Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The levels of the immunoglobulins IgA, IgG1, IgG2, and IgM were measured in serum and fluid from various locations in the reproductive tract of normal rams. These fluids included semen, preputial washings, and fluid from the accessory sex glands (ASG), vasa deferens, rete testes, and tissue fluid from the seminal vesicles, bulbourethral glands, epididymal tails and efferent ducts. In addition, the prevalence of specific Ig-containing cells (ICC) was measured in sections of formalin fixed tissues stained by an indirect peroxidase-antiperoxidase labelling technique. Mean IgA levels in semen (1.23 mg/ml) and ASG fluid (0.46 mg/ml), were higher than in serum (0.19 mg/ml) and were at levels higher than IgG1 or IgG2 levels in semen, ASG fluid, and preputial washings, thus confirming the existence of a local immune system primarily in the ASG of ram genitalia. Relatively low concentrations of IgA and IgG in other genital fluids and IgG levels in these fluids were consistent with diffusion from serum. The relatively high prevalence of IgA-containing cells in bulbourethral (56% of all ICC) and prostate (49%) glands confirmed these tissues as major sites of local Ig production. ICC were also found in large numbers beneath pelvic urethral and preputial epithelia, but these were predominantly IgG-containing (88 and 72% respectively).
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PMID:Immunoglobulins and immunoglobulin-containing cells in the reproductive tract of normal rams. 336 70

Experiments were performed to clarify the debate over the entry of circulating proteins into the epididymal lumen by use of the marker horseradish peroxidase (HRP). Epididymal tubules from the caput epididymidis of the rat were immersed in medium TC 199 containing HRP (3.5 mg/ml) for 5 min to 3 h at 33 degrees C. Sections were examined for the presence of tracer within the epithelial cells by electron microscopy. From 5 min to 3 h, vesicles containing peroxidase reaction products were found throughout the cytoplasm of the principal cells. Vesicles occurred close to both the basal and apical membranes, and many were found opening into the interstitial space and lumen, depending on the length of incubation. By 5 min labelled vesicles were infrequently found in the apical part of the cells. Reaction product was observed in the epididymal lumen adhering to the microvilli from 30 min of incubation onwards. At all periods of incubation peroxidase was present at the base of the epithelium and between the cells, but it was never found within the tight junctional complexes, and no reaction deposits were found within epithelial cells of tubules incubated in the absence of peroxidase. It is concluded that large molecules leaving the capillaries may enter the epididymal lumen in the caput by means of fluid-phase endocytosis.
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PMID:Protein transport to the epididymal lumen. 360 48

Efferent reproductive ducts of male mice, including ductuli efferentes, epididymis, and vas deferens, were fixed and embedded in paraffin, and sections were stained with a battery of lectin-horseradish peroxidase conjugates to localize specific sugars or sugar sequences in glycoconjugates. Cilia and the apical surfaces of ciliated cells in the ductuli efferentes stained intensely with lectin specific for sialic acid and terminal alpha-N-acetyl-D-galactosamine. Flask cells and clear cells in the epididymis reacted positively and similarly with most lectins used, providing evidence that these cell types are related. In contrast, disparities in lectin staining suggest that flask cells and clear cells are a cell type distinct from principal cells. Basal cells were not present in the ductuli efferentes but formed a continuous layer in the epididymis and vas deferens. Basal cells contained oligosaccharides terminated by sialic acid and alpha-D-galactose and varying amounts of terminal beta-D-galactose and alpha-N-acetyl-D-galactosamine. Basal cells also stained variably with lectins specific for the core region of complex type N-glycosidic side chains. The basal cells varied structurally, having long spinous apical processes approaching or reaching the lumen in region I of the epididymis and being low cuboidal or squamoid and lacking apical processes in epididymal regions II-V and in the vas deferens. The contiguous nature of the basal cells and the presence of glycoconjugates bearing terminal alpha-galactosyl residues in all basal cells suggest a possible role for these cells in a regulatory influence on transepithelial movement of fluid and/or ions in the epididymis and vas deferens.
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PMID:Histochemical evaluation of glycoconjugates in the male reproductive tract with lectin-horseradish peroxidase conjugates: II. Staining of ciliated cells, basal cells, flask cells, and clear cells in the mouse. 382 61

To investigate the origin and nature of vesicles found within multivesicular bodies (mvb), the cytochemical staining properties of mvb vesicles were compared with those of other cytoplasmic vesicles, i.e. those associated with the Golgi complex and endocytic vesicles found near the apical cell surface. Rat epididymal tissue was stained in unbuffered OsO(4) for 40-48 hr, and the distribution of stain was compared to that of reaction products for acid phosphatase (AcPase) to mark lysosomal vesicles, or thiamine pyrophosphatase (TPPase) to mark certain Golgi vesicles, or infused with peroxidase (HRPase) to demonstrate endocytic vesicles. Mvb vesicles were stained only by OsO(4); AcPase, TPPase, and HRPase reaction products stained the mvb matrix. OsO(4) also stained certain vesicles along the convex surface of the Golgi complex. The findings suggest that mvb vesicles in epididymal epithelium are not lysosomes and are not involved in protein uptake. The majority of these vesicles have cytochemical reactions in common with vesicles located along the convex surface of the Golgi complex and may be derived therefrom. A minority are derived from the mvb-limiting membrane.
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PMID:Cytochemical staining of multivesicular body and golgi vesicles. 418 Mar 53

Modifications in bull sperm plasmamembrane during epididymal passage were investigated by the use of four different lectins: Concanavalin A (Con A); Ricinus communis I (RCA1); Wheat germ agglutinin (WGA); Ulex europaeus agglutinin I (UEA1). During sperm passage from caput to cauda epididymidis agglutination by RCA1 and WGA distinctly increased. Similar but somewhat less pronounced difference in the agglutinability was found for Con A. No agglutination was observed with UEA1. Ultrastructural examination of Con A binding sites on sperm plasma membrane with a Con A-horseradish peroxidase-gold technique (Con A-HRP-G) revealed a significant increase in the number of gold granules on the sperm tails during the epididymal passage of spermatozoa. No change in WGA-binding sites was observed between caput and cauda spermatozoa using a WGA-peroxidase method.
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PMID:Glycoproteins of bovine epididymal spermatozoa--a cytochemical study. 620 49

Orchitis, epididymitis and prostatitis have been reported in male dogs infected with Brucella canis (B. canis), but the pathogenesis of infertility in male dogs has not been clarified yet. We examined localization of B. canis in the tissue of infected male reproductive organs and production of autoantibody to spermatozoa in male dogs by immunofluorescence and unlabeled antibody peroxidase-antiperoxidase (PAP) methods and electron microscopy. B. canis were found in the cytoplasm of macrophages and epithelial cells in testis, epididymis and prostate. Particularly in the prostate, B. canis multiplied in the cytoplasm of epithelial cells and emerged in the glandular lumen with destroyed epithelial cells. Head-to-head agglutination of spermatozoa was found in the semen, urine and epididymal duct with varying degrees of intensity among the infected dogs. Appearance of the spermagglutination began following the detection of B. canis in urine and semen, suggesting invasion of the organisms in male reproductive organs. In the sera from the dogs orally inoculated with B. canis, (Ig M), Ig G and Ig A anti-spermantibodies were detected in parallel with the appearance of the serum spermagglutinating activity. The heads of agglutinated spermatozoa in the epididymal duct and semen were coated with Ig A antibody, which is considered to be anti-spermautoantibody locally produced. The target of these circulating and local antibodies was acrosome of the dog spermatozoa and spermatids. It seems probable that multiplication of B. canis in epithelial cells is the direct cause of damage to the infected cells, and the damage acts as a trigger of the production of autoantibody to spermatozoa.
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PMID:Multiplication of Brucella canis in male reproductive organs and detection of autoantibody to spermatozoa in canine brucellosis. 638 74

Mammalian spermatozoa that leave the testis are neither motile nor fertile. Maturation of spermatozoa occurs during epididymal transport. Among the changes during epididymal passage alterations of the surface properties of spermatozoa appear especially interesting. In this report we describe ultrastructural localization of Con A and WGA-binding sites on bovine spermatozoa from caput and cauda epididymides using a indirect lectin-horse-radish-peroxidase gold technique. With Con A the plasma-membrane covering the sperm head was heavily labelled with gold granules in caput as well as in cauda epididymal spermatozoa. A different distribution was observed for WGA-binding sites. The acrosomal region of caput and cauda spermatozoa was heavily labelled with gold, both in caput and cauda spermatozoa. The postacrosomal region was only sparsely marked in caput sperm whereas in sperm cells originating from the cauda a calix like membrane area displayed intense labelling. Some differences in the number of binding sites were also seen on sperm tails: those of caput spermatozoa show generally more Con A binding sites that those from cauda epididymal spermatozoa. No changes in the number of WGA-binding sites on sperm tails was observed during epididymal passage. The technical aspects of the indirect lectin-horse-radish-peroxidase gold technique are briefly discussed.
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PMID:Localization of lectin receptors on bovine epididymal spermatozoa using a colloidal gold technique. 665 99

The localization of androgen-binding protein (ABP) in the reproductive tract of young adult male rats was studied with the peroxidase-antiperoxidase technique using frozen sections and light microscopy. Within the seminiferous tubules, a positive reaction was noted in the apical portion of the epithelium, apparently in spermatids and/or Sertoli cells. ABP was localized in granules in the apical cytoplasm of the principal epithelial cells of the proximal part of the caput epididymis and in the epithelial cells of the ductuli efferentes. The cells in the distal part of the caput as well as the corpus and cauda of the epididymis did not contain ABP. Numerous coated vesicles and multivesicular bodies were present in the supranuclear cytoplasm of the epididymal epithelium where ABP was taken up. The results indicate that ABP is taken up from the lumen by epithelial cells of the ductuli efferentes and proximal part of the caput epididymis.
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PMID:Immunocytochemical localization of androgen-binding protein in the male rat reproductive tract. 700 29

An improved method is presented for processing single cells for electron microscopy. Agarose, which has a low (30 degrees C) gelling temperature, was used as an initial embedding medium for single cells (spermatozoa and oocytes) and dissociated cell preparations (luteal cells and spleen cells). Dispersed cells of corpus luteum, spleen, and epididymal spermatozoa were placed in 1.5% agarose after aldehyde fixation. These fixed cells, embedded in agarose, were packed into a dense pellet by centrifugation, postfixed, then embedded in Epon. Mammalian eggs were not centrifuged; instead, they were embedded in agarose discs. Cells embedded in agarose were cooled below 30 degrees C to allow for gelling, then processed for electron microscopy. Because agarose has a low gelling temperature, some heat-labile substances were preserved, as demonstrated by retention of peroxidase activity using the DAB histochemical method. The agarose embedding procedure is both rapid and facile, and has proven to be of value in the handling of fragile single cells for electron microscopic studies.
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PMID:An improved method for processing single cells for electron microscopy utilizing agarose. 703 63

Soluble antigens, specific for mouse testis, were detected by immunoelectrophoresis using a rabbit antiserum against a testicular extract (TE; supernatant of a mouse testicular homogenate spun at 105,000 g for 2 hr). At least 18 archs of precipitation were defined for the adult TE, but only three were testis specific. They were found in the epididymal extract, thus suggesting that these may be spermatozoal antigens. In immature mice, the testis-specific antigens start to appear in coincidence with the onset of pachytene spermatocytes. Immunohistochemical observations (peroxidase-antiperoxidase) showed specific reaction over spermatocytes and spermatids. The site of reaction was the surface or the peripheric cytoplasm of these cells.
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PMID:Testicular specific soluble antigens and spermatogenic onset in the mouse. 714 54


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