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)

Rabbit Acrosome Stabilizing Factor (ASF) is an epididymal product that reversibly inhibits the process of sperm capacitation. The native molecular weights of the monomer and dimer ASF were determined from sedimentation and diffusion data at 129,000 and 259,000 Mr. The monomer is composed of 92,000 and 38,000 Mr subunits according to sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), with size heterogeneity demonstrated for the latter. The stoichiometry of the subunits appears to be one-to-one by gel scanning. Amino acid and carbohydrate compositions are characteristic of a globular glycoprotein, which is high in cysteine content and is 8.3% carbohydrate by weight. The sugar composition suggests the presence of both high mannose and complex N-linked oligosaccharides with the unusual feature of appreciable amounts of glucose. The isoelectric character of ASF spans a range from 5.3 to 7.0.
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PMID:Chemical and physical characterization of rabbit sperm acrosome stabilizing factor. 379 Jun 69

Clusterin, a glycoprotein that elicits cell aggregation, has previously been isolated from ram rete testis fluid, and has been partially characterized. In experiments reported, we have used monoclonal antibodies against clusterin in combination with indirect immunofluorescence microscopy to investigate the distribution of clusterin in the adult ram testis, rete testis, and excurrent ducts. Tissue blocks (5 mm3) were fixed in periodate/lysine/paraformaldehyde containing 0.1% glutaraldehyde and, after embedding, 5-microM sections were prepared for immunolocalization. In the testis, 2 basic patterns were observed: 1) strong to moderate staining for clusterin in the adluminal region with little staining in the basal region of the seminiferous epithelium and germinal cells; and 2) moderate staining throughout the seminiferous epithelium between germinal cells. In the rete testis, strong clusterin staining was localized intracellularly in the rete epithelial cells, most often associated with the luminal surface. In the epididymis, intracellular clusterin was localized in some principal cells of the caput epididymidis. The luminal surfaces and spermatozoa within the lumen were strongly positive. In the vas deferens, clusterin staining was associated with the luminal surface only. The presence of clusterin was clearly detected in unwashed isolated epididymal spermatozoa, but not in spermatozoa washed with phosphate-buffered saline containing 0.05% Tween 20.
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PMID:Immunolocalization of clusterin in the ram testis, rete testis, and excurrent ducts. 390 51

Highly motile goat cauda-epididymal spermatozoa, when diluted markedly with a modified Ringer's solution, bind (approx. 100%) rapidly to the glass surface of haemocytometer. However, presence of epididymal plasma (EP, 2 mg protein/ml) in the dilution medium prevents nearly completely sticking of cells to the glass surface. The anti-sticking factor (ASF) of EP that prevents adhesion of spermatozoa to glass is nondialysable, heat-stable and sensitive to the action of trypsin. ASF is a glycoprotein that binds with high affinity to concanavalin a-agarose. EP-proteins (approx. 85%) that did not bind to the affinity column had little antisticking activity, indicating high protein specificity for ASF. Addition of exogenous Ca++ (1 mM) and Mg++ (4 mM) had no effect on the activity of ASF.
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PMID:Occurrence of specific glycoprotein factor(s) in goat epididymal plasma that prevent adhesion of spermatozoa to glass. 400 71

This study investigated the effects on the progressive motility, zona-binding capacity, and fertility of spermatozoa from the cauda epididymidis of adult male rats that were actively immunized against an acidic glycoprotein secreted by the epididymis. The percentage of motile spermatozoa was less than 5% in nine of ten rats that received the epididymal antigen, and 40 to 50% in eight of the 10 control rats. In animals immunized against the antigen, there was a dramatic decrease, but not a complete suppression, in the capacity of epididymal spermatozoa to bind the zona pellucida as compared with the nonimmunized controls. Fertility was decreased two weeks after the end of the treatment, but partial restoration of fertility was observed 6 months later.
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PMID:Decreased fertility and motility of spermatozoa from rats immunized with a prealbumin epididymal-specific glycoprotein. 404 Sep 2

Immobilin, the highly viscoelastic glycoprotein isolated from rat cauda epididymal fluid, exhibits all of the key biochemical characteristics of a mucin: 1) it has a very high molecular weight (will not pass through a 10(6) dalton cut-off filter; 2) it contains 56% carbohydrate, with low or undetectable levels of mannose, xylose and uronic acid; 3) the carbohydrates (primarily galactose, N-acetylglucosamine and N-acetylgalactosamine) are arranged in short, oligosaccharide chains (4-20 monosaccharides per chain); 4) these oligosaccharide chains can be cleaved by NaOH in the presence of NaBH4, suggesting O-glycosidic linkages; and 5) the protein core is pronase-resistant. Immobilin, however, contains no detectable sialic acid, and 67% of the oligosaccharides are uncharged, indicating that immobilin is less acidic than most other mucins.
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PMID:Rat cauda epididymal fluid is a mucus. 405 30

To determine sequential surface glycoprotein changes in ram spermatozoa during epididymal maturation, labeling procedures were used that were specific for galactosyl, galactosaminyl, and sialyl residues. Spermatozoa and fluids were collected from the rete testis through surgically inserted catheters or flushed from the lumen of selected regions of the epididymis: i.e., caput, proximal and distal corpus, and cauda epididymidis. Ejaculated spermatozoa were collected by electrical stimulation. Electrophorectic analysis of galactose (GAO)-sodium boro[3H]hydride (NaB3H4)-treated spermatozoa revealed a sharp overall decrease in carbohydrate residue labeling during sperm transport through the efferent ducts and caput epididymidis, whereas several high molecular weight components in the 600K to 250K zone persisted throughout epididymal transit. Preincubation of spermatozoa with neuraminidase (NEUA) exposed galactose residues that had not been labeled with GAO alone (i.e., 97K, 43K, 24K) in both cauda epididymal and ejaculated spermatozoa. Treatment with sodium metaperiodate-NaB3H4 labeled many of the surface components displayed by NEUA-GAO-treated spermatozoa and revealed an overall shift in sialyl residue labeling from high molecular weight components in immature testicular spermatozoa to low molecular weight components in mature cells. The labeling procedures applied allowed only a qualitative interpretation of the results and they presumably represent the minimum possible changes. Nonetheless, our results demonstrate that glycoproteins are a major factor in surface transformations of ram spermatozoa in the epididymis, especially during the initial stages of maturation.
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PMID:Glycoproteins: a variable factor in surface transformation of ram spermatozoa during epididymal transit. 406 38

Cellulose acetate electrophoresis of rabbit seminal fluid give, after amidoschwartz staining, 19 protein bands, all migration towards the anode. Nine of them are present in at least 80% of the samples. With the acid of specific detection techniques, it was possible to demonstrate th presence of zinc in four bands, acid phosphatase activity in two and glycoprotein in three of the bands. Serum compounds seem to be present in small quantities. Study of fluids squeezed out from prostate, paraprostate, seminal vesicle and epididymal tail show few specific bands in these secretions: four in the case of prostate, three for paraprostate and one for seminal vesicle. Comparisons between human and rabbit seminal fluid electrophoresis show no relationship between these two types of secretion.
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PMID:Comparative electrophoretic study between rabbit and human seminal fluid. 408 49

Different proteins are secreted by the various regions of rat epididymis. We have examined the messenger RNA dependence of this varied gene expression by cell-free translation of poly(A)RNA extracts from initial segment, caput plus corpus, and cauda. Labeled translation products were analyzed by polyacrylamide gel electrophoresis under denaturing conditions. Poly(A)RNA from initial segment coded for several unique bands of labeled protein, including a 23,000 MW protein that may correspond to an initial segment protein reported previously to be regulated by testicular fluid factors. Messenger RNA encoding 20,000 MW protein believed to be alpha-lactalbumin, was most abundant in caput but also present in initial segment. Acidic epididymal glycoprotein (AEG) was identified previously by immunoperoxidase staining in epithelial cells of caput, corpus, and cauda. AEG was not readily identified on electrophoresis of total translated proteins, but when concentrated by immunoprecipitation with purified AEG antibody prior to electrophoresis, AEG appeared in both caput plus corpus, and in cauda poly(A)RNA translations.
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PMID:Translation of messenger RNA from rat epididymis and identification of poly(A)RNA coding for acidic epididymal glycoprotein. 615 23

A correlative ultrastructural and histochemical study of the epididymal principal cells was carried out on six normal mature macaque monkeys with known reproductive histories. The outstanding cytologic feature of the principal cells was the abundance of infranuclear electron-dense granules (0.2-0.5 micronsm). These cellular inclusions are found in close proximity with large clusters of small mitochondria and to the subepithelial and periductular capillaries surrounding the basal epithelium. Histochemical tests revealed that these granules do not contain acid phosphatase, are not lipid, but do contain mucopolysaccharides and glycoprotein moieties. This intriguing morphological characteristic of the infranuclear region of the principal cells is similar throughout the entire length of the epididymis and appears to be unique in the monkey. The close relationship of these secretion type granules to mitochondria and their proximity to basal epithelial capillaries is in agreement with the concept of epididymal secretion and a possible endocrine function of the mammalian epididymis must be considered.
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PMID:Ultrastructural and histochemical observations on the principal cells of monkey epididymis. 615 21

Hamster spermatozoa were isolated from the caput, corpus and cauda epididymidis. They were observed in culture medium at 37 degrees C with a phase-contrast microscope and their motility recorded cinematographically. About 20 p. 100 of the caput epididymidis spermatozoa were motile and moved in a confined space with no forward progression. 30 p. 100 of the corpus epididymidis spermatozoa were motile, showing increased flagellar activity and moving in wide circles. 90 p. 100 of the cauda epididymidis spermatozoa were motile and moved forward. Forward motility was induced in immotile spermatozoa from the caput epididymidis by adding cyclic 3'-5' adenosine monophosphate (cAMP) phosphodiesterase inhibitors (caffeine, theophylline, IMX) and epididymal plasma. The best stimulation was initiated by 15 mM caffeine with 10 p. 100 of cauda epididymal plasma; a mean of 60 p, 100 of forward motility was obtained which lasted for one hour and then ceased. Cinematographic studies revealed that some induced sperm movements differed from the equivalent natural ones by the amplitude of the head movements. It is shown that during epididymal transit of hamster spermatozoa, the induction of forward motility requires not only an increased cAMP level but also factors from the cauda epididymal plasma. The idea that glycoprotein of epididymal origin initiates forward motility is discussed.
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PMID:Development and initiation of sperm motility in the hamster epididymis. 618 85


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