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Two cases of fistulation into the seminal vesicles are described. One related to Crohn's disease and the other following surgery for carcinoma of the rectum. Both cases were diagnosed by CT sinography. This technique is described and is recommended when attempting to demonstrate the internal communications of difficult perineal fistulae when standard techniques of fistulography fail.
PURPOSE: We investigated whether purified prostate specific antigen (PSA), a seminal plasma serine protease of the kallikrein enzyme family, is capable of releasing kinin-like peptides from natural substrate glycoproteins in human seminal vesicle fluid. MATERIALS AND METHODS: An in vivo rat bladder model was used to monitor for release of substances capable of inducing smooth muscle contractions. Purified PSA, seminal vesicle fluid (SVF) from radical prostatectomy specimens, bradykinin, saline and a bradykinin antagonist were injected intravesically into urethane-anesthetized rats, and the resulting bladder contractions were measured. RESULTS: Injection of either PSA or SVF alone did not induce bladder contractions. Injection of a mixture of SVF and PSA preincubated 15 minutes, however, induced strong bladder contractions (23 +/- 7 cm. H2O) that decreased with time (4 +/- 2 cm. H2O, after 90 minutes). Similar contractions were observed after injection of bradykinin (10(-4) M. = 39 +/- 14, 10(-6) M. = 27 +/- 9, 10(-8) M. = 7 +/- 4 cm. H2O). Addition of a bradykinin antagonist to the PSA-SVF mixture prior to injection blocked the observed bladder contractions (23 +/- 7 cm. H2O before, versus 0.3 +/- 1.2 cm. H2O after adding antagonist). CONCLUSIONS: We conclude that PSA produces a kinin-like substance by enzymatic cleavage of glycoproteins in human seminal fluid. This substance induces smooth muscle contractions which can be specifically blocked by addition of a bradykinin antagonist.
Soybean lipoxygenase and cyclooxygenase from ram seminal vesicles were inhibited by tannic acid and the apparent ID50's were 7.5 x 10(-7) M and 6 x 10(-6) M, respectively. The inhibition of lipoxygenase by tannic acid was noncompetitive. Benzophenone inhibited cyclooxygenase, and the ID50 was 8 x 10(-7) M. The inhibition constant, Ki values of both tannic acid and benzophenone are presented.
The genes for seminal vesicle secretory protein IV and prostate steroid binding protein component 3 of the rat share upstream homologies of which the most striking is a 30 nucleotide sequence located between position -190 and -330 relative to the major transcriptional initiation sites. This sequence does not appear to be a common repetitive element and deserves consideration as a potential site involved in the androgen regulated expression of these genes.
Selected peripheral autonomic nerves have been surgically divided or removed and the seminal vesicles subsequently examined using neurohistochemical and electron microscopic techniques. Following bilateral hypogastric anf pelvic nerve transection, the arrangement and distribution of intramural axons 14 days after operation were similar to those in control specimens. In contrast, removal of the pelvic plexus was accompanied by a gradual reduction of catecholamine and acetylcholinesterase so that by the seventh post-operative day nerves were not observed light microscopically in the muscle coat or the submucosa. These observations have been endorsed using electron microscopy, and the fine structure of intramural autonomic nerves in response to axotomy has been monitored during the post-operative period. It has been concluded that the cell bodies of axons which supply the wall of the seminal vesicles are located within the pelvic plexus and do not extend proximal to the sites of division of the hypogastric and pelvic nerves.
The seminal vesicles of Phlebotomus perniciosus were investigated by light microscopy, confocal scanning laser microscopy and by scanning and transmission electron microscopy. They have a complex structure, and three different morphological compartments called A, B and C are distinguished on the basis of their position and fine structure. Compartment A is continuous with the vasa deferentia and consists of a cylindrical wall limiting a lumen in which the spermatozoa are stored. Compartment B is hemispherical and surrounds compartment A like a muff. Compartment C constitutes an external coat surrounding A and B. The epithelial cells of each compartment are characterized by morphologically different secretory granules. The ultrastructural features of these cells are described and their role in sandfly reproductive biology is discussed.
Rat seminal vesicle secretion (SVS) contains a variety of protein complexes that seem to be linked by interchain disulfide bonds. Upon reduction and analysis by sodium dodecyl sulfate (SDS) gel electrophoresis, this pattern resolves to 3 major high molecular weight (SVS I-100,000, SVS II-50,000, SVS III-37,000) and 3 major low molecular weight protein bands (SVS IV, V, and VI). A two-dimensional SDS gel (1st dimension unreduced, 2nd dimension reduced) permitted identification of the components of the cross-linked species. In the native secretion, SVS I forms a series of oligomers that include both SVS II and III. Essentially all of SVS III is involved in these complexes, while the bulk of SVS II occurs instead as an apparent homodimer. The smaller proteins (SVS IV-VI) are not involved in covalently crosslinked complexes. The reduced forms of the larger polypeptides were isolated by a variety of procedures involving agarose gel filtration in 6M guanidine hydrochloride, reversed-phase high pressure liquid chromatography, ammonium sulfate fractionation, and preparative polyacrylamide gel electrophoresis. Based on its size, solubility, and amino acid composition, SVS II was identified as the major clottable protein of the secretion.
A modification of the rat isolated seminal vesicle preparation is described, emphasizing the necessity to use younger animals (40-50 days old and weighing between 125 and 150 g) and to expel thoroughly all vesicular contents. Under the experimental conditions used (tissues suspended under a resting tension of 350 mg in a continuous flow of a modified Krebs solution run at the rate of 15 ml/min, maintained at 32 degrees C, and bubbled with 5% CO2 in O2), the preparation was quite sensitive, but only to a few selected agonists, and remained viable for over 4-6 hr. Adrenaline, noradrenaline, dopamine, and acetylcholine all produced concentration-dependent and reproducible contractions. However, histaminergic, serotoninergic, purinergic, and opioid agonists were inactive as were prostaglandins of the E and F series and the polypeptides angiotensin, vasopressin, and oxytocin. In general, the tissue was rather insensitive to relaxant drugs, with only papaverine and sodium nitrite producing some relaxation in tissues previously contracted by carbachol. Advantages of the preparation include marked responsiveness, but only to a few selected agonists, and suitability for use as a paired tissue. It is suggested that employed under suitable experimental conditions, the preparation deserves a more frequent consideration for use during pharmacological investigations concerned with postsynaptic aspects of noradrenergic or cholinergic transmission.
Caltrin proteins from seminal vesicle content of the guinea pig bind with great specificity to different regions of the spermatozoa. Indirect immunofluorescence studies with polyclonal antibodies showed that caltrin I binds to the head, on the acrosomal cup, while caltrin II binds on the principal tail and the neck. No fluorescence was detected either in the midpiece or in the post-acrosomal area of the head when sperm were exposed to either of the caltrins. Calcium-induced hyaluronidase release, which occurs during the acrosomal reaction, was dramatically inhibited by caltrin I (approximately 85% inhibition). Caltrin II was less effective in preventing the enzyme release (approximately 50% inhibition). Chemical modification of the structure modified the biological activity of the two caltrins. Reduction and carboxymethylation of the cysteine residues diminished the inhibitory activity on 45Ca2+ uptake and reduced the ability of the proteins to react with their antibodies. Removal of the carbohydrate portion by chemical deglycosylation transformed the inhibitor proteins into enhancers of calcium uptake into the spermatozoa. Caltrin proteins from the guinea pig appear to play the same physiological role as bovine caltrin, regulating specifically calcium transport across the spermatozoal membranes related with the acrosome reaction and hyperactivation process. The dual behavior of caltrins to inhibit or enhance Ca2+ uptake enables them to fulfill this function. Nevertheless, molecular mechanisms different from those described for bovine caltrin seem to be involved in the control of the functional activity of the guinea pig caltrins.
A case report of a unilateral seminal vesicle cyst presenting as painless hematospermia in a 44-year-old patient is presented. Ultrasound-guided needle aspiration of the cyst demonstrated a markedly elevated LDH level in the cyst fluid of unknown significance. Antibiotic injection under ultrasound guidance into the seminal vesicle cyst was accomplished. Laboratory evaluation on the cyst fluid is suggested.
When the in vitro translation products of mRNAs from castrated animals (48 h) were compared with those from androgen-treated animals (48 h) to survey the molecular mechanism of androgen-responsive gene expressions in the rat seminal vesicles, some peptide bands which were repressed in response to androgen were observed. From these findings, we constructed a partial cDNA library of poly(A+)RNAs which had been isolated from the seminal vesicles of castrated rats (48 h) and modestly enriched with respect to the concentration of androgen-repressed mRNAs by sucrose density gradient centrifugation, and screened by differential colony hybridization. One cDNA clone, pSvr-1, whose mRNA is markedly induced within 24 h after castration of the animal in the seminal vesicles as well as in the ventral prostate, was isolated. pSvr-1 hybridized to a mRNA of 1,700 nucleotides in length. Partial sequence analysis showed that this clone had highly homologous but not identical sequences to those reported for rat sulfated glycoprotein-2. This cDNA clone may provide a useful probe for the study of the negative regulation mechanism of gene expression by androgens.
A 37-year-old man was hospitalized for a more extensive examination of azoospermia. A seminal vesiculogram demonstrated a cystic lesion of the right seminal vesicle, but failed to show the left seminal vesicle because of intrascrotal adhesion caused by previous orchidopexy. A transrectal ultrasonogram and CT-scan revealed a large cystic mass in the retrovesical region. At urethrocystoscopy, the left half of the trigone and left ureteral orifice were absent, and the verumontanum increased in size. Bilateral testicular biopsies demonstrated a small type of the seminiferous tubule showing a thickening of the basement membrane and low spermatogenesis. The cystic mass was examined by transabdominal needle aspiration under the guidance of supurapubic ultrasound. Microscopic examination of the cystic fluid obtained revealed a few immobile spermatozoa. The patient was not subjected to any surgical intervention.
Aminopeptidases hydrolysing L-leucine-beta-naphthylamine (LeuNA), L-alanine-beta-naphthylamide (AlaNA) and L-arginine-beta-naphthylamide (ArgNA) were studied in tissue homogenates of various parts of the rat prostatic complex and seminal vesicles after castration as well as in their 'cellular' and 'secretory' compartments. The 'secretory' fluids were also fractionated by chromatofocusing to reveal the enzymes possibly secreted by the glands. After castration the ventral prostate showed a temporary increase of LeuNA and a continuous rise of AlaNA hydrolysis, while ArgNA hydrolysis remained unaltered. Its 'secretory' fluid contained high hydrolysis rates of the substrates and chromatofocusing revealed two activity peaks with pI values of 6.2 and 5.4. In the lateral prostate no activity changes were recorded after castration. The 'secretory' fluid contained low enzyme activities and the fractionation showed one enzyme activity with pI 5.4. The posterior prostate, coagulating glands and seminal vesicles showed high hydrolysis rates of ArgNA with a rapid decline after castration. The 'secretory' fluid of posterior prostate contained rather low activity levels and in chromatofocusing two activity peaks with pI values of 6.2 and 5.4 were found. The 'secretory' fluid of coagulating gland contained a strong hydrolysis of ArgNA and chromatofocusing gave two activities with pI values of 5.4 and 5.1. The latter seemed to hydrolyse only ArgNA. The viscous secretion of the seminal vesicles contained very low aminopeptidase activities and chromatofocusing also showed a poor result. It is concluded that the various parts of the rat prostatic complex differ in their aminopeptidase composition. Only part of these enzymes appears to be secretory and controlled by testosterone. The major contribution to the seminal plasma aminopeptidase activity seems to derive from the ventral prostate and the coagulating gland.
In the present work we have investigated the effects of medium- (15 days) and long-term (2 months) castration on vasoactive intestinal peptide (VIP)-immunoreactive nerve fibres and 125I-labelled VIP binding sites in the adult hamster seminal vesicle. The density of VIP- and synaptophysin (general neuronal marker)-containing nerve fibres was determined in immunofluorescently stained cryostat sections using a computerised image analysis system. The morphological analysis of 125I-VIP binding sites in seminal vesicle cryostat sections was performed by quantitative receptor autoradiography. Our results show that the densities of the overall (synaptophysin immunoreactive) and VIPergic innervation increase in both medium and long-term castrated animals. In absolute terms, the quantity of VIP- and synaptophysin- containing nerves is not altered in medium-term castrates, but decreases for synaptophysin in long-term castrates. Medium-term castration does not affect the density of 125I-VIP binding sites in the gland muscular coat, but a significant decrease is observed after long-term castration. In conclusion, our results indicate that whereas VIP nerves are apparently unaffected by castration, 125I-VIP binding sites in the muscular coat of hamster seminal vesicle are sensitive to androgen levels.
Experiments were conducted to determine the effects of aryl hydrocarbon receptor (AhR) null mutation and in utero and lactational 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) exposure, alone and in combination, on prostate and seminal vesicle development in C57BL/6 mice. AhR heterozygous (Ahr+/-) mice were mated, and pregnant females were dosed orally on gestation day 13 with TCDD (5 microg/kg) or vehicle. Pups underwent necropsy on postnatal days (PNDs) 35 and 90. Comparison of vehicle-exposed AhR knockout (AhRKO;Ahr-/-) with wild-type (Ahr+/+) pups revealed that the AhR is necessary for normal dorsolateral prostate, anterior prostate, and seminal vesicle development but apparently not for ventral prostate development. In wild-type mice,in utero and lactational TCDD exposure reduced ventral prostate weight by 79-87% and mRNA expression for its major androgen-dependent secretory protein (MP25) by 99%. Yet high levels of mRNA for a secretory protein normally produced primarily by the lateral prostate (PSP94) were expressed. These effects were predominantly AhR dependent because TCDD had little if any effect in AhRKO mice. TCDD reduced dorsolateral prostate weight in wild-type but not AhRKO mice and had no significant effect on expression of mRNA for PSP94 or for probasin, a major androgen-dependent secretory protein. The PSP94 results suggest that TCDD may have caused a respecification of prostatic gene expression. TCDD reduced anterior prostate weight by more than half, and expression of mRNA for its major androgen-dependent secretory protein (renin-1) was greatly reduced. These effects were AhR dependent. Seminal vesicle weight was reduced by TCDD in wild-type mice but was increased in AhRKO mice on PND 35 and decreased on PND 90 (relative weight only). Androgen receptor mRNA levels were not significantly altered in any prostate lobe, and all organs appeared histologically normal in all groups. Serum testosterone concentrations were unchanged, and modest reductions in serum 5alpha-androstane-3alpha,17beta-diol concentrations could not account for the effects on sex organs. Collectively, these results indicate that the AhR signaling pathway plays a role in normal accessory sex organ development and thatin utero and lactational TCDD exposure disrupts development of these organs via spatially and perhaps temporally specific mechanisms.
A case of ectopic ureter in a cystic seminal vesicle associated to a microkidney is presented. The diagnosis was established by history, physical examination, CT and direct contrastography by perineal access. Treatment consisted of excision of the cystic seminal vesicle with the ectopic ureter and dysplasic kidney.
To assess the role of androgen receptors (ARs) in the expression of androgen-dependent seminal vesicle (SV) secretory proteins, tissue recombinants were prepared with rat seminal vesicle mesenchyme plus ureter epithelium of wild-type or Tfm mice (rat SVM plus wild-type mouse URE and rat SVM plus Tfm mouse URE, respectively). After growth in male hosts, both the wild-type and Tfm ureter epithelia were induced by SVM to differentiate into a simple columnar epithelium exhibiting the complex folded morphology characteristic of the SV. In SVM plus wild-type mouse URE recombinants, epithelial ARs were induced, and the epithelium expressed the full spectrum of SV secretory proteins. By contrast, in SVM plus Tfm mouse URE recombinants, the Tfm epithelium was genetically incapable of producing functional ARs and failed to produce SV secretory proteins. These data demonstrate in vivo that the induction of SV secretory proteins by androgens is an event requiring intraepithelial ARs. In contrast, androgen-dependent epithelial morphogenesis, columnar cytodifferentiation, and probably also proliferation can be expressed in Tfm epithelium grown in association with wild-type mesenchyme, strongly suggesting that these events are indirect effects on the epithelium mediated by mesenchymal ARs.
A 25-year-old man presented with painful ejaculation, an ejaculate volume of 0.75, and complaints of passing "granules" in the semen. Transrectal ultrasonography showed bilateral seminal vesicle enlargement. The patient underwent transurethral resection of the ejaculatory duct. The entry point of duct was resected using pure cutting current, resulting in the passage of multiple proteinaceous-appearing stones. Approximately 10 months later, the patient reported recurrent painful ejaculation and passage of granules in his semen. At cystoscopy, the ejaculatory duct openings were intubated with a cone-tipped catheter to perform bilateral seminal vesiculograms, which showed numerous mobile filling defects and a Steinstrasse appearance at the ejaculatory ducts. A 7F semirigid ureteroscope entered the lumen without difficulty over a guidewire, and the stones were fragmented with a 270-microm holmium laser fiber. The ejaculatory ducts were balloon dilated to 18F. To our knowledge, this is the first reported case where a ureteroscope was utilized to treat seminal-vesicle stones. The seminal vesiculogram proved to be extremely valuable in the diagnosis.