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1.
The presence of Aquaporins 1 (AQP1) and 9 (AQP9), integral membrane water channels that facilitate rapid passive movement of water and solutes, was immunohistochemically detected in the excurrent ducts collected from sexually mature buffalo bulls of proven fertility during the mating (late autumn–winter) and non‐mating (late spring to the beginning of autumn) seasons. Furthermore, the research was performed also on the epididymal cauda of a senile buffalo bull with inactive testis. Aquaporins 1 and 9 were immunolocalized at distinct levels. In the efferent ducts, AQP1 immunoreactivity was strongly evidenced at the apical surface of the non‐ciliated cells and weakly along the basal membrane of the epithelial cells. The latter reactivity disappeared during the non‐mating season. No AQP1 immunoreactivity was detected in the epithelium of epididymis and vas deferens, whereas AQP1 was expressed in the smooth muscle layer of the vas deferens. Aquaporin 1 was present in the blood vessels and in small nerve bundles all along the genital tract. The supranuclear zone of the epididymal principal cells was AQP9 immunoreactive, limited to the corpus and cauda regions, and vas deferens. The samples collected in the two reproductive seasons showed a weaker AQP9 immunoreactivity during the non‐mating season. A typical AQP9 immunoreactivity was noticed in the old buffalo examined. The tested AQP molecules showed a different expression pattern in comparison with laboratory mammals, primates, equine, dog and cat. In addition, seasonal differences were noticed which are possibly useful in regard to the comprehension of the morphophysiology of reproduction in the bubaline species, which are still a matter of debate.  相似文献   

2.
Aquaporins (AQPs) are channel proteins that facilitate the transepithelial and bidirectional movement of water. AQP9 is an aquaporin that is expressed in the mammalian epididymis. This water transport contributes to epididymal sperm concentration. This study aimed to examine the morphology of epididymal epithelium in piglets and boars, as well as the expression and immunolocalization of AQP9. The piglets presented an epididymal epithelium in differentiation with principal, basal and apical cells. The cellular population of the epididymal epithelium in boars consisted of principal, basal, apical, clear and narrow cells. The migratory cells known as halo cells were observed in the epididymis of both piglets and boars. AQP9 expression presented differences between piglets and boars. Moderate intensity of AQP9 immunoreaction was observed in the apical border of the epididymal epithelium of the caput and cauda regions in the piglet epididymis. A moderate‐to‐intense reaction for AQP9 was observed in the nuclei of epithelial cells of the three epididymal regions in the boar epididymis. The region of the cauda epididymis showed reactivity for AQP9 also in the apical border of the epithelium. It is believed that the AQP9 is already functional in piglets at only 1 week of age and is more active, playing a pivotal role in the caput and cauda regions of the epididymis. Moreover, the intense AQP9 expression in the apical border of epithelial cells in the cauda region of the boar epididymis suggests a higher performance of AQP9 in this region, where sperm complete their maturation process, stored and concentrated.  相似文献   

3.
Aquaporins (AQPs) are essential membrane protein channels for the transport of water across membranes. Fluid movement in the epididymis is important for modulation of the luminal environment, in which sperm mature and reside. This study was designed to understand the morphology and localization of AQPs in ram efferent ducts (ED) and epididymis. For this purpose, the epididymis of seven animals were removed for histologic and immunohistochemical analyses. AQP1 immunoreactivity was observed in the apex of the ED, and AQP9 was found adjacent to the nuclei of the epithelial cells of the ED. The epithelial lining of ram epididymis is pseudostratified columnar and presents principal, basal, apical and narrow cells. In the initial segment (IS), a moderate reaction for AQP1 was observed in the apical cytoplasm of epithelial cells. An intense reactivity for AQP1 was noted over the microvilli of principal cells and in spermatozoa in the caput. In the corpus and cauda, AQP1 was noted only over the endothelial cells of vascular channels located in intertubular spaces. A weak‐to‐moderate reaction for AQP9 was observed in the nuclei of epithelial cells in the IS, caput and corpus of the epididymis. In the cauda, an intense reaction to AQP9 was observed in the epithelial border. In the IS, caput and corpus, the reactivity for AQP9 differed from those observed in domestic animals. The cauda showed a pattern similar to that previously described. These results indicate that AQPs 1 and 9 have reversed locations and roles in rams, suggesting activity variations related with fluid and solute absorption throughout the epididymis.  相似文献   

4.
The expression of six different aquaporins (AQP1, 2, 3, 4, 5 and 9), integral membrane water channels that facilitate bi‐directional passive movement of water, was investigated by immunohistochemistry in the uterine tube of pre‐pubertal and adult Saanen goats (Capra hircus), comparing the different phases of the oestrous cycle. Regional morphology and secretory processes were markedly different during the goat oestrous cycle. The tested AQP molecules showed different expression patterns in comparison with already studied species. AQP1‐immunoreactivity was evidenced at the endothelium of blood vessels and in nerve fibres, regardless of the tubal tract and cycle period. AQP4‐immunoreactivity was shown on the lateral plasmalemma in the basal third of the epithelial cells at infundibulum and ampulla level in the cycling goats, more evidently during follicular than during luteal phase. No AQP4‐immunoreactivity was noticed at the level of the isthmus region, regardless of the cycle phase. AQP5‐immunoreactivity, localized at the apical surface of epithelial cells, increased from pre‐puberty to adulthood. Thereafter, AQP5‐immunoreactivity was prominent during the follicular phase, when it strongly decorated the apical plasmalemma of all epithelial cells at ampullary level. During luteal phase, immunoreactivity was discontinuous, being weak to strong at the apex of the secretory cells protruding into the lumen. In the isthmus region, the strongest AQP5‐immunoreactivity was seen during follicular phase, with a clear localization in the apical plasmalemma of all the epithelial cells and also on the lateral plasmalemma. AQP2, 3 and 9 were undetectable all along the goat uterine tube. Likely, a collaboration of different AQP molecules sustains the fluid production in the goat uterine tube. AQP1‐mediated transudation from the blood capillaries, together with permeation of the epithelium by AQP4 in the basal rim of the epithelial cells and final intervening of apical AQP5, could be involved in fluid production as well as in secretory processes.  相似文献   

5.
Water transport across epithelial cells that line the airways and alveoli is a crucial component of lung physiology. Aquaporins (AQPs) facilitate water transport across the air space–capillary barrier in the distal lung. However, the roles of lung AQPs in desert animal adaptation to dry airstream environments are still unclear. A hare (Lepus yarkandensis) only lives in the Tarim Basin, and its living environment is an arid climate with rare precipitation. We studied cellular localization and expression levels of AQP1, AQP3, AQP4 and AQP5 in L. yarkandensis lungs by immunohistochemistry, quantitative real-time polymerase chain reaction and Western blot. The lung of rabbits (Oryctolagus cuniculus) that inhabit in mesic environment was similarly studied. Obtained results in two species of animals were compared to investigate whether AQPs in the lung altered expression in the animal living in arid region. AQP1 was localized to the endothelial cells in capillaries and venules surrounding terminal bronchioles and alveoli. AQP5 was localized to the ciliated columnar cells in terminal bronchioles and the alveolar type I cells in the alveolus. Quantitative real-time PCR analysis showed higher AQP1 and AQP5 mRNA levels in L. yarkandensis compared to O. cuniculus. Similar results were obtained by Western blot. These results revealed that the higher expression levels of AQP1 and AQP5 played a significant role in water transport in the lungs of arid-desert living L. yarkandensis and might accelerate water transport from capillary compartments to the airspace.  相似文献   

6.
In this study, elimination of the element zinc from spermatozoa during epididymal maturation was investigated. Testes and epididymides from 40 bulls were collected; epididymal fluid was flushed, pooled, labelled with 0.5 MBq 65Zn2+ per sample and proteins were separated on a Sephacryl S‐200 HR and zinc chelate column chromatography. To follow the resorption of zinc in the epididymal epithelial lining, an autometallographic technique (AMG) was performed in tissue from caput, corpus, cauda and vas deferens. The results showed a zinc‐binding protein fraction with an apparent molecular weight of 150–160 kDa, which was enriched after chelate column chromatography. Specific labelling of 65Zn was about five times higher in the caput than in the cauda epididymidis. AMG revealed no detectable zinc in the caput, but a significant increase of zinc resorption from the corpus to the cauda and vas deferens. Controls showed that the detectable zinc was located within the principal cells. In conclusion, our study proves that zinc present in the sperm flagellum starts to be mobilized in the caput epididymidis and is resorbed by the epididymal epithelium as from the corpus. This zinc elimination is a mandatory step in sperm maturation to obtain motility.  相似文献   

7.
Freezing of boar spermatozoa includes the cryoprotectant glycerol, but renders low cryosurvival, owing to major changes in osmolarity during freezing/thawing. We hypothesize that aquaporins (AQPs) 7 and 9 adapt their membrane domain location to these osmotic challenges, thus maintaining sperm homeostasis. Western blotting (WB) and immunocytochemistry (ICC) at light and electron microscope levels with several commercial primary antibodies and protocols explored AQP location on cauda epididymal and ejaculated spermatozoa (from different fractions of the ejaculate), unprocessed, extended, chilled and frozen‐thawed. Although differences in WB and ICC labelling were seen among antibodies, AQP‐7 was conspicuously located in the entire tail and cytoplasmic droplet in caudal spermatozoa, being restricted to the mid‐piece and principal piece domains in ejaculated spermatozoa. AQP‐9 was mainly localized in the sperm head in both caudal and ejaculated spermatozoa. While unaffected by chilling (+5°C), freezing and thawing of ejaculated spermatozoa clearly relocated the head labelling of AQP‐7, but not that of AQP‐9. In vitro mimicking of cell membrane expansion during quick thawing maintained the localization of AQP‐9 but relocated AQP‐7 towards the acrosome. AQP‐7, but not AQP‐9, appears as a relevant marker for non‐empirical studies of sperm handling.  相似文献   

8.
Aquaporins (AQPs) are members of a large family of integral membrane proteins involved in the rapid movement of water and neutral solutes across cell membranes. In this study, we have prepared an affinity-purified porcine-specific polyclonal antiserum to AQP9 and have investigated the distribution and expression of AQP9 in pig liver tissue and in hepatocytes in primary culture. Immunocytochemical analysis showed that AQP9 was primarily localized in the membrane structures of hepatocytes and was not associated with intrahepatic bile ducts or blood vessels. Western blot analysis indicated that AQP9 ranged in apparent molecular mass between 27 and 38 kD in whole liver and hepatocyte membrane fractions; minor components were also observed at approximately 34 kD in the cytosol compartment of hepatocytes, bile duct and gall bladder. A prominent immunoreactive band at 44 kD was shown to be an artifact of Western blot analysis. In primary cultures of porcine hepatocytes, glucagon enhanced absolute levels of AQP9 protein, while gene expression was enhanced by T3 and glucagon. Insulin alone had no discernable influence on AQP9 gene expression or its cellular protein levels. These data suggest that AQP9 is a major AQP in porcine hepatic tissue and appears to be primarily responsive to glucagon induction.  相似文献   

9.
The expression of 12 different aquaporin subtypes in equine endometrium was examined at the mRNA and protein level. Endometrial samples were obtained during anoestrus, oestrus, 8, and 14 days after ovulation in non‐pregnant mares, and 14 days after ovulation in pregnant mares. Quantitative PCR revealed a time‐dependent pattern for all aquaporin subtypes examined except for AQP10 and 12. AQP3, 5 and 7 showed highest mRNA abundance 8 days after ovulation, while AQP0 and 2 were most abundant at Day 14 of the cycle in non‐pregnant mares. At 14 days of pregnancy, AQP1, 4, 8, 9 and 11 displayed highest expression levels. Western blot analysis confirmed protein expression of AQP0, 2 and 5. Immunohistochemistry localized protein expression to luminal and glandular epithelial and stromal cells. AQP0 staining intensity was highest in samples obtained on Day 14 of the oestrous cycle. AQP2 immunoreactivity seemed to be stronger in samples collected 14 days after ovulation from non‐pregnant animals, in particular luminal epithelial staining. Samples collected 8 days after ovulation from cyclic animals were characterized by intense AQP5 staining of glandular epithelium, predominantly in the deeper glands. Progesterone treatment of anoestrous mares did not enhance expression of AQPs, indicating that factors other than progesterone are required for the up‐regulation of certain AQP subtypes during dioestrus. In conclusion, it seems that an equine‐specific collaboration of aquaporin subtypes contributes to changes in endometrial fluid content occurring throughout the oestrous cycle and contributes to endometrial receptivity during early pregnancy in the mare.  相似文献   

10.
Contents: The periodic acid-Schiff (PAS) reactive materials of epididymal and ejaculated spermatozoa have been studied in Friesian bulls, buffalo bulls, rams and camels. In the four species, the cytoplasmic droplets displayed strong PAS reaction which did not appear to change markedly during epididymal transit. Only in ram a slight reduction was noted in cauda epididymal and vas deferens spermatozoa. In Friesian bulls, the acrosomes of epididymal spermatozoa exhibited moderate PAS reaction which increased on passage to the vas deferens and after ejaculation. In the buffalo the reaction increased in cauda epididymal and vas deferens spermatozoa but returned again to mderate on ejaculation. In the camel the acrosomes of caput spermatozoa showed strong reaction which was sharply reduced on passage beyond. Meanwhile in rams the acrosomes of spermatozoa obtained from any level of the genital tract exhibited weak PAS reaction. The postnuclear reagions, middle pieces and tails of bull, buffalo, ram and camel spermatozoa showed varying degrees of PAS reaction. The pattern of change during transit of spermatozoa differed from species to another which might be related to the nature of maturational processes. Inhalt: PAS-reaktive Polysaccharide in Saugetierspermien wahrend der Passage durch den Nebenhoden PAS-positive Reaktionen von Nebenhodenspermien und ejakulierten Spermien wurden an Friesian- und Büffelbullen, Schafböcken und Kamelhengsten untersucht. In allen 4 Spezies zeigten die Cytoplasmatröpfchen starke Reaktion, die sich wahrend der Nebenhodenpassage nicht merklich veränderte. Nur beim Schafbock wurde eine geringfügige schwächere Reaktion bei Spermien aus dem Nebenhodenschwanz und dem Vas deferens beobachtet. Bei Friesianbullen zeigte das Akrosom der Nebenhodenspermien eine mittelstarke PAS-Reaktion, die nach Passage durch den Samenleiter und nach der Ejakulation weiter verstarkt war. Beim Büffel war die Reaktion in der Cauda und Vas deferens verstarkt, in ejakulierten Spermien aber wieder schwächer. Beim Kamel war das Akrosom der Caput-Spermien stark positiv, bei der nachfolgenden Passage nahm die Reaktion deutlich ab. Das Akrosom der Schafspermien war in allen Organabschnit-ten nur schwach angefärbt. Bei allen vier untersuchten Spezies zeigten die anderen Spermienbereiche (postnukleare Region, Mittelstück, Schwanz) sehr unterschiedliche Reaktionen. Die Veränderungen während er Nebenhodenpassage waren zwischen den Spezies unterschiedlich und vermutlich abhängzg von Unterschieden in den Reifungsprozessen.  相似文献   

11.
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12.
This study aims to investigate the role of matrix metalloproteinases (MMPs) in determining semen quality and to evaluate the expression and cellular localization of MMP‐2, MMP‐9, tissue inhibitor of metalloproteinase‐1 (TIMP‐1) and TIMP‐2 in the testes, epididymis and ejaculated spermatozoa. Gelatinase activities between normal (n = 21) and abnormal (n = 25) semen samples showed a significant, sixfold increase in proMMP‐2 and MMP‐2 activity in high than low sperm concentration samples (p < 0.001). ProMMP‐9 and MMP‐9 levels were significantly elevated in samples with low sperm counts compared to those with high sperm density (p < 0.001). High levels of proMMP‐2 and MMP‐2 were associated with high sperm motility (≥70%, p < 0.001). Sperm‐rich fraction showed significantly (eight‐fold) higher proMMP‐9 enzymatic activity compared with prostatic fraction. The mRNA expressions of MMP‐2, MMP‐9, TIMP‐1 and TIMP‐2 were confirmed in testicular and epididymal tissues. Immunohistochemical staining illustrated the MMP‐2‐specific strong immunoreactivity in the head of mature spermatids during spermatogenesis, whereas MMP‐9, TIMP‐1 and TIMP‐2 were absent in these cells. Matrix metalloproteinase‐9 immunoreactivity was observed in the spermatocyte and round spermatid, whereas TIMP‐1 was only exhibited in the residual bodies. Immunolabeling of epididymal and ejaculated sperm demonstrated MMP‐2 localization along acrosomal region of sperm, while MMP‐9, TIMP‐1 and TIMP‐2 localization was merely limited to the flagella. In conclusion, spermatozoa initially acquire MMP‐2 during their formation at testicular level, and the presence of this protein persists through the epididymal transit and up to ejaculate. The enzymatic activity of MMP‐2 and MMP‐9 may serve as an alternative biomarker in determining semen quality.  相似文献   

13.
The various ducts of the epididymides of four gallinaceous birds, the turkey (Meleagris gallopavo), domestic fowl (Gallus gallus), guinea-fowl (Numida meleagris) and Japanese quail (Coturnix coturnix japonica) were studied at the scanning and transmission electron microscopy levels. The tissues were fixed either by immersion or vascular perfusion, for comparative purposes. Each duct system, save for a few details, presented similar morphological features in all species. The epithelial surface of the rete testis was regular and each cell bore a single cilium, as well as numerous, or in some parts, very few, short, regular microvilli. Each of the Types I and II non-ciliated cells of the proximal and efferent ducts displayed abundant, moderately long and regular microvilli, and a solitary cilium. The ciliated cells exhibited tufts of cilia. The Type III non-ciliated cell of the connecting and epididymal ducts exhibited a solitary cilium, and numerous microvilli which were intermediate in length between those of the rete testis and those of the efferent ducts. Vascular perfusion of the avian epididymal tissue was the superior method of fixation because it minimised the developments of fixation artefacts. Apocrine secretion did not appear to occur in the epididymis of these birds as the apical blebs of Types I, II and III cells, which have previously been reported, only manifest in this study in inadequately fixed tissues, and were therefore viewed as being artefacts. The present findings suggest that the current terminology, as applied to the avian epididymis, be retained.  相似文献   

14.
The goal of this study was to determine whether in the Japanese quail the male genital tract contains receptors for progesterone, androgen and estrogen (PR, AR and ER, respectively), which have significant roles in reproductive functions, and whether their localization changes during sexual maturation. The epididymis and ductus deferens (middle and ampulla regions) of immature (approximately 30-day-old) and mature male Japanese quail were collected and frozen sections of them were immunostained for PR, AR and ER. The immunoreaction products for AR and PR were found in the nuclei of epithelial cells in the efferent ductules, epididymal duct, and the middle and ampulla regions of the ductus deferens of mature and immature birds. In the mature birds, the epithelial cells of the efferent ductules, epididymal duct, and the middle and ampulla regions of the ductus deferens were positive for ER, although some of the cells in the ductus deferens were negative. The epithelial cells of the ductules in the epididymis stained positive for ER, but the immunoreactions were negligible in the ductus deferens of immature birds. These results suggest that the epididymis and ductus deferens in quail possesses PR, AR and ER receptors. Each receptor is expressed before sexual maturation, although enhancement of ER expression may occur during maturation.  相似文献   

15.
Lectins are glycoproteins of plant and animal origin that have the ability to bind specific carbohydrate residues of cell glycoconjugates, particularly in terminal positions. In this study, the binding of lectins, Dolichos biflorus agglutinin (DBA), soybean agglutinin (SBA), Bandeiraea simplicifolia BS-1 (isolectin B4), Triticum vulgaris (WGA), Arachis hypogaea (PNA), and Ulex europaeus (UEA-I), was studied in the reproductive systems of male thoroughbred horses.DBA was detected in the stereocilia of the caput and corpus epididymis, and in the vas deferens. It was weakly detected in connective tissue of the corpus epididymis. Strong SBA staining was seen in epithelial cells in the testis, stereocilia of the corpus and cauda epididymis, and in the vas deferens. There were intense positive reactions for isolectin B4 in interstitial cells in all tissue and serosa of the vas deferens. PNA staining was seen only in stereocilia in the caput and corpus epididymis, and in the vas deferens. Strong WGA staining was seen throughout the testis, except in Sertoli cells, stereocilia, and connective tissue. UEA-I was detected in secondary spermatids, stereocilia, and epithelial cells of the cauda epididymis. These results show that degenerating cells in the testis, epididymal tubules, and vas deferens have differential affinities for lectins, and suggest that lectins play a role in the reproductive system of the horse. The heterogeneity of the lectin staining pattern in the reproductive tubules of adult horses suggests that the carbohydrate composition of each cell type is region specific.  相似文献   

16.
Oestrogens are involved in regulation of spermatogenesis and sperm maturation and are essential for male fertility. To study the role of oestrogens on epididymal function in the domestic cat, we analyzed the localization patterns of oestrogen receptors (ERs) within the epididymis of juvenile, pubertal and adults using immunohistochemistry. Cat epididymal tissues obtained during routine castrations were fixed in chilled Bouin's solution and processed for immunohistochemistry with ER-specific antibodies. For a certain receptor type, ER localization was influenced by donor age. In the juvenile epididymis, ERα was localized in the nuclei of epithelial cells of efferent ducts and undifferentiated epithelium of the ductus epididymis. During puberty, ERα localization in the undifferentiated epithelium of the epididymis shifted from the nuclei to the cytoplasm and plasma membrane. Oestrogen receptor-α level was highest in the pubertal and adult epididymis, especially within the cytoplasm and in plasma membranes of caput epithelial cells. This finding was suggestive of a role in fluid reabsorption within the efferent ducts and the epididymis. In corpus and cauda regions, ERα was less abundant, suggesting a minor role for oestrogens in sperm storage areas. Interestingly, localization of ERβ was neither influenced by age nor location within the epididymis and was ubiquitous throughout. Results demonstrate that oestrogen actions within the epididymis may be predominantly mediated through ERα during sexual maturation in the domestic cat.  相似文献   

17.
The volumetric proportion of the various ducts of the epididymis of the emu and ostrich and the immunohistochemistry of actin microfilaments, as well as cytokeratin, desmin and vimentin intermediate filaments, were studied in the various ducts of the epididymis of the emu and ostrich. The volumetric proportions of various ducts, which are remarkably different from those of members of the Galloanserae monophyly, are as follows: the rete testis, 5.2 ± 1.4% for the emu and 2.4 ± 1.8% for the ostrich; efferent ducts, 14.2 ± 2.3% (emu) and 11.8 ± 1.8% (ostrich); epididymal duct unit, 25.8 ± 5.8% (emu) and 26.1 ± 4.1% (ostrich) and connective tissue and its content, 54.7 ± 5.8% (emu) and 60.0 ± 4.9% (ostrich). Unlike in mammals and members of the Galloanserae monophyly, only vimentin was immunohistochemically demonstrated in the rete testis epithelium of the emu, and none of the cytoskeletal protein elements in the ostrich rete testis. The epithelium of the efferent ducts of the emu co-expressed actin, cytokeratin and desmin in the non-ciliated type I cells, and vimentin in the ciliated cell component. The ostrich demonstrated only cytokeratin in this epithelium. The ratite epididymal duct unit is different from that of mammals in lacking actin (only weaky expression in the ostrich), desmin and cytokeratin, and a moderate/strong immunoexpression of vimentin in the basal cells and basal parts of the NC type III cell in the epididymal duct unit. Immunoexpression of the microfilaments and intermediate filaments varied between the two ratite birds, as has been demonstrated previously in birds of the Galloanserae monophyly, and in mammals.  相似文献   

18.
To elucidate synthesis, processing, and subcellular localization of mouse ADAM3 (cyritestin) during spermatogenesis and epididymal sperm transport, we carried out immunoblotting and immunohistochemical analysis of testicular germ cells, and epididymal and vas deferens sperm, using affinity-purified anti-ADAM3 antibody. ADAM3 was initially synthesized as a 110-kDa precursor in round spermatids, and the precursor was then processed into a 42-kDa mature protein during the sperm transport into and/or once in the epididymis. The mature ADAM3 was localized on the anterior part of capacitated sperm heads and was rapidly removed from the head region during the calcium ionophore A23187-induced acrosome reaction. These results demonstrate that the mature form of ADAM3 is involved in the binding of sperm to the egg zona pellucida, not in the membrane fusion between sperm and egg.  相似文献   

19.
In this study, the epididymal region of the Sudani duck was investigated using histological and lectin histochemical methods. Morphologically, the epididymal region of the Sudani duck is composed of extratesticular rete testis, proximal and distal efferent ductules, a short connecting duct, and epididymal ducts. Morphometric analysis of the epididymal region of Sudani duck revealed that the efferent ductules predominate in relation to the epididymal ducts. The distribution of sugar moieties within the epididymal region of the Sudani duck was investigated using ten different fluorescein isothiocyanate (FITC) conjugated lectins. In the rete testis epithelium, only PHA-L showed a positive reaction. Efferent ductules in contrary exhibited a wide range of lectin affinity whereas six positive lectins (Con A, LCA, PNA, WGA, PHA-L, PHA-E) were observed. In the connecting and epididymal ducts, four lectins (Con A, WGA, PHA-L, PHA-E) were also detected. GSA-I, UEA-I, and LTA were at all not evident in the epididymal region of the Sudani duck. In conclusion, the correlation between the large areas of the epididymal region occupied by the efferent ductules and the wide range of sugar affinity of this portion may confirm the speculation that efferent ductules might be the primary site of fluid reabsorption in the epididymal region of Sudani duck.  相似文献   

20.
Aquaporins (AQPs), a family of small membrane-spanning proteins, are involved in fluid transport, cell signalling and reproduction. Regulating AQP8 expression influences apoptosis of granulosa cells (GCs), ovarian folliculogenesis, oogenesis and early embryonic development in mice, but its role has never been investigated in other species. The aim of the present study was to characterize the AQP8 function in buffalo follicular development. The expression pattern of AQP8 in buffalo follicle was analysed by immunohistochemistry method. 17β-Estradiol (E2) or oestrogen receptor antagonist ICI182780 was used to treat GCs cultured in vitro, and the expression of AQP8 was detected using qRT-PCR. Its roles in apoptosis of buffalo GCs were investigated by shRNA technology. AQP8 was found to be expressed higher in secondary follicles (p < .05), and its mRNA level in GCs was upregulated by E2 via receptor-mediated mechanism in a dose-dependent manner. A 732-bp buffalo AQP8 coding region was obtained, which was highly conserved at the amino acid level among different species. AQP8-shRNA2 had more effective inhibition on target gene than AQP8-shRNA1 (66.49% vs. 58.31%) (p < .05). Knockdown of AQP8 induced GCs arrested at G2/M stage and occurred apoptosis. Compared with the control group, higher Caspase9 expression were observed in AQP8-shRNA2 lentivirus infected GCs (p < .05), while Bcl-2 and Bax expression levels had no obvious change (p > .05). Altogether, the above results indicate that AQP8 is involved in oestrogen-mediated regulation of buffalo follicular development by regulating cell cycle progression and apoptosis of GCs.  相似文献   

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