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Journal articles on the topic 'Seminal vesicles'

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Published: 4 June 2021
Last updated: 29 July 2024

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1

Higgins, S. J., P. Young, J. R. Brody, and G. R. Cunha. "Induction of functional cytodifferentiation in the epithelium of tissue recombinants. I. Homotypic seminal vesicle recombinants." Development 106, no. 2 (June 1, 1989): 219–34. http://dx.doi.org/10.1242/dev.106.2.219.

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Functional cytodifferentiation of seminal vesicle epithelium was investigated in tissue recombinants. Neonatal rat and mouse seminal vesicles were separated into epithelium and mesenchyme using trypsin. Epithelium and mesenchyme were then recombined in vitro to form interspecific rat/mouse homotypic recombinants. Growth as renal grafts in adult male athymic mice resulted in seminal vesicle morphogenesis in 70% of the recombinants (the remaining 30% failed to grow). Functional cytodifferentiation was judged by the expression of the major androgen-dependent secretory proteins characteristic of the seminal vesicles of adult rats and mice. Antibodies specific for each of these proteins were used to screen tissue sections by immunocytochemistry and to probe protein extracts by immunoblotting techniques. The heterospecific recombinants synthesized the full range of seminal vesicle secretory proteins that typifies the species providing the epithelium of the recombinant, not the mesenchyme. There was little functional variation between individual recombinants. The time course of development corresponded to that of intact neonatal seminal vesicles grown under the same conditions. Morphogenesis and functional cytodifferentiation were not evident after one week, but were well advanced after two weeks. Seminal vesicle recombinants grown for three weeks were indistinguishable morphologically and functionally from normal adult seminal vesicles. In addition, the ability of adult seminal vesicle epithelium to be induced to proliferate was examined. In association with neonatal seminal vesicle mesenchyme, the epithelium of the adult seminal vesicle proliferated and retained its normal functional activity. Thus, seminal vesicle functional cytodifferentiation can be faithfully reproduced in homotypic tissue recombinants. The methods used in this study will be used to investigate seminal vesicle development in instructive inductions of heterotypic epithelia.
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2

Dalimunthe, Naela Wanda Yusria, Agung Budiyanto, Erna Prawita Setyowati, and Agustina Dwi Wijayanti. "Korelasi Berat Badan dan Umur Sapi terhadap Berat, Volume Cairan dan Konsentrasi Prostaglandin F2α pada Vesikula Seminalis." Jurnal Sain Veteriner 35, no. 1 (June 1, 2017): 49. http://dx.doi.org/10.22146/jsv.29291.

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Seminal vesicles were collected from 60 heads of Bulls which butchered in slaughter house (RPH) Yogyakarta. The aims of this study are knowing the relationship between body weight, age, fluids volume and concentration of prostaglandin F2 α (PGF2α) in seminal vesicle of beef cattle. Those seminal vesicles were gathered from bulls which recorded its body weight and age then measured its seminal vesicles for weight, fluids volume and PGF2α levels. The PGF2α level was measured by Enzyme-Linked Immunosorbent Assay. Statistical analysis was performed using one way – analysis of varian, regression and correlation with P<0.05. Body weight of bulls showed positive correlation with the weight of seminal vesicle and its fluids volume. However, PGF2α levels were not correlated with the body weight of cattle. Weight of seminal vesicles also exhibited positive correlation with volume of vesicle fluids but no correlation with PGF2α levels. Based on the age of bulls, there were no correlation withthe weight of seminal vesicles, seminal fluids volume and PGF2α levels. Those result indicated that the weight and fluids volume were affected by the body weight of bulls altough the PGF2α levels have a standard of developmentwhich seems affected by other factors such as concentration of androgen hormone.
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3

Tamano, S., S. Rehm, M. P. Waalkes, and J. M. Ward. "High Incidence and Histogenesis of Seminal Vesicle Adenocarcinoma and Lower Incidence of Prostate Carcinomas in the Lobund-Wistar Prostate Cancer Rat Model Using N-nitrosomethylurea and Testosterone." Veterinary Pathology 33, no. 5 (September 1996): 557–67. http://dx.doi.org/10.1177/030098589603300511.

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The origin of chemically induced male accessory sex gland tumors was studied in Lobund-Wistar rats. Rats were treated at the age of 3 months with a single intravenous injection of 30 mg N-nitrosomethylurea (NMU)/kg body weight and given subcutaneous silastic implants filled with 40 mg testosterone propionate. Previous reports described a high incidence of prostate carcinomas in these rats with this treatment protocol. Additional animal groups included untreated controls, rats that received only an injection of 30 mg NMU/kg, and rats that were subjected to ablation of the seminal vesicle lobes prior to the treatment with NMU and testosterone. Three to 14 rats per group were sacrificed 4 to 10 months after NMU treatment and all remaining rats after 12 months. Twenty-four additional rats died or became moribund during the study. All rats were necropsied and the dorsolateral and ventral prostate and seminal vesicles with coagulating gland (anterior prostate) were examined histologically according to a standardized protocol. Lesions detected included atypical hyperplasia in all glands (resembling prostate intraepithelial neoplasia of human beings), adenomas in seminal vesicles only, and early carcinomas and adenocarcinomas in seminal vesicles and coagulating gland. Early carcinomas of the seminal vesicle, microscopically small and with invasion of the lamina propria and/or tunica muscularis, were detected as rapidly as 4 months after treatment. The vast majority (>95%) of the grossly visible nodules/masses originated from the seminal vesicles. Testosterone treatment enhanced occurrence and increased the incidence of all lesions, particularly of seminal vesicle adenocarcinomas, from 30% (7/23) to 64% (21/33). Coagulating gland tumors were found in 21% (7/33) of the rats. Ablation of the seminal vesicle lobes reduced the incidence of seminal vesicle adenocarcinomas to 11% (3/29), and these tumors arose from tissues remaining within the parenchyma of the seminal vesicle/prostate complex after ablation. Thus, NMU-induced and testosterone-promoted male sex gland tumors of the Lobund-Wistar rat arise almost exclusively in the seminal vesicles and coagulating gland (anterior prostate), are highly invasive in seminal vesicles before attaining a grossly visible size, and progress rapidly within 4 months, spreading to adjacent tissues and other organs.
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4

Malinowski, Damian, Paweł Grzegółkowski, Katarzyna Piotrowska, Marcin Słojewski, and Marek Droździk. "Membrane Transporters and Carriers in Human Seminal Vesicles." Journal of Clinical Medicine 11, no. 8 (April 15, 2022): 2213. http://dx.doi.org/10.3390/jcm11082213.

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Seminal vesicles play an important role in the male reproductive system, producing seminal fluid and thus adequate environment for sperm. However, mechanisms underlying secretory functions of the seminal vesicles’ epithelium have not been defined yet. The aim of the present study was to characterize expression and immunolocalization of selected membrane transporters and carriers in the seminal vesicles. The study included biopsy specimens collected from non-affected parts of seminal vesicles from 53 patients of Caucasian origin subjected for prostatectomy. RT-PCR was used to define expression of 15 genes coding for ABC-family and 37 genes encoding 37 SLC-family transporters/carriers. Immunohistochemistry was used to define localization of 6 transporters. In the seminal vesicles, the following membrane transporters and carriers were defined: ABCA1, ABCB1, ABCB5, ABCB6, ABCC1, ABCC2, ABCC3, ABCC4, ABCC5, ABCC6, ABCG2, SLC01C1, SLC02B1, SLC04A1, SLC04C1, SLC10A1, SLC15A1, SLC15A2, SLC16A1, SLC16A3, SLC19A1, SLC22A1, SLC22A3, SLC22A11, SLC22A18, SLC22A4, SLC22A5, SLC28A1, SLC2A9, SLC33A1, SLC47A1, SLC47A2, SLC51A, SLC51B, SLC7A5, SLC7A6. Age-dependent expression was evidenced for ABCB1, ABCG2, SLC04C1, SLC15A1, SLC16A1, SLC22A11, SLC22A18, SLC47A1 and SLC47A2. ABCG2, P-gp, MRP1, MRP3, MCT1 and LAT1 were localized in the apical membrane and P-gp in the basolateral membrane of the seminal vesicle epithelium. The expression of the membrane transporters and carriers in the seminal vesicle epithelium confirms its secretory and barrier functions.
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5

Eken, Alper, Volkan Izol, I. Atilla Aridogan, Seyda Erdogan, Arbil Acikalin, and Zuhtu Tansug. "An unusual cause of hematospermia: Primary adenocarcinoma of the seminal vesicle." Canadian Urological Association Journal 6, no. 6 (December 13, 2012): 259. http://dx.doi.org/10.5489/cuaj.127.

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Adenocarcinoma of the seminal vesicles is one of the rare causes of hematospermia. Primary seminal vesicle adenocarcinoma is extremely rare and difficult to diagnose due to frequent invasion of adenocarcinomas of the surrounding organs, especially the prostate. In the present study, a case of a primary seminal vesicle adenocarcinoma will be discussed in the light of the current literature.
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6

HORTON, MICHAEL J., and ROBERT H. GETZENBERG. "Rat Seminal‐Vesicle Secretory Protein SVS II Binds DNA With a Preference for the 5′ Regulatory Region of Secretory Protein SVS IV Gene: Co‐Isolation With Components of the Nuclear Matrix." Journal of Andrology 20, no. 2 (March 4, 1999): 267–79. http://dx.doi.org/10.1002/j.1939-4640.1999.tb02518.x.

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ABSTRACT: In rats, the ventral prostate and seminal vesicles produce distinct sets of proteins whose functions and tissue‐specific regulation by androgens remain unclear. We have utilized the genes encoding the major secretory protein of seminal vesicles, SVS IV, and the C3 subunit of prostatein of the ventral prostate to study how the nuclear matrix might determine their tissue‐specific gene expression. Nuclear matrix proteins were prepared from purified nuclei with DNase and 2 M NaCl, separated in SDS gels, and transferred onto membranes for DNA‐binding (southwestern) and immunological (western) analyses. The 5′ region of the SVS IV gene (SVS IV‐7S) bound to a 45,000‐kDa molecular‐weight protein band in the nuclear matrix of seminal vesicles but not to that of ventral prostate, kidney, or liver. Sequencing revealed that this band was a seminal‐vesicle secretory protein, SVS II, whose identity was confirmed with an anti‐SVS II antiserum in western blots. Actin‐like protein, similar in mobility to SVS II, was detected in seminal‐vesicle and ventral prostate nuclear matrix, but not in seminal‐vesicle fluid. Reducing agent (10 mM dithiothreitol) and acidic (pH 6.5) buffer did not eliminate SVS II, but isolation of nuclear matrices with ammonium sulfate, nucleases, and urea decreased SVS II immunoreactivity and removed actin‐like protein. SVS II binding to SVS IV‐7S DNA was greater than its binding to either a comparable fragment of the C3 gene or linearized pUC‐19 plasmid, and it was not eliminated by a 100‐fold competition. When seminal‐vesicle fluid was mixed with rat liver, some SVS II co‐isolated with the nuclear‐matrix proteins, indicating that nonspecific interactions contribute to its association with the nucleo‐skeleton. However, these interactions may not represent the intracellular behavior of SVS II in seminal‐vesicle epithelium. Sequence comparisons indicate significant homologies between SVS II and some other seminal proteins, including bovine caltrin, which, under the name seminalplasmin, is known to possess antimicrobial activity. Collectively, these data suggest that in addition to its known functions, SVS II may also bind extraneous DNA in seminal fluid. Additionally, SVS II may participate as a structural component in the organization of a tissue‐specific seminal‐vesicle nuclear matrix.
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7

Shukri, N. M., F. Grew, and J. G. M. Shire. "Recessive mutation in a standard recombinant-inbred line of mice affects seminal vesicle shape." Genetical Research 52, no. 1 (August 1988): 27–32. http://dx.doi.org/10.1017/s0016672300027270.

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SummaryA recessive autosomal mutation has been found in the CXBI/ByEss recombinant-inbred line but in neither of the parental strains, C57BL/6ByEss and BALB/cByEss. Its presence in the CXBI/ByJax and CXBI/ByLac sublines suggests an origin early in inbreeding. The locus, seminal vesicle shape (svs), appears to be linked to the albino locus on chromosome 7. The homozygote has seminal vesicles with a smooth tubular external appearance. In segregating crosses homozygotes had slightly lighter seminal vesicles but the weights of other androgen target organs were not reduced. Exogenous testosterone increased the size of the seminal vesicles but did not alter their shape. The mutation did not affect the pattern of proteins on SDS–acrylamide gel electrophoresis, which did differ between the parental strains. The locus affecting a 27000 Da protein has provisionally been assigned the symbolsvp-4.
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8

Hiroyoshi, Satoshi, Takayuki Mitsunaga, Tomoko Ganaha-Kikumura, and Gadi V. P. Reddy. "Effects of Age, Phase Variation and Pheromones on Male Sperm Storage in the Desert Locust, Schistocerca gregaria." Insects 12, no. 7 (July 14, 2021): 642. http://dx.doi.org/10.3390/insects12070642.

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In general, sperm produced in the testis are moved into the seminal vesicle via the vas deferens in insects, where they are stored. How this sperm movement is controlled is less well understood in locusts or grasshoppers. In this study, the effects of age, phase variation and pheromones on male sperm storage were investigated in the desert locust, Schistocerca gregaria (Forskål). In this locust, a pair of ducts, the vasa deferentia, connect the testes to a pair of the long, slender seminal vesicles that are folded approximately thirty times, and where the sperm are stored. We found that phase variation affected the level of sperm storage in the seminal vesicle. Moreover, adult males that detected pheromones emitted by mature adult males showed enhanced sperm storage compared with males that received the pheromones emitted from nymphs: The former, adult male pheromones are known to promote sexual maturation of immature adults of both sexes, whereas the latter, nymphal pheromones delay sexual maturation. Most mature adult males had much sperm in the vasa deferentia at all times examined, suggesting daily sperm movement from the testes to the seminal vesicles via the vasa deferentia. As adult males aged, sperm were accumulated from the proximal part to the distal end of the seminal vesicle. Many sperm remained in the seminal vesicle after mating. These results suggest that young or new sperm located near the proximal part of the seminal vesicle could be used for mating, whereas old sperm not used for mating are stored in the distal part of the seminal vesicle.
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9

Komori, Koji, Takashi Hirai, Yukihide Kanemitsu, Yasuhiro Shimizu, Tsuyoshi Sano, Seiji Ito, Yoshiki Senda, Kazunari Misawa, Yuichi Ito, and Tomoyuki Kato. "Pathology Studies of Combined Radical Resection of Seminal Vesicle in the Treatment of Rectal Cancer." International Surgery 96, no. 1 (January 1, 2011): 51–55. http://dx.doi.org/10.9738/1362.1.

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Abstract To inhibit local recurrence of rectal cancer, it is very important to ensure that there is a sufficient circumferential resection margin. We evaluated pathology studies of combined radical resection of seminal vesicles in the treatment of rectal cancer. We analyzed data from 7 cases of combined radical resection of the seminal vesicle in the treatment of rectal cancer; we also analyzed data from 35 control cases without seminal vesicle resection. The circumferential resection margin averaged 5.97 mm for cases that had combined radical resection of the seminal vesicle, and this was significantly longer than for cases without resection (P &lt; 0.001). Local recurrence was not seen in cases that had combined radical resection of the seminal vesicle, whereas 3 cases (5.9%) occurred in the group that did not undergo resection. Combined radical resection of the seminal vesicle in patients with rectal cancer ensures that the distance of the circumferential resection margin is sufficient to inhibit local recurrence.
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10

Shah, Rajal B., Min W. Lee, Alvaro A. Giraldo, and Mahul B. Amin. "Histologic and Histochemical Characterization of Seminal Vesicle Intraluminal Secretions." Archives of Pathology & Laboratory Medicine 125, no. 1 (January 1, 2001): 141–45. http://dx.doi.org/10.5858/2001-125-0141-hahcos.

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Abstract Context.—We have observed intraluminal crystalloid morphology in seminal vesicles that is superficially similar to that seen in prostate neoplasia, but found little information on such morphology in the literature. Design.—Two hundred fifty-three prostate specimens (163 needle biopsies, 75 radical prostatectomies with prostate carcinoma, 11 prostates from autopsy, and 4 cystoprostatectomies without prostate carcinoma) were examined for seminal vesicle secretions, which were categorized as (a) dense platelike inspissated, (b) fluidlike, (c) crystalloid morphology, and (d) absent. Histochemical stains (periodic acid–Schiff with and without diastase, Alcian blue at pH 2.5, and mucicarmine) were performed to characterize the nature of secretions. Results.—Proteinaceous secretions were identified in 82% of seminal vesicles examined. Of these, 61% had predominantly dense, platelike, inspissated secretions, 15% had predominantly fluidlike secretions, and 24% had predominantly crystalloid morphology. Although in some cases the crystalloid morphology resembled that of prostatic intraluminal crystalloids, the seminal vesicle crystalloids differed in that they were invariably multiple, had curved edges, and had varied forms (elliptical, cylindrical, rodlike, and rectangular). Seventy-one percent of seminal vesicle crystalloids were associated with dense, platelike, inspissated secretions and appeared to be created by fracturing within platelike secretions. There was no relationship between seminal vesicle crystalloid morphology and associated malignancy in the prostate gland, as it was seen in 24% of cases with prostate carcinoma and 25% of cases without prostate carcinoma (P = 1.0000). Fluidlike secretions were positive for Alcian blue (pH 2.5) and mucicarmine, whereas dense platelike secretions and crystalloid morphology were negative for Alcian blue (pH 2.5) and mucicarmine. Conclusions.—Seminal vesicle secretions are fairly common and, when fluidlike, are composed of acid mucopolysaccharides. Inspissation of secretions appears to be associated with loss of acidity, presumably resulting in dense platelike secretions and crystallization. Awareness of both the crystalloid morphology in seminal vesicle tissue and the distinguishing features from prostatic crystalloids may be important while interpreting prostate needle biopsies in which seminal vesicle epithelium may be confused for prostate carcinoma because of a small acinar morphology with accompanying cytologic atypia and crystalloid morphology.
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11

Higgins, S. J., P. Young, and G. R. Cunha. "Induction of functional cytodifferentiation in the epithelium of tissue recombinants. II. Instructive induction of Wolffian duct epithelia by neonatal seminal vesicle mesenchyme." Development 106, no. 2 (June 1, 1989): 235–50. http://dx.doi.org/10.1242/dev.106.2.235.

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When grown as renal grafts in adult male hosts, the upper (cranial), middle and lower (caudal) portions of fetal mouse and rat Wolffian ducts developed into epididymis, epididymis plus ductus deferens, and seminal vesicle, respectively. In heterotypic tissue recombinants, the epithelia from upper and middle Wolffian ducts were instructively induced to undergo seminal vesicle morphogenesis by neonatal seminal vesicle mesenchyme. Functional cytodifferentiation was examined in these recombinants using antibodies against major androgen-dependent, seminal vesicle-specific secretory proteins. The instructively induced Wolffian duct epithelia synthesized normal amounts of all of the secretory proteins characteristic of mature seminal vesicles, as judged by immunocytochemistry on tissue sections and gel electrophoresis plus immunoblotting of secretions extracted from the recombinants. In heterospecific recombinants composed of rat and mouse tissues, the seminal vesicle proteins induced were specific for the species that had provided the epithelium. This showed that the seminal vesicle epithelium in the recombinants was derived from instructively induced Wolffian duct epithelium and not from epithelial contamination of the mesenchymal inductor. Upper Wolffian duct epithelium, instructively induced to undergo seminal vesicle morphogenesis, did not express epididymis-specific secretory proteins, showing that its normal development had been simultaneously repressed.
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12

Veyssiere, G., Ch Jean-Faucher, M. Berger, and Cl Jean. "Evidence for reversible and irreversible biochemical defects in accessory sex organs and kidney of neonatally androgenized male mice." Acta Endocrinologica 121, no. 1 (July 1989): 121–28. http://dx.doi.org/10.1530/acta.0.1210121.

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Abstract. Studies were conducted to evaluate the effects of neonatal administration of supraphysiological doses of testosterone on the growth, hormone responsiveness, DNA and protein content, and protein profiles of the epididymis, vas deferens and seminal vesicles in adult mice. Results indicate that in androgenized males, testicular growth (DNA and protein content), circulating and organ androgen levels, and fertility were significantly depressed. The weights of the epididymis, vas deferens, seminal vesicle and kidney, but not that of the spleen, were significantly diminished subsequently to a reduction of protein (all organs) and DNA (epididymis, vas deferens) content. The efficacy of testosterone in promoting accessory sex organs and kidney growth, in adult castrated males, was persistently reduced in neonatally androgenized males. When assessed by DNA content, the response of all organs (except the seminal vesicle) was similar to that of controls, but it was significantly reduced from 16 to 43% when measured in terms of protein content. The protein profiles from seminal vesicles and vas deferens analysed by polyacrylamide gel electrophoresis, showed reproducible persistent alterations which could be reversed by adult androgen therapy.
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13

Cordeiro, Luiz, Hsiu-Lien Herbie Lin, Anaïs Vitorino Carvalho, Isabelle Grasseau, Rustem Uzbekov, and Elisabeth Blesbois. "First insights on seminal extracellular vesicles in chickens of contrasted fertility." Reproduction 161, no. 5 (May 2021): 489–98. http://dx.doi.org/10.1530/rep-20-0462.

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Male subfertility causes are very varied and sometimes related to post-gonadic maturation disruption, involving seminal plasma constituents. Among them, extracellular vesicles are involved in key exchanges with sperm in mammals. However, in birds, the existence of seminal extracellular vesicles is still debated. The aim of the present work was first to clarify the putative presence of extracellular vesicles in the seminal plasma of chickens, secondly to characterize their size and protein markers in animals showing different fertility, and finally to make preliminary evaluations of their interactions with sperm. We successfully isolated extracellular vesicles from seminal plasma of males showing the highest differences in semen quality and fertility by using ultracentrifugation protocol (pool of 3 ejaculates/rooster, n =3/condition). Size characterization performed by electron microscopy revealed a high proportion of small extracellular vesicles (probably exosomes) in chicken seminal plasma. Smaller extracellular vesicles appeared more abundant in fertile than in subfertile roosters, with a mean diameter of 65.12 and 77.18 nm, respectively. Different protein markers of extracellular vesicles were found by western blotting (n = 6/condition). Among them, HSP90A was significantly more abundant in fertile than in subfertile males. In co-incubation experiments (n = 3/condition), extracellular vesicles enriched seminal fractions of fertile males showed a higher capacity to be incorporated into fertile than into subfertile sperm. Sperm viability and motility were impacted by the presence of extracellular vesicles from fertile males. In conclusion, we successfully demonstrated the presence of extracellular vesicles in chicken seminal plasma, with differential size, protein markers and putative incorporation capacity according to male fertility status.
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14

Noorafshan, Ali, and Saied Karbalay‑Doust. "Curcumin Protects the Seminal Vesicles from Metronidazole‑induced Reduction of Secretion in Mice." Acta Medica (Hradec Kralove, Czech Republic) 55, no. 1 (2012): 32–36. http://dx.doi.org/10.14712/18059694.2015.72.

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Seminal vesicle secretion is important for increasing the stability of sperm chromatin, inhibition of the immune activity in the female reproductive tract and so on. Metronidazole (MTZ), a drug used for treatment of infections caused by anaerobic bacteria and protozoa, may have negative effects on the genital gland including the seminal vesicles. Curcumin exhibits antioxidant as well as anti‑inflammatory properties. The present study aims to evaluate the negative effects of MTZ on the seminal vesicle structure and ameliorative effects of curcumin using stereological methods. Thirty balb/c mice were divided into six groups. The control group was received distilled water. The second and the third received higher doses of MTZ (500 mg/kg body weight/day) and MTZ (500 mg/kg/day) + 100 mg/kg/day curcumin, respectively. The fourth and the fifth were treated with lower doses of MTZ (165 mg/kg body weight/day) and MTZ (165 mg/kg body weight/day) + curcumin (100 mg/kg body weight/day), respectively. The sixth group received 100 mg/kg body weight/day curcumin. All the administrations were done by oral gavages for 14 days. After 30 days, seminal vesicles were removed. Stereological study of the seminal vesicle structure revealed a significant reduction in gland and vesicular fluid volume in MTZ‑treated (higher or lower doses) animals. Curcumin protected the reduction of both parameters in therapeutic‑dose treated animals. Metronidazole treatment does not induce structural changes in the seminal gland; however, it can have a significant impact on its secretion ability. Importantly, these deteriorations might be preventable by curcumin co‑treatment.
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15

Hevia Palacios, M., M. Álvarez-Maestro, J. Gómez Rivas, A. Aguilera Bazan, and L. Martínez-Piñeiro. "Zinner Syndrome with Ectopic Ureter Emptying into Seminal Vesicle." Case Reports in Urology 2021 (January 25, 2021): 1–4. http://dx.doi.org/10.1155/2021/8834127.

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A 66-year-old male patient in follow-up in the urology department for a non-muscle-invasive bladder cancer was detected by ultrasound to have absence of the left kidney and a cystic, multilobed image at the location of the seminal vesicle. Magnetic resonance imaging reveals left renal agenesis and the existence of multiple cysts in the ipsilateral seminal vesicle that reaches a size of 6.9 × 3.7 cm , as well as a ureteral remnant that opens into the seminal vesicle. The patient does not present urinary symptoms, neither pain with ejaculation nor hematuria. A triad of seminal vesicle cyst, ipsilateral renal agenesis, and ipsilateral ejaculatory duct obstruction is known as Zinner syndrome. Congenital anomalies of the seminal vesicles are rare; some of them are associated with malformations of the upper urinary system. Seminal vesicle cysts are associated with ipsilateral renal agenesis and ectopic or dysplastic ureter. Patients may remain asymptomatic and be diagnosed incidentally or may present with symptoms such as increased urinary frequency, dysuria, recurrent infections, pain with ejaculation, and perineal discomfort.
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16

Tani, Y., A. Suttie, G. P. Flake, A. Nyska, and R. R. Maronpot. "Epithelial-Stromal Tumor of the Seminal Vesicles in the Transgenic Adenocarcinoma Mouse Prostate Model." Veterinary Pathology 42, no. 3 (May 2005): 306–14. http://dx.doi.org/10.1354/vp.42-3-306.

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The transgenic adenocarcinoma mouse prostate (TRAMP) model, designed for researching human prostatic cancer, was genetically engineered to harbor a transgene composed of the simian virus 40 Large-T/small-t antigen promoted by the rat probasin gene. In addition to prostatic neoplasms, the TRAMP mouse develops tumors in the seminal vesicles. This study was conducted to evaluate the pathology and histogenesis of TRAMP seminal vesicle neoplasms. Tissues of accessory sex organs harvested from 72 TRAMP mice of various ages (11-40 weeks of age) were fixed in neutral buffered formalin and stained with hematoxylin and eosin, desmin, 5-bromo-2′-deoxyuridine (BrdU, treated animals only), and SV40 Large-T antigen (SV40-Tag). In the seminal vesicles, we found neoplastic stromal cells that emerged multicentrically just beneath the epithelium, densely packed between the epithelium and the smooth muscle layer These stromal cells frequently exhibited mitotic figures and showed BrdU incorporation and SV40-Tag protein expression in the nuclei and immunopositivity for desmin. The proliferative mesenchymal cells were lined by cuboidal to columnar epithelium. Some of the larger papillary, polypoid lesions exhibited a phyllodes pattern resembling that seen in mixed epithelial-stromal tumors of the breast, prostate, and seminal vesicles of humans. Although the epithelium was negative for SV40-Tag and showed only occasional incorporation of BrdU, it clearly participated in the biphasic proliferation, forming papillary, cystic, and tubuloglandular structures. No conclusive evidence of malignancy (invasion or metastasis) was identified. Our recommended diagnosis of this lesion in the seminal vesicles is epithelial-stromal tumor.
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17

Sandeep, Bande, Nerkar Archana, and Bhandarkar Sudhir. "Histological Investigation of Cyclic Variation in Secretory Activity of Seminal Vesicles in Emballonurid Bat, Taphozous kacchensis (Dobson)." International Journal of Zoological Investigations 08, no. 02 (2022): 262–71. http://dx.doi.org/10.33745/ijzi.2022.v08i02.033.

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The present study describes the cyclical changes in the secretory activity of the seminal vesicle in the emballonurid bat, Taphozous kacchensis. The secretory activity in the seminal vesicles during the quiescence cycle was not well marked in T. kacchensis. During the sexually quiescent period (May to August), seminal vesicles were regressed, the tubules were lined by cuboidal to low columnar epithelial cells with round to elongated darkly stained basally to centrally placed nuclei. Cytoplasm was basophilic containing fine or coarse secretory granules in the cytoplasm. The lumina of the tubules were devoid of secretion. During the pre-breeding (September to January) period, the tubules were enlarged and were lined by tall columnar epithelial cells with large spherical basally situated nucleus. The secretory blebs were seen arising from the apical surface of the cells and were seen releasing into the lumen. Lumina of the tubules were filled with homogenous eosinophilic secretion. During the breeding period (February to March), the seminal vesicle showed hypertrophy resulting in the increase in the tubular diameter as compared to that of quiescent period. The epithelial lining of the tubules was cuboidal with centrally placed nuclei. The tubular lumina were full of homogenous secretion during active pre-breeding and breeding period as the secretory material released into the lumen by both apocrine and merocrine modes. Regressive changes in the seminal vesicle were evident from April. The tubules showed gradual hypotrophy as the quiescent period approaches in May.
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18

Li, Sheng-Hsiang, Robert Kuo-Kuang Lee, Ming-Huei Lin, Yuh-Ming Hwu, Chung-Hao Lu, Ying-Jie Chen, Hsuan-Chiang Chen, Wen-Hwei Chang, and Wei-Chao Chang. "SSLP-1, a secreted Ly-6 protein purified from mouse seminal vesicle fluid." Reproduction 132, no. 3 (September 2006): 493–500. http://dx.doi.org/10.1530/rep.1.01183.

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The Ly-6 protein family refers to a group of glycophosphatidyl inositol-anchored membrane proteins with ten conserved cysteines. They are thought to be involved in cellular adhesion and signaling. Recently, a subfamily of secreted Ly-6 proteins has been identified. In the present study, we report a secreted Ly-6 protein, secreted seminal vesicle Ly-6 protein 1 (SSLP-1) purified from mouse seminal vesicles using a series of steps including ion-exchange chromatography on a diethylaminoethyl (DEAE)-Sephacel column, gel filtration on a Sephadex G-75 column, and ion-exchange HPLC on a sulfopropyl column. Further analysis demonstrated it to be a novel, previously unnamed, 17 kDa glycoprotein.N-glycosidase F treatment revealed a core protein with a molecular mass of 8720 Da. By Basic Local Alignment Search Tool Protein analysis, we found that SSLP-1 had ten conserved cysteine residues identical with other secreted Ly-6 proteins. The geneGm191, which is located on chromosome 9, encodes SSLP-1. By Northern blotting with 21 different mouse tissues, we found thatSslp-1mRNA was predominantly expressed in the seminal vesicle. Immunohistochemistry revealed SSLP-1 protein in the luminal fluid and mucosal epithelium of the seminal vesicles. The amount ofSslp-1mRNA and SSLP-1 protein in the seminal vesicle was regulated by testosterone and correlated with the stage of animal maturation. The tissue-specific expression pattern suggests that SSLP-1 may play a physiological role in male mouse reproduction.
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Gupta, Sounak, Loren Herrera-Hernandez, and Lori A. Erickson. "Amyloid Involving the Seminal Vesicles." Mayo Clinic Proceedings 97, no. 6 (June 2022): 1213–14. http://dx.doi.org/10.1016/j.mayocp.2022.04.010.

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Tjionas, George A., Jonathan I. Epstein, Sean R. Williamson, Mireya Diaz, Mani Menon, James O. Peabody, Nilesh S. Gupta, et al. "Average Weight of Seminal Vesicles." International Journal of Surgical Pathology 23, no. 8 (August 25, 2015): 617–22. http://dx.doi.org/10.1177/1066896915600519.

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21

Herts, Brian R. "Calcification of the Seminal Vesicles." Journal of Urology 194, no. 1 (July 2015): 209–11. http://dx.doi.org/10.1016/j.juro.2015.04.017.

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22

Panach-Navarrete, J., F. García-Morata, J. A. Hernández-Medina, and J. M. Martínez-Jabaloyas. "When to biopsy seminal vesicles." Actas Urológicas Españolas (English Edition) 39, no. 4 (May 2015): 203–9. http://dx.doi.org/10.1016/j.acuroe.2015.03.002.

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23

Ramchandani, Parvati, Marc P. Banner, and Howard M. Pollack. "Imaging of the seminal vesicles." Seminars in Roentgenology 28, no. 1 (January 1993): 83–91. http://dx.doi.org/10.1016/s0037-198x(05)80115-4.

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Llerena, José, and Janis Letourneau. "Other Prostatic Interventions Seminal Vesicles." Seminars in Interventional Radiology 6, no. 02 (June 1989): 102–7. http://dx.doi.org/10.1055/s-2008-1075904.

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25

Alikhan, Mir Basharath, Vera Tesic, Jerome B. Taxy, and Tatjana Antic. "Cytomegalovirus Infection of Seminal Vesicles." International Journal of Surgical Pathology 24, no. 8 (July 28, 2016): 720. http://dx.doi.org/10.1177/1066896916657592.

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Ferreira, Ríudo De Paiva, Hugo De Azevedo Werneck, Juliana Malta, Aparecida Das Dores Teixeira, Lucio Antonio de Oliveira Campos, and José Eduardo Serrão. "Post-embryonic Development of the Seminal Vesicle in the Stingless Bee Melipona quadrifasciata Lepeletier, 1836 (Apidae: Meliponini)." Sociobiology 66, no. 2 (August 20, 2019): 287. http://dx.doi.org/10.13102/sociobiology.v66i2.3431.

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The male accessory glands of stingless bees (Apidae: Meliponini) are absent and the morphology of their seminal vesicle indicate probable secretory function by this organ. This study investigated the post-embryonic development of the seminal vesicles in males of the stingless bee Melipona quadrifasciata by histology and histochemistry. White-eyed pupae, pink-eyed pupae, brown-eyed pupae, black-eyed pupae, newly emerged and sexually mature males were studied. Seminal vesicle has a wall with a single layered epithelium onto a thin basement membrane, followed by a well-developed muscle layer. The epithelium is polarized in the pupal stage with basal cell region strongly positive for glucoconjugates and carbohydrates. The seminal vesicle has an enlarged lumen from the young pupal stages with luminal content increasing gradually with glucoconjugates along the pupal development. In the newly emerged and mature males, the histochemical tests to carbohydrates were negative. In the sexually mature males, spermatozoa clusters are embedded by the glucoconjugates content of the seminal vesicle lumen. In conclusion, the seminal vesicle of M. quadrifasciata has a secretory function during the pupal stage and in newly emerged males, whereas in adult males this organ stores the spermatozoa..
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Torry, D. S., C. Thaler, W. Page Faulk, and John A. McIntyre. "Seminal vesicles: A source of TLX in seminal plasma." Human Immunology 23, no. 2 (January 1988): 152. http://dx.doi.org/10.1016/0198-8859(88)90276-5.

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28

Sysoeva, A. P., N. P. Makarova, and E. E. Kraevaya. "The role of seminal plasma extracellular vesicles in changes in the morphofunctional characteristics of human spermatozoa." CLINICAL AND EXPERIMENTAL MORPHOLOGY 10, no. 4 (2021): 5–13. http://dx.doi.org/10.31088/cem2021.10.4.5-13.

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For a long time, the role of seminal plasma during human fertilization remained underestimated. Numerous studies related to the development of different methods for human embryo in vitro cultivation were gener-ally concerned with the quality of male and female gametes. However, in recent years, the development of Omix technologies provided a new insight into great seminal plasma influence on the morphofunctional characteristics of spermatozoa. This is especially true for the regulatory function of extracellular vesicles secreted by male reproductive tract cells. In this work, we attempted to analyze current data on the influence of extracellular seminal plasma vesicles on the morphofunctional characteristics of spermatozoa to solve male infertility topical issues. The review includes studies by foreign and Russian research groups that werу conducted within the past 5 years and found in PubMed, Google Scholar, and Cochrane Library databases. Very few studies demonstrate that seminal plasma vesicles act as functional regulators of male fertility and their dysfunction may lead to infertility. The use of seminal plasma extracellular vesicles in clinical practice may significantly increase the success of IVF programs, especially in impaired spermatogenesis. Keywords: extracellular vesicles, exosomes, biomarkers, seminal plasma, spermatozoa, assisted reproductive technology, cell biology, morphology
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DELİKGÖZ SOYKUT, Ela, and Hatice TATAROĞLU. "Dosimetric evaluation of inclusion of proximal seminal vesicle in target volume in low-risk prostate cancer treated with stereotactic body radiotherapy." Anatolian Current Medical Journal 5, no. 3 (July 28, 2023): 253–60. http://dx.doi.org/10.38053/acmj.1320219.

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Aims: Ultra hypofractionation using stereotactic body radiotherapy (SBRT) for low-risk PCa is considered a viable treatment option. The target volume for ultra hypofractionated RT was determined as prostate and/or proximal seminal vesicles; however, there are no clear guidelines on when to add a proximal seminal vesicle to the target volume. We aimed to dosimetrically assess the effect of inclusion of the proximal seminal vesicle in the planning target volume (PTV) on the dose distribution of organ at risk (OAR) when SBRT is administered to patients with low-risk PCa. Methods: Low-risk PCa cases who underwent SBRT with CyberKnife were retrospectively screened, and 20 random cases were included. The contours of OARs and target volumes were checked as recommended in international contouring atlases by the same radiation oncologist. Two treatment plans by determining two different PTV (prostate alone in plan 1 and prostate with proximal seminal vesicles in plan 2) were made by the same specialist physicist. 5×7.25 Gy was chosen as the dose schedule defined for both plans. Results: Regarding coverage, homogeneity index, and new conformity index (nCI), there was no significant difference between the two plans (p=0.397, p=0.452, p=0.225). The plan 2 had a greater PTV Dmax (p
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30

Deshmukh, C. K. I. "341. STUDY OF APHRODISIAC DRUG ACID PHOS ON MALE ALBINO RAT." Reproduction, Fertility and Development 22, no. 9 (2010): 141. http://dx.doi.org/10.1071/srb10abs341.

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The male albino rat, Rattus norvegicus maintained in the laboratory by supplying regularly food and water. Acid phos is a well known aphrodisiac drug from homeopathy medical system. Doses of 200 gm of 30 number globules made from sugar of milk and moistened by 15 mL of acid phos (H3PO3) of 6 potency. Group-I, II and III experimental rats were carried out for 15, 30, and 15 day recovery period respectively. Appreciable behavioral changes and changes in the body weights were noticed. In 15, 30 and in 15 days of recovery period, the acid phosphatase, SGOT and albumin were significant (P < 0.05) while alkaline phosphatase, SGPT, cholesterol, glucose, total proteins and globulin was found non-significant but A:G ratio was increasedsignificantly in 30 days of treatment. The weight of liver, kidney, and testis has found linear increased relationship with the body weight but significant (P < 0.050) increased in the weight of seminal vesicle and body weight in the experimental rat. Various histo-architectural changes were observed in the tissues of liver, kidney, testis and seminal vesicle. Both liver and kidney showed degenerative changes after 15 and 30 days .Tetraploid stages of liver pernchymal cells were predominant in the experimental rats while in 15 days of recovery period, both attained the recovery. In 30 days, the diameter of seminiferous tubules is markedly reduced, with thin unfolded mucosa. In 15 days of administration of acid phos, the intertubular spaces between the seminiferous tubule were also reduced. The number of spermatids was increased in recovery period, the testis showed the recovery. In 15 days of administration, the secretion in the lumen of seminal vesicles increased related with the structure of the epithelium of seminal vesicles while in 15 days of recovery period, the seminal vesicles showed recovery of secretory activities with pseudostratified epithelium. All the results are discussed detailed in paper.
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31

Gong, Maolei, Fei Wang, Weihua Liu, Ran Chen, Han Wu, Wenjing Zhang, Xiaoqin Yu, et al. "Pattern recognition receptor-mediated innate immune responses in seminal vesicle epithelial cell and their impacts on cellular function†." Biology of Reproduction 101, no. 4 (July 27, 2019): 733–47. http://dx.doi.org/10.1093/biolre/ioz136.

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Abstract The seminal vesicles can be infected by microorganisms, thereby resulting in vesiculitis and impairment in male fertility. Innate immune responses in seminal vesicles cells to microbial infections, which facilitate vesiculitis, have yet to be investigated. The present study aims to elucidate pattern recognition receptor–mediated innate immune responses in seminal vesicles epithelial cells. Various pattern recognition receptors, including Toll-like receptor 3, Toll-like receptor 4, cytosolic ribonucleic acid, and deoxyribonucleic acid sensors, are abundantly expressed in seminal vesicles epithelial cells. These pattern recognition receptors can recognize their respective ligands, thus activating nuclear factor kappa B and interferon regulatory factor 3. The pattern recognition receptor signaling induces expression of pro-inflammatory cytokines, such as tumor necrosis factor alpha (Tnfa) and interleukin 6 (Il6), chemokines monocyte chemoattractant protein-1 (Mcp1) and C–X–C motif chemokine 10 (Cxcl10), and type 1 interferons Ifna and Ifnb. Moreover, pattern recognition receptor-mediated innate immune responses up-regulated the expression of microsomal prostaglandin E synthase and cyclooxygenase 2, but they down-regulated semenogelin-1 expression. These results provide novel insights into the mechanism underlying vesiculitis and its impact on the functions of the seminal vesicles.
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32

Di Stefano, Andrea F. D., Milko M. Radicioni, Francesca Morano, Alessandra Gentili, Elena Mallat, Dario Cuomo, Tonia Mazzarella, and Veronica Di Fonzo. "Fosfomycin Pharmacokinetic Profile in Plasma and Urine and Quantitative Estimation in Prostate and Seminal Vesicles after One and Two Consecutive Doses of Oral Fosfomycin Trometamol in Healthy Male Volunteers." Antibiotics 11, no. 11 (October 22, 2022): 1458. http://dx.doi.org/10.3390/antibiotics11111458.

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The present Phase I study investigated, for the first time, fosfomycin pharmacokinetics in humans after two 3 g doses of fosfomycin trometamol administered 27 h apart, according to the dose regimen recommended for the prophylactic indication for transrectal prostate biopsy in adult men. Plasma, urine and seminal plasma concentrations were measured after one and two consecutive doses in 24 healthy men, representative of the target population of the prophylactic indication. Prostate and seminal vesicle concentrations were estimated based on seminal plasma concentrations using a one-step regression method. The exposure to fosfomycin was very similar in rate (Cmax, tmax) after one and two doses. The AUC showed a minimal increment. On average, the apparent volume of distribution was high (>100 L), and the mean clearance had an intermediate value. The total amount and dose fraction of fosfomycin excreted in urine showed a small increment after two doses. The renal clearance was about 5 L/h. The fosfomycin concentration in the prostate and seminal vesicles showed that the antibiotic increased on average after two consecutive doses. This result confirmed the ability of fosfomycin to distribute into the prostate and into seminal vesicles after one single dose and that a two consecutive dose regimen increases the antibiotic availability inside these peripheral tissues.
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33

Gur, FM, and S. Timurkaan. "Androgen receptor distribution in the rat prostate gland and seminal vesicles." Veterinární Medicína 61, No. 3 (July 15, 2016): 148–54. http://dx.doi.org/10.17221/8766-vetmed.

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34

Gonzales, Gustavo F., Graciela Kortebani, and Alicia B. Mazzolli. "Leukocytospermia and function of the seminal vesicles on seminal quality." Fertility and Sterility 57, no. 5 (May 1992): 1058–65. http://dx.doi.org/10.1016/s0015-0282(16)55025-0.

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35

Cunha, G. R., P. Young, S. J. Higgins, and P. S. Cooke. "Neonatal seminal vesicle mesenchyme induces a new morphological and functional phenotype in the epithelia of adult ureter and ductus deferens." Development 111, no. 1 (January 1, 1991): 145–58. http://dx.doi.org/10.1242/dev.111.1.145.

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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.
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36

KISE, HIDEAKI, JUNJI NISHIOKA, KENJI SATOH, TOSHIYUKI OKUNO, JUICHI KAWAMURA, and KOJI SUZUKI. "Measurement of Protein C Inhibitor in Seminal Plasma Is Useful for Detecting Agenesis of Seminal Vesicles or the Vas Deferens." Journal of Andrology 21, no. 2 (March 4, 2000): 207–12. http://dx.doi.org/10.1002/j.1939-4640.2000.tb02097.x.

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ABSTRACT: Protein C inhibitor (PCI), a plasma serine protease inhibitor of activated protein C, is present at high concentrations in the seminal plasma of normal subjects and is decreased in some infertile patients. We measured the concentrations of PCI, prostate‐specific antigen, and fructose in the seminal plasma of infertile patients (n = 125) and of normal subjects (n = 13). We also measured time‐dependent changes in the concentrations of PCI and fructose in seminal plasma after ejaculation. A weak correlation was found between the levels of PCI and fructose (r =0.268, P = 0.016). The PCI level in seminal plasma of patients with seminal vesicle and/or vasal agenesis was significantly lower (P < .01) than in normal subjects. The level of fructose in seminal plasma decreased in vitro in a time‐dependent manner after ejaculation, whereas the concentration of PCI was stable at 48 hours after ejaculation. These data suggest that PCI in seminal plasma, as well as fructose, may become one of the markers for agenesis of seminal vesicles and/or the vas deferens.
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37

Goyal, Shikha, Renu Madan, Urmi Mukherjee, and Rajender Kumar. "Solitary fibrous tumor of the seminal vesicle." Journal of Cancer Research and Therapeutics 19, no. 5 (2023): 1412–14. http://dx.doi.org/10.4103/jcrt.jcrt_525_22.

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ABSTRACT Solitary fibrous tumors (SFTs) are mesenchymal neoplasms with variable clinical behavior depending on age, tumor site, and size, and pathologic factors such as mitoses and necrosis. Imaging features on computed tomography (CT) or magnetic resonance imaging (MRI) are not specific, and the diagnosis relies on histopathology with immunohistochemistry. SFTs arising from seminal vesicles is rare and reported in only eight earlier cases. We discuss the clinical, histopathologic and positron emission tomography (PET) imaging characteristics of a 54-year-old patient with SFT of the seminal vesicle. The patient was treated with robot-assisted seminal vesiculotomy and is doing well on follow-up at two years.
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38

Secaf, E., R. N. Nuruddin, H. Hricak, R. D. McClure, and B. Demas. "MR imaging of the seminal vesicles." American Journal of Roentgenology 156, no. 5 (May 1991): 989–94. http://dx.doi.org/10.2214/ajr.156.5.2017966.

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39

Khmara, T. V., M. O. Ryznychuk, T. B. Sykyrytska, V. D. Moisiuk, Ya P. Stefak, and P. O. Fedirchyk. "Fetal Microscopic Anatomy of Seminal Vesicles." Ukraïnsʹkij žurnal medicini, bìologìï ta sportu 3, no. 1 (January 15, 2018): 76–79. http://dx.doi.org/10.26693/jmbs03.01.076.

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40

Lna, J. M., and J. G. Let. "NONINVASIVE IMAGING OF THE SEMINAL VESICLES." INVESTIGATIVE RADIOLOGY 28, no. 12 (December 1993): 1213. http://dx.doi.org/10.1097/00004424-199312000-00152.

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41

SMITH, GAIL, CESAR ERCOLE, JOHN C. HULBERT, WILFRIDO R. CASTAÑEDA-ZUÑIGA, and JANIS GISSEL LETOURNEAU. "Transrectal Sonography and the Seminal Vesicles." Journal of Endourology 3, no. 2 (January 1989): 219–25. http://dx.doi.org/10.1089/end.1989.3.219.

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42

Castiñerias Fernández, J., C. González Cáliz, J. L. Moyano Calvo, and E. Sánchez Sánchez. "Prostate and seminal vesicles sparing cystectomy." European Urology Supplements 18, no. 11 (November 2019): e3601. http://dx.doi.org/10.1016/s1569-9056(19)34724-4.

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43

Kavoussi, Louis R., William W. Schuessler, Thierry G. Vancaillie, and Ralph V. Clayman. "Laparoscopic Approach to the Seminal Vesicles." Journal of Urology 150, no. 2 Part 1 (August 1993): 417–19. http://dx.doi.org/10.1016/s0022-5347(17)35498-8.

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44

THIEL, RALF, and PETER EFFERT. "Primary Adenocarcinoma of the Seminal Vesicles." Journal of Urology 168, no. 5 (November 2002): 1891–96. http://dx.doi.org/10.1016/s0022-5347(05)64260-7.

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45

Scheit, Karl Heinz, Michael Kemme, Gerhard Aumüller, Jürgen Seitz, Gerd Hagendorff, and Michael Zimmer. "The major protein of bull seminal plasma: Biosynthesis and biological function." Bioscience Reports 8, no. 6 (December 1, 1988): 589–608. http://dx.doi.org/10.1007/bf01117339.

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We isolated the major protein of apparent Mr of 15,000–16,000 from seminal plasma as well as from seminal veiscle secretion of bull and proved by amino acid analysis and tryptic peptide mapping that the two proteins were identical. An antiserum against this major protein was employed to quantitate and identify the major protein in seminal plasma as well as seminal vesicle secretion. The antiserum did not cross-react with proteins from bovine or human plasma or follicular fluid respectively. Cell-free translation of poly(A)RNA from seminal vesicle tissue and immunoprecipitation yielded one major species with apparent Mr of 18,000. Using the anti-major protein antiserum, this major species was specifically immuno absorbed. Cloning and sequencing of a major protein-specific cDNA led to the identification of clone pMP17, encoding a precursor of the major protein of 128 amino acid residues. We proved that the major protein is identical to protein PDC 109 (Esch et al., Biochem. Biophys. Res. Comm.113:861–867, 1983). The seminal vesicles synthesize major protein in an androgen-dependent fashion. In addition to intraluminal secretion of the vas deferens, ampullary spermatozoa revealed an intense immunoreaction which was restricted to the neck region of the sperm head and the middle piece, while the principal piece of the tail as well as the sperm head were devoid of immunoreactive material. Epididymal epithelium (as well as calf seminal vesicle epithelium) showed no immunoreactivity with major protein antiserum. Immunoelectron microscopy demonstrated that only spermatozoa devoid of a plasma membrane around the middle piece were able to bind the antiserum against major protein. After removal of the plasma membrane from epididymal spermatozoa, binding of major protein to subplasmalemmal binding sites was visualised using gold-labeled MP. Transblotting with gold-labeled MP demonstrated a protein of about 66 kDa which appears to represent the major protein-receptor. Binding of major protein to the receptor (after loss of the plasma membrane in the mid-piece region of the spermatozoa after contact with secretions from seminal vesicles) is interpreted as a phyisological process presumably related to the onset of sperm motility.
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46

Lin, Ming-Huei, Robert Kuo-Kuang Lee, Yuh-Ming Hwu, Chung-Hao Lu, Shian-Ling Chu, Ying-Jie Chen, Wei-Chao Chang, and Sheng-Hsiang Li. "SPINKL, a Kazal-type serine protease inhibitor-like protein purified from mouse seminal vesicle fluid, is able to inhibit sperm capacitation." REPRODUCTION 136, no. 5 (November 2008): 559–71. http://dx.doi.org/10.1530/rep-07-0375.

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We report a secreted serine protease inhibitor Kazal-type-like (SPINKL) protein. The SPINKL protein was purified from mouse seminal vesicle secretions through a series of steps, including ion-exchange chromatography on a diethylaminoethyl-Sephacel column, gel filtration on a Sephadex G-75 column, and ion-exchange HPLC on a Q strong anion exchange column. Further analysis identified several SPINKL proteins with various N-linked carbohydrates. The SPINKL protein has six conserved cysteine residues that are nearly identical to those of members of the SPINK protein family. It was noted that the SPINKL protein showed no inhibitory activities against common serine proteases such as trypsin, chymotrypsin, subtilisin, or elastase.SpinklmRNA and SPINKL proteins were found to be primarily expressed in seminal vesicles. Immunohistochemistry revealed that the SPINKL protein occurred in the luminal fluid and mucosal epithelium of the seminal vesicles and was regulated by testosterone. The SPINKL protein was able to bind onto sperm and enhance sperm motility. Also, it was able to suppress BSA-stimulated sperm capacitation and block sperm–oocyte interactionsin vitro, suggesting that SPINKL may be a decapacitation factor.
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47

Garcia, E. M., J. M. Vazquez, I. Parrilla, J. J. Calvete, L. Sanz, E. A. Martinez, J. Roca, and H. Rordríguez-Martínez. "323 EXPRESSION OF PSP-I AND PSP-II IN THE REPRODUCTIVE TRACT OF THE BOAR BY IMMUNOHISTOCHEMISTRY, WESTERN BLOTTING, AND RT-PCR." Reproduction, Fertility and Development 19, no. 1 (2007): 277. http://dx.doi.org/10.1071/rdv19n1ab323.

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In boar seminal plasma, PSP-I and PSP-II form a noncovalent heterodimer, which is known to have a beneficial effect on highly extended boar spermatozoa. These proteins are mainly produced by the seminal vesicles of the male reproductive tract and are mixed with the spermatozoa during ejaculation. This study assessed the epithelial localization and expression of spermadhesin PSP-I and PSP-II subunits using immunohistochemical, western blotting, and RT-PCR methods in porcine testis, epididymis (caput, corpus, and caudal), seminal vesicles, and bulbourethral glands. Tissues were collected from 10 mature boars (Swedish Yorkshire) of proven fertility, frozen or fixed, and embedded in paraffin. Sections of 5 �m were mounted on poly-l-lysine-coated glass slides for immunohistochemistry, and 50 mg from the frozen counterparts were homogenized to isolate proteins (Western blotting study) or RNA (RT-PCR study). Polyclonal antibodies (antiPSP-I and antiPSP-II) against proteins (PSP-I and PSP-II) were used. The immunohistochemistry showed positive labelling for both antibodies in the epithelium of seminal vesicles in all males. Positive immunolabelling, but of variable intensity, was present in the epididymal epithelium (caput, corpus, and caudal), with variation among segments and boars. No labelling was found in the seminiferous epithelium or bulbourethral glands of any boar. After SDS-PAGE and Western blotting, immunoreactive bands were obtained in the extracts of all tissues for both PSP proteins. Among tissues, the highest intensity corresponded to the seminal vesicle lane for both proteins. Epididymis (caput, corpus, and caudal), bulbourethral gland, and testis showed more feeble bands, yet present. The intensity of the bands varied among boars. Amplification products from mRNA were obtained in all tissues explored by RT-PCR, using specific primers for PSP-I and PSP-II. The same trend was obtained regarding intensity bands, corresponding with the intensity obtained by Western blotting. The results indicate that PSP-I and PSP-II are mainly expressed in seminal vesicles and epididymal segments and, in lower amount, in the testis and bulbourethral gland. This work was supported by Formas, Stockholm, and Fundaci�n S�neca, Murcia, Spain.
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48

Joo, Ijin, Seung Hyup Kim, and Jeong Yeon Cho. "A comparison of seminal vesicle size on CT between autosomal dominant polycystic kidney disease (ADPKD) patients and normal subjects." Acta Radiologica 51, no. 5 (June 2010): 569–72. http://dx.doi.org/10.3109/02841851003652583.

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Background: Extrarenal manifestations are common in autosomal dominant polycystic kidney disease (ADPKD). Although seminal vesicles can also be involved in patients with ADPKD, little is known about the size differences of the seminal vesicles between ADPKD patients and normal subjects. Purpose: To determine whether the size of seminal vesicles in ADPKD patients is larger than that in normal subjects with the use of three-dimensional (3D) CT. Material and Methods: Using a retrospective case-control study design, we reviewed the findings of 696 male patients with an age range of 20–69 years who underwent contrast enhanced multi-detector computed tomography (MDCT) imaging of the kidney in our institution from August 2007 to July 2008. A total of 68 male patients with ADPKD comprised the study group. Another 68 age-matched non-ADPKD male patients comprised the control group. The size of bilateral seminal vesicles was assessed by measurement of the short dimension on axial, coronal, and sagittal images by the use of a picture archiving and communication system (PACS). Results: The mean width of seminal vesicles in ADPKD patients was 1.70±0.40 cm (axial images), 1.86±0.45 cm (coronal), and 1.59±0.39 cm (sagittal). For control group subjects, the mean width was 1.53±0.29 cm (axial), 1.68±0.43 cm (coronal), and 1.48±0.31 cm (sagittal). The mean size differences between the ADPKD and control groups for the measured widths on axial and coronal images were statistically significant ( P=0.01 and P=0.02, respectively). The width as measured on axial images showed a decrease with age in the control group subjects (linear trend, P=0.005), but no significant decrease was noted in ADPKD patients. Conclusion: The seminal vesicles were demonstrated to be larger in ADPKD patients as compared with normal subjects as determined with the use of 3D CT.
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Ibraheem, Usama Murad, and Mazin Anwer Yadgar Alobaid. "Imaging characteristics of normal, common and uncommon diseases of seminal vesicles: A review article." Medical Journal of Tikrit University 29, no. 2 (December 31, 2023): 80–90. http://dx.doi.org/10.25130/mjotu.29.1.12.

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Abstract:
Seminal vesicles (SVs) are pair of androgen-dependent accessory glandular structures of the male reproductive system. They play a critical role in male fertility. The main purpose of this review is to illustrate the imaging findings of the normal and the spectrum of seminal vesicles diseases, including congenital anomalies, inflammation, neoplastic , and nonneoplastic diseases.
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Leung, A. Y., P. Y. Wong, J. R. Yankaskas, and R. C. Boucher. "cAMP- but not Ca(2+)-regulated Cl- conductance is lacking in cystic fibrosis mice epididymides and seminal vesicles." American Journal of Physiology-Cell Physiology 271, no. 1 (July 1, 1996): C188—C193. http://dx.doi.org/10.1152/ajpcell.1996.271.1.c188.

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Abstract:
Cystic fibrosis (CF) reflects the loss of adenosine 3',5'-cyclic monophosphate (cAMP)-regulated Cl- secretion consequent to mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene. In humans, but not mice, with CF, the disease is associated with male infertility. The present study investigated the relative magnitudes of the cAMP pathways and an alternative Ca(2+)-regulated Cl- secretory pathway in primary cultures of the epididymides and the seminal vesicles of normal and CF mice. The basal equivalent short-circuit currents (Ieq) of cultures derived from the epididymides and the seminal vesicles from the CF mice were lower (6.0 +/- 0.6 and 4.0 +/- 1.0 muA/cm2, respectively) than those from normal mice (11.1 +/- 1.0 and 6.6 +/- 0.6 muA/cm2, respectively). Forskolin induced significant Ieq responses in both the epididymis (8.0 +/- 0.7 muA/cm2) and seminal vesicles (4.0 +/- 0.5 muA/cm2) from normal mice, whereas forskolin-induced changes in Ieq in CF mouse epididymis and seminal vesicles were absent, consistent with defective cAMP-CFTR-mediated Cl- secretion in CF mice. Ieq responses to agonists (ionomycin, ATP) that raise intracellular Ca2+ (Ca2+i) were larger than forskolin responses in normal animals (6.6 +/- 0.9 and 13.4 +/- 1.8 muA/cm2, respectively) and were preserved in CF (6.5 +/- 0.9 and 17.1 +/- 1.0 muA/cm2, respectively). We speculate that the fertility of male CF mice is maintained by persistent expression of the predominant alternative Ca(2+)-mediated Cl- transport system in the epididymides and seminal vesicles.
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