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)

Tubules isolated from the initial segment, caput and corpus regions of the rat epididymis were incubated for 4 h in medium containing rat IgG or bovine-serum-albumin (10 mg ml-1) and processed for light microscopy immunocytochemistry using gold-labelled anti-rat IgG and silver staining or peroxidase/anti-peroxidase techniques. Distribution of IgG was confined to the peritubular matrix only, with no detectable uptake into the epithelium or lumen. In tubules incubated with rat IgG coupled to gold particles as tracer and fixed for electron microscopy, the IgG-gold complex failed to penetrate to the base of the epithelium. When IgG-peroxidase conjugates were used, sparse enzyme activity was localized in small basal and apical vesicles and multivesicular bodies of the principal cells. However, this uptake could not be inhibited by the presence of a 30-fold excess of non-labelled IgG, and the same distribution of enzyme activity was also observed when tubules were incubated with a similar activity of horseradish peroxidase alone. These findings indicate that there is no detectable receptor-mediated transport of IgG across the epididymal epithelium, although non-selective transfer could occur via fluid-phase endocytosis.
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PMID:Non-specific uptake of IgG by rat epididymal tubules in vitro. 166 82

The antispermatogenic effects of the multiglycosides of Tripterygium wilfordii (GTW) and monomer T4 isolated from GTW on the testes and epididymal spermatozoa of rats were examined microscopically following silver staining. The dosages of GTW and T4 were 10mg/kg.d and 0.05 mg/kg.d, respectively, fed for 7 weeks via gastric intubation. Different degrees of damage to the testis and epididymal tubes were found in rats treated with GTW. Deformed, round-headed sperms and exfoliated cells (mainly spermatids and occasionally pachytene spermatocytes) were seen in the tubular lumen of the epididymis. Spermatids with deformed acrosomal vesicles were also commonly observed. No significant pathological changes were seen in other internal organs. T4 mainly caused damage to the spermatozoa in the epididymis. Under the dosage of 0.05mg/kg.d the sperm count was almost nil, but no discernible changes in the seminiferous tubules, epididymal epithelia, Leydig cells or Sertoli cells were found. The antifertility potency of T4 was 200 times stronger than that of GTW.
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PMID:[Antispermatogenic effects of multiglycosides of Tripterygium wilfordii and monomer T4 in the testes and epididymal spermatozoa of rats]. 183 14

The surgical procedures and results of microsurgical epididymovasostomy for obstructive azoospermia at the epididymis are reported. These procedures include the separation of a single epididymal tubule, an incision in the side wall, and a side-to-end anastomosis to the mucosa of the vas deferens under microscopic view. The tunica of the epididymis and the muscle layer of the vas are sutured together to support the mucosal anastomosis. Ten patients with epididymal obstruction underwent the side-to-end epididymovasostomy. The group consisted of two with Young's syndrome, one with an epididymal blow-out after vasectomy, one unsuccessful epididymoepididymostomy, 4 after epididymitis and 2 cases of unknown origin. After the operation, sperm appeared in 9 patients, and semen quality was normalized in 4 patients, all of whom impregnated their wives. Microsurgical side-to-end epididymovasostomy is a much easier procedure than Silber's specific tubule method, and results in a high success rate.
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PMID:[Microsurgical side-to-end epididymovasostomy: surgical technique and outcomes]. 189 9

Human sex steroid-binding protein (hSBP) has been purified from late-pregnancy serum and labelled either by iodination (125I) or by photoaffinity with [3H]delta 6-testosterone. Using a micromanipulator, each labelled protein was separately injected into the lumen of epididymal tubules isolated from the head epididymis of the cynomologus monkey (Macaca fascicularis). Tubules were sampled from 3 to 90 min after the injection and processed for electron microscope autoradiography. Localization of the label occurred over the epididymal epithelium whichever tracer was used. The labelling was not randomly distributed over the different cell types constituting the epithelium, since only the 'principal cells' exhibited a silver grain count significantly greater than the background count. In these cells, labelled protein was found over endocytic organelles (coated structures, endosomes, multivesicular bodies and the trans Golgi network) and nuclei (including the nuclear envelope). Quantitative analysis demonstrated the same pattern of cellular and subcellular distribution for each tracer. Pretreatment with excess unlabelled protein significantly reduced the uptake of radioactivity by the principal cells, demonstrating the specificity of this phenomenon. This is the first study to show direct histological evidence for the internalization of hSBP in the primate epididymis, consistent with earlier immunohistochemical or biochemical localization of this protein. It is concluded that head epididymal cells are able to take up labelled hSBP across their apical membrane. The mechanism of internalization seems to involve endocytosis by the principal cells and leads to labelling of the nuclear compartment. This is strikingly similar to the pattern of uptake of rat androgen-binding protein (rABP) by rat epididymal cells previously demonstrated by our group. To what extent the chemical and structural homology between hSBP and rABP can be held responsible for the common cytophysiological behaviour of these sex steroid-binding proteins remains to be determined.
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PMID:Internalization of human sex steroid-binding protein in the monkey epididymis. 212 29

The selective uptake and localization of radioactivity in the fetal male reproductive organs (epididymis, seminal vesicles and prostate) of the guinea-pig (50-60 days of gestation) after in-vivo and in-situ subcutaneous injection of [3H]oestradiol was investigated by autoradiography. In 50-day-old fetuses, the different areas of the epididymis showed selective retention of radioactivity in the nuclei of peritubular and stromal cells surrounding the epididymal duct; no retention was observed in the epididymal epithelium. A similar distribution of silver grains was observed in the 60-day-old fetus. Seminal vesicles and prostate sections from both 50- and 60-day-old fetuses showed concentration and retention of radioactivity only in stromal cells, whereas the epithelium did not exhibit silver grains. In all the tissues studied, the nuclear labelling was abolished after injection of [3H]oestradiol plus a 100-fold excess of non-labelled oestradiol. As the mesenchyme surrounding the epithelia of the epididymis, seminal vesicles and prostate were labelled selectively with [3H]oestradiol, it is suggested that during fetal life of the guinea-pig the mesenchymal stroma of these fetal male reproductive organs may be considered as a target tissue for oestrogen.
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PMID:Autoradiographic localization of [3H]oestradiol in epididymis, seminal vesicles and prostate of the fetal guinea-pig. 234 38

A case of secondary epididymal obstruction caused by vasal obstruction due to bilateral inguinal herniorrhaphy is reported. A 28-year-old patient, who had undergone right inguinal herniorrhaphy at the age of 3 and bilateral inguinal herniorrhaphy at the age of 25, was diagnosed as having obstructive azoospermia because testicular biopsy disclosed normal spermatogenesis. Vasography revealed bilateral vasal obstruction at the level of the inguinal canal. Bilateral microscopic vasovasostomy was performed but postoperative semen analysis showed azoospermia. At the operation only one sperm was found in the left vasal fluid while no sperm was found in the right. Postoperative vasography showed that the left vasovasostomy was accurate while the right vas was reobstructed. Microscopic epididymovasostomy using Silber's specific tubule technique was performed on the left side. The left epididymis was transected at its tail and numerous normal sperms were found in the epididymal fluid. Four months after the second operation, semen analysis showed normal sperm density of 34 x 10(6)/ml.
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PMID:[Obstructive azoospermia treated by epididymovasostomy following vasovasostomy: a case report]. 317 30

Hepatic stimulator substance is a liver growth stimulator derived from the hepatocyte cytosol of weanling or regenerating adult rat livers. The present paper reports the almost 9,000-fold purification of hepatic stimulator substance with an approximately 100,000-fold increase in specific growth stimulator activity. Purification steps included heating at 95 degrees C for 15 min, 40% cold ethanol precipitation, passage over Procion Red HE3B, DEAE cellulose and Sephadex G75 columns and gel filtration and reverse-phase fast protein liquid chromatography techniques. As little as 27 ng per ml of the purest material produced a 2-fold stimulation in the standard HTC cell activity assay. Further studies indicate that hepatic stimulator substance is a highly negatively charged protein and that disulfide bonds or a complex tertiary structure are not essential to its activity. Hepatic stimulator substance is stable over a wide range of pH's and temperatures. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis with silver stain revealed 1 major band at 12,400 daltons and 1 minor band at 17,500 daltons.
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PMID:Purification and physical-chemical characterization of hepatic stimulator substance. 380 88

Luminal fluid samples were collected by micropuncture of the seminiferous tubule, rete testis, and defined levels of the epididymal tubule. After removal of spermatozoa by centrifugation, the supernatant fluids were analyzed by two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) and an ultrasensitive silver staining procedure to define the sequential change in protein composition along the excurrent duct system. Fluid from each segment displayed a characteristic 2-D PAGE map composed of numerous polypeptides. Seminiferous tubule fluid contained a wide array of polypeptides, with most concentrated in the 45 Kd to 90 Kd range, but, in contrast, rete testis fluid lacked most of these polypeptides. The major complex of rete testis fluid comigrated with serum albumin and was present in all distal segments. Other major rete testis components were not noted distally. Fluid from the caput was characterized by new major components of 30 to 37 Kd, 28 to 30 Kd, 24 Kd, and 23 Kd, each of which consisted of multiple spots of apparent isoelectric variants; all except the 30 to 37 Kd complex were present in the fluid from more distal segments. Proceeding distally, there was a temporal appearance of new polypeptides, especially in the molecular weight range below 30 Kd. Two-dimensional PAGE analysis of detergent extracts of washed spermatozoa indicate that a specific subset of these fluid polypeptides are sperm associated.
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PMID:Regional differences in luminal fluid polypeptides of the rat testis and epididymis revealed by two-dimensional gel electrophoresis. 397 17

The secretory process for glycoproteins in principal cells of the mouse caput epididymis was studied by electron microscope radioautography at intervals after exposure to [3H] fucose in vitro. The large Golgi apparatus showed very heavy labeling at the initial interval, followed by a steady decline in percent of grains and relative grain concentrations. Conversely, the epididymal lumen and the apical cell surface began low and increased in radioactivity at the 30-min interval. The extensive sparsely granulated endoplasmic reticulum showed modest increases in percent of grains and relative grain concentrations 30 min after administration of the percursor. Subdivision of the sparsely granulated reticulum into "intermediate" profiles (some ribosomes attached to the membranes) and "smooth" profiles (lacking ribosomes) showed that this increase was due to silver grains assigned to the smooth portions. After the initial interval, high relative grain concentrations were calculated for vesicles. The results indicate that glycosylation of epididymal secretory glycoproteins occurs in the Golgi apparatus, which is, therefore, not bypassed as its morphological features had suggested. The kinetics of the secretory process in the principal cells includes 15 to 30 min for synthesis of the polypeptide parts of secretory products and addition of sugars in the Golgi apparatus, and a similar time for subsequent release from the Golgi apparatus, transport to the apical end of the cell and discharge to the lumen. Ribosome-studded (intermediate) portions of the sparsely granulated endoplasmic reticulum are probably involved in synthesis of polypeptide parts of secretory products, while vesicles or smooth portions of the sparsely granulated reticulum may play a role in intracellular transport of glycoproteins.
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PMID:Radioautographic analysis of the secretory pathway for glycoproteins in principal cells of the mouse epididymis exposed to [3H] fucose. 398 69

Arylsulfatase A was extracted and purified from boar epididymal sperm acrosomes. Acrosomes were extracted by sonication in 50 mM Tris-maleate buffer containing 50 mM MgCl2, pH 6.1, followed by treatment with 50 mM Tris-maleate plus 0.2% Brij-35, pH 6.1. Purification of arylsulfatase A was performed with a three-step procedure consisting of centrifugation (85,000 X g), affinity chromatography with p-aminobenzamidine-Sepharose followed by chromatography on diethyaminoethyl (DEAE) Sephadex. The specific activity of the purified enzyme was 54 mumol/h per mg protein. The purified arylsulfatase did not contain any detectable acrosin or hyaluronidase activities. Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis revealed a major band with an estimated molecular weight of 65,000 daltons. Properties of arylsulfatase A, determined by hydrolysis of p-nitrocatechol sulfate, indicated that the enzyme was inhibited 46% by 3.1 microM Ag+ and had a pH optimum of 4.2. Boar acrosomal arylsulfatase A dispersed the cumulus cells of ovulated hamster and rabbit eggs as well as those of follicular pig eggs. No effect of the enzyme on the zona pellucida or the oolemma was observed.
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PMID:Purification of boar acrosomal arylsulfatase A and possible role in the penetration of cumulus cells. 614 55


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