This whole cell system shows a specific binding of the androgen, reaching saturation in the presence of increasing amounts of ligand and the Scatchard Plot indicates a good affinity (KD = 4.4 x 10(-9) M), involving a number of sites of 5.06 x 10(-15) mole/culture. The possible existence of a second binding-site population with lower affinity and greater number of sites remains to be demonstrated. At 18 degrees C, the time course shows a maximal binding after about 60 min. of incubation, followed by a rapid decline at 90 min. The competition experiments involving estradiol, 11-keto- and 11-hydroxytestosterone indicate an effective if not total specificity to these steroids. The cross-reaction percentages at the 50% binding level are respectively 10.9, 8.5, 4.02%. Ovine Prolactin treatment of the cultures for 6 days before the binding experiment significantly improves the specific binding level of testosterone if compared to the controls (p .019, p .005). This result indicates that the Prolactin-Testosterone synergistic data already obtained on the seminal vesicles of Siluridae and Gobiidae is explained by a direct effect of the Prolactin on the androgen receptor level in the seminal vesicle cell.

Analysis of Variance↗
PubMed1996

Prediction of capsular perforation and seminal vesicle invasion in prostate cancer.

PURPOSE: Capsular perforation and seminal vesicle invasion are unfavorable prognostic factors in prostate cancer. Accurate preoperative prediction of these factors would be clinically useful for planning treatment, especially in patients being considered for radiation therapy, nerve sparing radical prostatectomy and watchful waiting. However, current methods are imprecise at predicting the presence and extent of these factors. We determined which combination of commonly available preoperative variables provides the best prediction of capsular perforation and seminal vesicle invasion of patients with clinically localized prostate cancer. MATERIALS AND METHODS: We reviewed the preoperative medical records and biopsy findings from 314 patients with clinical stages T1cN0M0 to T2cN0M0 cancer who underwent radical retropubic prostatectomy and bilateral pelvic lymphadenectomy between September 1991 and June 1993. Radical prostatectomy specimens were embedded and evaluated by whole mount sections. RESULTS: Capsular perforation was observed in 104 patients (33.1%) and seminal vesicle invasion was noted in 46(14.6%). Preoperative variables predictive of capsular perforation and seminal vesicle invasion on univariate analysis were serum prostate specific antigen (PSA) concentration, clinical, stage, Gleason primary and secondary patterns, Gleason score, nuclear grade, perineural invasion and percent cancer in the biopsy specimens. On multivariate analysis, independent prognostic factors for capsular perforation and seminal vesicle invasion were PSA, Gleason score and percent cancer in the biopsy specimens. CONCLUSIONS: The combination of serum PSA concentration, Gleason score and percent cancer in the biopsy specimens provides the best prediction of capsular perforation and seminal vesicle invasion. Models based on this combination of factors may be clinically use to stratify patients for nonoperative treatment.

Adenocarcinoma↗
PubMedDate not supplied

Computed tomography of the normal seminal vesicles.

Fifty patients without pelvic pathology were studied in order to determine the normal appearance of the seminal vesicles on computed tomography (CT). The seminal vesicles could be identified in all patients. The mean length of each seminal vesicle was 3.1 +/- 0.5 cm and the mean width was 1.5 +/- 0.4 cm. Calculated areas of the seminal vesicles assuming an ellipsoid shape were 3.6 +/- 1.1 cm2 for each side. When correlated with patients' ages, no significant difference was identified between age and the length of the seminal vesicles, however, a significant difference was noted between the widths (P less than 0.01) and areas (P less than 0.05) of the seminal vesicles with patients of increasing age having smaller seminal vesicles. In 67% of patients these structures were symmetrical and in 33% some degree of asymmetry was noted. Variability in shape ranged from ovoid (70%), tubular (20%), and rounded (10%). In 48 of 50 patients, small punctate densities could be seen along the lateral aspects of both seminal vesicles which correspond to the anatomic region of the pudendal venous plexus.

Adult↗
PubMed1990

Seminal vesicles: development, secretory products, and fertility.

The development of the seminal vesicle from the mesonephric duct is described. Particular attention is given to the recent biochemistry of seminal vesicle proteins. Proteins in the seminal vesicle fluid are few in number, may be insoluble at certain pH, and frequently form large macromolecular aggregates. Although not an absolute requirement for fertility, seminal vesicle fluid assists in a number of ways to insure fertility. A biochemical model is presented that demonstrates that cAMP dependent phosphorylation may be an important interaction between sperm and certain seminal vesicle proteins.

Animals↗
PubMed1986

Primary leiomyosarcoma of the seminal vesicle.

A leiomyosarcoma of the seminal vesicle, found at an early stage on routine rectal examination, is described. The authors believe that this report represents, to date, the most conclusive documentation of primary origin of a sarcoma in the seminal vesicle. It is also the first report in which electron microscopy yielded definitive diagnostic information. Review of the previously reported cases suggests that radical surgery may offer a realistic chance for cure.

Genital Neoplasms, Male↗
PubMed1994

Sperm motility inhibitor from human seminal plasma: presence of a precursor molecule in seminal vesicle fluid and its molecular processing after ejaculation.

Human seminal plasma contains a protein factor that has the capacity to inhibit the movement of demembranated and intact spermatozoa. This factor 'seminal plasma motility inhibitor' (SPMI) has been shown to originate exclusively from the seminal vesicles. The present results demonstrate that the biological activity of SPMI in semen decreases rapidly from 1000 U/ml, immediately after ejaculation, to 220 U/ml 2 h later. Immunoblots of seminal plasma proteins probed with an antibody against human SPMI, revealed the rapid processing of a predominant 52 kDa SPMI antigen, present in the seminal vesicle secretions. This precursor was degraded initially into intermediate molecular mass fragments of 25-40 kDa, and subsequently into smaller fragments of 17-21 kDa. When seminal vesicle fluid was mixed with prostatic secretions (3:1 v/v), proteases present in prostatic secretions were shown to be responsible for processing of the SPMI precursor. Addition of protease inhibitors such as phenylmethylsulphonyl fluoride (PMSF, 5 mM), benzamidine (100 mM) or ethylenediaminetetraacetic acid (EDTA, 5 mM) to the mixture of seminal vesicle and prostate secretions partially prevented the loss of activity of SPMI by 54%, 27% and 9%, respectively. However, the simultaneous addition of PMSF and benzamidine conferred almost total stability to the SPMI precursor activity. These results demonstrate that SPMI exists as a predominant 52 kDa precursor form in the seminal vesicles and is processed rapidly after ejaculation into less active, lower molecular mass forms by one or more serine proteases and/or metalloproteases of prostatic origin which are present in liquefied semen.

Adult↗
PubMed1997

Indications for preoperative seminal vesicle biopsies in staging of clinically localized prostatic cancer.

OBJECTIVE: To identify patients at high risk of extraprostatic seminal vesicle infiltration, in whom preoperative seminal vesicle biopsies should be performed. MATERIALS AND METHODS: We studied the relationship between extraprostatic seminal vesicle infiltration and the available preoperative data [age, clinical stage, prostate-specific antigen (PSA) level, number and site of positive prostatic sextant biopsies, Gleason score] in a total of 75 patients suffering from clinically localized prostatic adenocarcinoma who were candidates for radical prostatectomy. RESULTS: The chi 2 test showed that the preoperative data most significantly correlated with extraprostatic seminal vesicle infiltration were the presence of positive basal biopsies (p < 0.001). The PSA level did not have any predictive value. The most discriminant preoperative parameter of the state of the seminal vesicles (analysis of variance on a univariate model) was the state of the basal prostatic biopsies. The importance of this parameter was confirmed by cluster analysis. Overall, the risk of extraprostatic seminal vesicle invasion was 0 (0/21 patients) when the 2 basal prostatic biopsies were negative, 10.25% (4/39 patients) when 1 of the 2 basal prostatic biopsies was positive and 73.33% (11/15 patients) when both basal prostatic biopsies were positive. CONCLUSIONS: In a patient with clinically localized prostatic adenocarcinoma who is a candidate for radical prostatectomy, seminal vesicle biopsies are useless when basal prostatic biopsies are negative, regardless of the state of other preoperative parameters. When 1 or 2 basal prostatic biopsies are positive, seminal vesicle biopsies can improve the pretreatment pathological staging.

Adenocarcinoma↗
PubMed1990

Biochemical properties of secretory proteins from rat seminal vesicles.

The secretions of rat seminal vesicles from the so-called copulatory plug when getting in contact with the secretions of the coagulating gland. Depending on the sexual activity of the respective animal and the extraction conditions, the protein pattern of the seminal vesicle secretion varies to some extent. We have studied the biochemical properties of the proteins SVS I, SVS II, sulfhydryl oxidase and SVS III-VIII. The most interesting protein is SVS II which is the main substrate of coagulating gland transglutaminase and serves as the most important monomer during semen coagulation. It is highly soluble in acidic solutions. The monomeric polypeptide has a molecular mass of 49 kDa, is glycosylated with fucose, glucose, mannose and N-acetylated sugars and has a highly basic pI of 10.5. Particularly interesting are its functional and structural relationships with actin. It is the first described protein with actin modulating properties that is secreted in an androgen-dependent manner.

Animals↗
PubMed2005

Congenital agenesis of seminal vesicle.

Congenital agenesis of the seminal vesicle (CASV) is frequently associated with congenital absence of the vas deferens (CAVD) or ipsilateral congenital vasoureteral communication. We reported two cases of a rare condition that the vas deferens open ectopically into Mullerian duct cyst associated with agenesis of the ipsilateral seminal vesicle. The diagnosis was confirmed by vasography. Transurethral unroofing of the Mullerian duct cyst was performed in both patients with favourable results, however, assisted reproductive technology (ART) was still necessary for them to father children.

Adult↗
PubMed1984

Hydrolysis of polyphosphoinositides by purified sheep seminal vesicle phospholipase C enzymes.

Sheep seminal vesicles contain two immunologically distinct phospholipase C (PLC) enzymes that can hydrolyze phosphatidylinositol (PI) (Hofmann, S.L., and Majerus, P.W. (1982) J. Biol. Chem. 257, 6461-6469). One of these enzymes (PLC-I) has been purified to homogeneity; the second (PLC-II) has been purified 2600-fold from a crude extract of seminal vesicles. In the present study we have compared the ability of these purified enzymes to hydrolyze PI, phosphatidylinositol 4-phosphate (PI-4-P), and phosphatidylinositol 4,5-diphosphate (PI-4,5-P2). Using radiolabeled substrates in small unilamellar phospholipid vesicles of defined composition, the two enzymes were found to hydrolyze all three of the phosphoinositides. Hydrolysis of all three phosphoinositides by both enzymes was stimulated by Ca2+; however, in the presence of EGTA only the polyphosphoinositides were hydrolyzed. The two enzymes displayed substrate affinities in the order PI greater than PI-4-P greater than PI-4,5-P2, and maximum hydrolysis rates in the order PI-4,5-P2 greater than PI-4-P greater than PI. When present in the same vesicles, PI and the polyphosphoinositides competed for a limiting amount of either enzyme. Inclusion of phosphatidylcholine into vesicles containing the phosphoinositides resulted in greater inhibition of PI hydrolysis than polyphosphoinositide hydrolysis. When all three phosphoinositides were present in vesicles mimicking the cytoplasmic leaflet of cell membranes, there was preferential hydrolysis of the polyphosphoinositides over PI. We conclude that a single phospholipase C can account for the hydrolysis of all three phosphoinositides seen during agonist-induced stimulation of secretory cells. The cytoplasmic Ca2+ concentration and phospholipid composition of the membrane, however, may influence the relative rate of hydrolysis of the three phosphoinositides.

Animals↗
PubMed1994

Major proteins of bovine seminal vesicles bind to spermatozoa.

Bovine seminal vesicles synthesize a family of closely related proteins, namely BSP-A1, BSP-A2, BSP-A3, and BSP-30-kDa (collectively called BSP proteins). Recently, we showed that these proteins bind specifically to choline phospholipids. Since this class of phospholipids is the major phospholipid fraction of the spermatozoan membrane, we investigated the binding of BSP proteins to spermatozoa. Polyclonal antibodies against purified BSP proteins raised in rabbits were used to detect these antigens in bovine epididymal and ejaculated spermatozoa as well as in bovine seminal plasma. Comparison of spermatozoa taken from the caudae epididymides with ejaculated spermatozoa through use of various techniques, namely, surface labeling followed by immunoprecipitation and immunoblotting, showed that epididymal spermatozoa are devoid of BSP proteins whereas ejaculated spermatozoa possess membrane-bound BSP proteins. Through use of the indirect immunofluorescence technique, the ejaculated spermatozoa of bull were characterized by an immunoreaction restricted to the midpiece, acrosome, and postacrosomal region, but no specific immunostaining could be found on the surface of epididymal spermatozoa. Surface-labeled BSP proteins on spermatozoa could not be displaced with buffers containing high salt concentration (1 M NaCl), but could be displaced specifically with phosphorylcholine (alone or in combination with urea). The data indicate that the BSP proteins that are secretory products of the seminal vesicles bind to the sperm surface upon ejaculation.

Animals↗
PubMed1997

The route of seminal vesicle involvement in adenocarcinoma of prostate: lymphaticovascular or local extension?

BACKGROUND: Adenocarcinoma of the prostate with seminal vesicle involvement indicates a rather poor prognosis. The aim of this study is to evaluate the route of seminal vesicle involvement via lymphaticovascular or local extension, as a possible way which may determine the extent of disease as systemic or local. METHODS: In a retrospective study of 32 patients who underwent radical prostatectomy for localized cancer of the prostate, medical records and imaging studies were reviewed, and the histopathological slides of the resected specimens were rechecked. RESULTS: Of 32 patients, 12 (37.5%) had seminal vesicle involvement. Seven patients had involvement of bilateral seminal vesicles and five had unilateral involvement. Tumor cells invaded the muscle portion of seminal vesicle from the adjacent prostatic tissues in all 12 patients. Four of the seven patients with involvement of bilateral seminal vesicles developed bony metastasis 7 to 12 months after operation. No patient with unilateral involvement of seminal vesicle was found to have disease progression to bony metastasis during follow-up for as long as 39 months. CONCLUSIONS: The route of seminal vesicle involvement in prostate cancer was through local extension in all of our patients. Involvement of bilateral seminal vesicles may have more chances to develop bony metastasis than unilateral involvement. Further study with a large number of patients is necessary to clarify the issue regarding the route of seminal vesicle involvement in adenocarcinoma of prostate.

Adenocarcinoma↗
PubMed1976

Control of the mitotic activity in the rat seminal vesicle by "chalone".

One month after castration male rats were injected daily with 2 X 50 mug of testosterone. Starting before the highest mitotic activity of seminal vesicles, 3 injections of normal seminal vesicle extract were given into the lumen at 3 h intervals. The contralateral seminal vesicle was injected with rat liver extract. Tritiated thymidine was given intravenously. The labelling index of the seminal vesicles was determined by means of radioautography. The crude supernatant of seminal vesicle was the most effective to inhibit the mitotic activity of the seminal vesicles. The decrease was on an average 34 per cent. The liver extract did not influence the mitotic activity. When the seminal vesicle extract was fractionated by Sephadex G-25, the largest fraction (M. W. greater than 3000) showed the highest inhibitory activity, whereas the smallest fraction (M. W. less than 1000) was ineffective. The inhibition of mitosis can also be induced by an unspecific factor, since pronase showed slight inhibitory action on seminal vesicle mitosis. However, the seminal vesicle extract had no inhibitory action on the epidermal mitotic activity.

Animals↗
PubMed1992

Immunohistochemical study of metallothionein in human seminal vesicles.

Metallothionein (MT) in human seminal vesicles was examined by use of the avidin-biotin-peroxidase complex method. Tissues were obtained from six patients with prostate cancer who underwent luteinizing hormone-releasing hormone agonist or estrogen therapy before radical prostatectomy (group 1) and from 18 patients without hormone therapy (three with prostate cancer, three with urinary bladder cancer, and twelve free of urogenital diseases at autopsy) (group 2). MT was localized in the cytoplasm and nuclei of epithelial cells and also in secretory products in the lumen. The epithelial cells lacked uniformity in immunoreaction; for instance, some stained strongly while others stained weakly. Smooth muscle cells were found to have positive immunoreaction, but other connective tissues had no immunoreaction. The number of strongly positive cells in group 1 was fewer than that in group 2 (not significant), and the secretory products in group 1 had no immunoreaction. These results suggest that MT is synthesized in the epithelial cells of the seminal vesicles and secreted into the fluids, and that the synthesis of MT is suppressed by the hormone therapy.

Aged↗
PubMed1997

In vitro administration of 17 beta-estradiol inhibits drug-induced contractions of the rat isolated seminal vesicle.

1. The rat isolated seminal vesicle responded to noradrenaline (NA), acetylcholine (ACh), potassium chloride (KCl) and barium chloride (BaCl2) with reproducible contractions. 2. 17 beta-estradiol (17 beta E) cumulatively added in the isolated organ bath reduced the number of contractions with all agonists used in the rank order of potency: BaCl2 > or = KCl > ACh > NA. The dose-response curves constructed in the presence of 17 beta E (2 x 10(-5) mol/l) produced a rightward shift and a reduction in the maximum response showing inhibitory activity. 3. When the calcium content in the normal Krebs medium (2.5 mmol/l) was reduced to half, the inhibitory activity of 17 beta E was potentiated. The maximum inhibition rates to KCl (phasic and tonic), BaCl2 and ACh were significantly (P < 0.05) different from each other. 4. The inhibitory effects of 17 beta E against all agonists tested were found to be similar in their responses to verapamil, but were much lower in potency. 5. The inhibitory effects of 17 beta E was seen only when the hormone was present in the tissue environment and was readily reversible as soon as the tissue was washed with the Krebs medium, suggesting that the effect of 17 beta E is localized. 6. It is suggested that the in vitro application of 17 beta E on the rat isolated seminal vesicle interferes with the process of translocation of calcium ions from the extracellular medium.

Acetylcholine↗
PubMed1994

[The volume of the seminal vesicles in general senior population].

The volume of the seminal vesicles in 413 males, who were submitted to a mass screening program for prostatic diseases by transrectal sonography, was measured by tracing ultrasonograms using a multi-planimeter. Ages of the subjects ranged from 46 to 88 years (mean age 67.0 years). The mean volume of the seminal vesicles for all cases was 14.55 +/- 5.11 cm3. The volume of the seminal vesicles was not related statistically to the height, body weight and body mass index of the subject. The volume of the seminal vesicles in cases of no prostatic diseases decreased with age, while that of cases of benign prostatic hypertrophy increased with the progress of the disease. These facts suggested that the seminal vesicles were androgen dependent, similar to the prostate.

Aged↗
PubMed1993

Primary structure and characterization of an androgen-stimulated autoantigen purified from mouse seminal-vesicle secretion.

A protein extract of mouse seminal-vesicle secretion was used to immunize mature mice (Balb/c) of both sexes. Results of Western-blot analyses for these secretory proteins indicated that only one minor protein component could be recognized by the autoantisera prepared from either autoimmunization of male mice or isoimmunization of female mice. The autoantigen was purified from seminal-vesicle secretion. The purified autoantigen retained the ability to induce autoantibody formation. The autoantigen has glycoprotein characteristics: the majority of the carbohydrate is N-linked and the remainder is O-linked. Rabbit antibodies to the autoantigen were used to isolate the corresponding cDNA from a mouse seminal-vesicle cDNA library. The primary structure deduced from the cDNA sequence was confirmed by direct amino acid sequence determination. The results indicate that the core protein consists of 131 amino acid residues. Analysis of the primary structure indicates that the autoantigen has two potential acceptor sites for the N-linked carbohydrate at Asn-12 and Asn-122, three potential phosphorylation sites for casein kinase II at Thr-55, Ser-68 and Thr-76, and three potential phosphorylation sites for protein kinase C at Thr-28, Thr-40 and Thr-124. The core protein and the carbohydrate portion together have a molecular mass of 19 kDa. Results from Western- and Northern-blot analyses for various tissues indicate that the seminal vesicle is the sole organ producing this autoantigen. Expression of this autoantigen gene was stimulated by testosterone.

Amino Acid Sequence↗