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Little is known about morphological changes in the epididymis in relation to the natural photoperiod or their influence on sperm maturation. The viscacha is a seasonal rodent living in the Southern Hemisphere. The adult males exhibit an annual reproductive cycle with periods of maximum gonadal activity and gonadal regression. In this work, we studied seasonal variations in the morphology and cellular population of the epididymis during both periods, and we compared these results with those recorded at the testicular level. Epididymides were removed and studied by light microscopy. Measurements of luminal diameter, epithelial height, thickness of the lamina propria, and relative cellular distribution were performed. Analysis of variance (ANOVA) or nonparametric ANOVA was used to compare the results. Striking quantitative and qualitative changes were observed. Epididymides in periods of gonadal regression showed a significant decrease in luminal diameter and epithelial height in cauda, while the thickness of the lamina propria increased. In the epididymal corpus, the number of clear cells increased, and the cytoplasm of principal cells showed numerous giant vacuoles. During the active period, the number of halo cells increased and the cytoplasm of these cells was filled with dense bodies. In conclusion, the epididymis of the viscacha exhibits important seasonal morphological changes throughout annual reproductive cycle. The epididymal corpus and cauda segments appeared to be the segments most sensitive to seasonal cyclical variations of the external environment. We therefore postulate that the epididymal morphology of the viscacha probably could be regulated by the natural photoperiod.
Anat Rec A Discov Mol Cell Evol Biol 2005 Jan
PMID:Epididymis of viscacha (Lagostomus maximus maximus): morphological changes during the annual reproductive cycle. 1562 16

Nine groups of four 18- to 24-month-old rams were inoculated with Actinobacillus seminis by the following routes: intraconjunctival, intranasal, oral, intravenous, intramuscular, intraepididymal, vas deferens, intraurethral or intrapreputial. Eight similar rams were left uninoculated as controls. Systemic clinical signs were minimal and were confined primarily to the inoculation sites and the scrotal contents. Mild to severe epididymitis resulted from all the routes of inoculation except intraconjunctival and intranasal. Direct inoculation into the genital tract, especially into the cauda epididymis, was more effective. Intrapreputial and intraurethral inoculation led to ascending urethral infection, and inoculation into the vas deferens resulted primarily in descending infection of the accessory sex glands. A seminis was isolated from 11 of the 36 test rams (30.6 per cent); 26 of the 36 rams, some from each of the test groups except those inoculated intravenously, reacted serologically.
Vet Rec 2005 Jul 30
PMID:Experimental transmission of Actinobacillus seminis infection to rams. 1605 62

Basigin (Bsg) is a transmembrane protein that is responsible for targeting of monocarboxylate transporters (MCTs) to the cell membrane. The present study was conducted to determine whether or not Bsg was required for the proper localization of MCT isoform 1 (MCT1) in a wide range of tissues in adult male mice. The tissue distributions of Bsg and MCT1 in wild-type (WT) mice, the tissue distribution of MCT1 in Bsg gene knockout (Bsg-KO) mice, and the protein and mRNA levels of MCT1 in both genotypes were studied. Immunohistochemistry demonstrated that Bsg colocalized with MCT1 in the cerebrum, retina, skeletal and cardiac muscle, duodenal epithelium, hepatic sinusoid, proximal uriniferous tubules, Leydig cells, and efferent ductule epithelium in WT mice. Bsg was absent but MCT1 was present in Sertoli cells, cauda epididymis, myoepithelial cells and duct of the mandibular gland, surface epithelium of the stomach and bronchioles. In Bsg-KO mice, with the exception of Leydig cells, MCT1 immunostaining was greatly reduced in intensity and its distribution was altered in tissues that expressed both Bsg and MCT1 in WT mice. Levels of the protein and mRNA for MCT1 in these tissues did not change significantly in Bsg-KO mice. On the other hand, immunostaining patterns in cells in which Bsg was absent but MCT1 was present in WT mice remained unchanged in Bsg-KO mice. These observations suggest that Bsg is required for the proper localization of MCT1 in a wide range of cells but not in every cell type.
Anat Rec A Discov Mol Cell Evol Biol 2006 May
PMID:Tissue distribution of basigin and monocarboxylate transporter 1 in the adult male mouse: a study using the wild-type and basigin gene knockout mice. 1661 30

Spermatogenesis and spermatocytogenesis in 16 species of viviparous clinid fishes (Clinidae, Blennioidei) from various localities were followed for the first time by means of light and electron microscopy. The testes of the studied species are of the lobular type, with germinal stem cells situated at the apical ends of the lobules and a vas efferens along the internal margin. Maturation of the spermatides takes place in spermatocysts formed by Sertoli cells around the B-spermatogonia. The gradual condensation and relocation of the chromosomes along the nuclei membranes are highly prominent in this process, which can be divided into several stages. Anisodiametric and slightly flattened sperm heads are eventually formed, 0.4-0.5 microm in diameter and 7.5 +/- 1 microm long, bearing 80 +/- 15 microm long flagella. The sperms are packed into spermatozeugmata within the spermatocysts, enveloped and penetrated by the mucotic material of the Sertoli cells. With division of the germ cells and maturation of the spermatids, the spermatocyst dimensions increase, attaining 40 +/- 8 microm in diameter in the smaller species of Heteroclinus, and up to 90 +/- 10 microm in the larger males of Clinus superciliosus and C. cottoides. Accordingly, the volume of the maturing spermatocysts attains ca. 1,300 +/- 100 microm(3) in the smaller species, and ca. 6,500 +/- 300 microm(3) in the larger ones. As sperm head volume is ca. 2.24 microm(3), the number of sperm in the smallest mature spermatocysts reaches ca. 440 and in the largest over 2,900. Upon release from the cysts, the spermatozeugmata are transported along the sperm ducts to the posterior ampullae where they are stored in the epididymis. During copulation, the sperms are transported from there to the female via the intromittent organ. The sperm formation parameters and their structure and numbers are discussed.
Anat Rec (Hoboken) 2007 Mar
PMID:Comparative spermatogenesis, spermatocytogenesis, and spermatozeugmata formation in males of viviparous species of clinid fishes (Teleostei: Clinidae, Blennioidei). 1752 46

In many mammals, sperm associations had been observed, but not in the mouse. In this work, mouse sperm rosettes are morphologically described inside the epididymis and during its dissolution in a culture medium. Also characterized are the saccharides present in the linking material. Sperm association and other epididymal actions are supported by sperm during epididymal transit and are verified at the caudal region, suggesting a relation between epididymal transit and sperm maturation. In drops of epididymal content obtained from distal (cauda), but not from proximal (caput and corpus) regions; dissolved in culture medium, rosettes appear to be 10 to 15 motile sperm joined by their heads. After 3 min, sperm progressively detach, disassembling the rosette. These structures are studied by several techniques, including optic, electronic (scanning electron microscopy and transmission electron microscopy), and video microscopy. At the ultrastructural level, a dense network of electron-dense material was observed between sperm heads, joining them. Based on previous works in rat, several lectins were used to characterize the type of saccharides present in this linking material. To avoid the contact between sperm and epididymal fluid from distal region--that probably exerts an influence on sperm association--a ligature was placed between caput and corpus. This epididymal content isolated from caput did not display any rosettes after 28 days.
Anat Rec (Hoboken) 2007 Jul
PMID:Mouse sperm rosette: assembling during epididymal transit, in vitro disassemble, and oligosaccharide participation in the linkage material. 1754 71

Claudins are integral membrane proteins at tight junctions (TJs) and form TJ strands. In the present study, we found that claudin-7 was localized along the entire lateral membranes of epididymal epithelium, including the apical junctional region throughout the epididymis, but claudin-8 was restricted to the apical junctional region. This finding raises the possibility that aberrant TJ strands may be formed on lateral membranes. Thus, we focused on examining whether TJ strands exist on lateral membranes of epididymal epithelium. Freeze-fracture electron microscopy showed that aberrant TJ strands were observed in only a few principal cells in all segments of the epididymis except for the initial segment, indicating that the occurrence of aberrant strands is very rare. Aberrant TJ strands were smooth and not subdivided into individual particles in the protoplasmic face, and complementary grooves in the extracellular face were almost free of particles. Aberrant TJ strands in the distal caput and corpus epididymis were accompanied by many vesicle-like structures but those in the proximal caput and cauda epididymis were not. These results suggest that most of claudin-7 in lateral membranes may exist in a nonpolymerized form and may play some different roles other than the formation of TJ strands, for example, in the formation of a pool of claudin proteins or in the reinforcement of cell adhesion.
Anat Rec (Hoboken) 2007 Nov
PMID:Claudin-7 expressed on lateral membrane of rat epididymal epithelium does not form aberrant tight junction strands. 1785 15

Aquaporins (AQPs) are small, intrinsic membrane proteins that are present in many cell types involved in fluid transport. AQP9 is a major apical water channel that is expressed throughout the efferent ducts, epididymis, and vas deferens, as well as in other regions of the human and rodent male reproductive tract. The target of this study was to examine the expression of AQP9 in epithelial cells in the adult dog efferent ducts, epididymis, and vas deferens. Samples of dog male reproductive tract comprising fragments of the testis; initial segment, caput, corpus, and cauda of the epididymis; and vas deferens were obtained from eight adult mongrel dogs. Immunohistochemistry and Western blotting procedures were used to show AQP9 localization and distribution. AQP9 expression was not detected either in dog seminiferous tubules or rete testis. However, apical labeling for AQP9 was detected in the different regions of epididymis and vas deferens, with the reaction being less intense in the caput epididymis. Thus, AQP9 is abundantly expressed in dog male reproductive tract, in which it is an important apical pathway for transmembrane flow of water and neutral solutes.
Anat Rec (Hoboken) 2007 Dec
PMID:Aquaporin 9 (AQP9) localization in the adult dog testis excurrent ducts by immunohistochemistry. 1795 52

We have recently shown that Lgr4 knock-out (LGR4KO) male mice are infertile due to a developmental defect of the reproductive tract. Spermatozoa do not reach the epididymis and accumulate at the rete testis and efferent ducts (ED). We have proposed that in LGR4KO, ED might fail to connect resulting in blind-ended tubes that preclude the normal transit of sperm cells. To explore this possibility, we reconstructed the three-dimensional (3D) structure of the organ from serial microphotographs. The resulting model allowed to individualize and follow each ED from the testis up to the epididymis, and to display the spatial distribution of their content. The transit of spermatozoa is indeed blocked in LGR4KO mice but, contrary to the expectation, the ducts connect normally to each other, forming a single tube that flows into the epididymis, as in the wild-type animals. In the KO however, transit of the sperm is abruptly blocked at the same level syncytial-like aggregates appear in the luminal space. The model also allowed calculating, for the first time, morphometric parameters of the mouse ED, such as total volume, surface, radius, and length. These data unambiguously showed that ED in the mutant mouse are dramatically shortened and less convoluted than in the wild-type animal, providing an explanation to the phenotype observed in LGR4KO. Combined with in situ immunodetection or RNA in situ hybridization, 3D reconstruction of serial histological sections will provide an efficient mean to study expression profiles in organs which do not lend themselves to whole-mount studies.
Anat Rec (Hoboken) 2009 Apr
PMID:Three-dimensional reconstruction of efferent ducts in wild-type and Lgr4 knock-out mice. 1930 Dec 69

Recent studies indicated that leptin, a 16 kDa hormone, is a regulatory signal in human and rodent male reproduction. This work was designed to investigate the expression of leptin and its receptor in testes and epididymides from immature and mature pigs. Immunolocalization revealed that leptin and its receptor were confined only in the interstitial compartment of immature testes, whereas both proteins were detected in Leydig cells and within seminiferous tubules of mature gonads. The immunostaining of epididymal tissues showed that leptin was absent in the epithelial cells of immature pigs but it was present in all the three regions of mature epididymides, although with a minor signal in the cauda. Conversely, leptin receptor was observed in all the epithelial cells of both immature and mature epididymides. Western blot analysis of tissue extracts detected a 16 kDa band for leptin and five/six isoforms, ranging from 120 to 40 kDa, for leptin receptor. In conclusion, this work has identified, for the first time, leptin and leptin receptor in the testis and in the epididymis of the pig showing a differential cell-type expression pattern of the two proteins in young and adult animals. Therefore, our findings suggest a possible involvement of leptin in endocrine or autocrine/paracrine control of porcine male reproductive structures.
Anat Rec (Hoboken) 2009 May
PMID:Leptin and its receptor are expressed in the testis and in the epididymis of young and adult pigs. 1930 34

The efferent ducts of the Mediterranean Gecko, Hemidactylus turcicus (Gekkonidae) were investigated using light and electron microscopy. The seminiferous tubules unite into a single rete testis tubule. The rete testis divides into 3-4 ductuli efferentes which all drain into the cranial portion of the ductus epididymis. All efferent ducts are most active during the months of December to August. The rete testis is composed of a simple squamous epithelium with bifurcated nuclei and a labyrinthine network of intercellular canaliculi. Ciliated and nonciliated cells are present, and more than one cilium extends from the scattered ciliated cells. The presence of small clear vesicles and widened intercellular canaliculi suggest that cells of the rete testis are responsible for intake of luminal fluids. The ductuli efferentes are composed of a simple cuboidal epithelium consisting of ciliated and nonciliated cells, and ciliated cells are the dominant cell type. During the inactive season the number of lysosomes increases and the cells become spermiophagic. The ductus epididymis is composed of a tall pseudostratified columnar epithelium with relatively scarce basal cells. No evidence for regionalization was observed. The ductus epididymis is highly secretory during the active season with numerous electron-dense secretory granules, whose glycoprotein products are released by merocrine secretion. Basally, the active epididymis has swollen intercellular canaliculi and enlarged cisternae of rough endoplasmic reticulum. During the inactive season the secretory activity decreases and membranous structures and fibrous material are observed within widened intercellular canaliculi apical to the basal cells.
Anat Rec (Hoboken) 2010 Dec
PMID:Proximal testicular ducts of the Mediterranean gecko (Hemidactylus turcicus). 2108 37


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