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)

Acidic epididymal glycoprotein (AEG) is a 31,000 molecular weight secretory protein of the rat epididymis. Screening of a rat epididymal cDNA library with affinity-purified AEG antiserum yielded cDNA for AEG. Identity of the clones was verified by comparison of amino acid sequence of the purified protein with the sequence derived from the nucleotide sequence of the cDNA isolates. Two classes of AEG cDNA, approximately 1500 base pairs (bp) and 950 bp in length, differed by 538 bp in the 3'-untranslated region and by four single nucleotide mismatches, one of which was in the coding region. Northern blot hybridization of epididymal RNA revealed two species of AEG mRNA, corresponding in length to each type of cDNA. Analysis of RNA from individual animals provided evidence that the two mRNA species are the products of allelic genes. In vivo studies demonstrated that the level of total AEG mRNA is regulated by androgen. Amino acid sequence homology of AEG with metal-binding domains of several proteins suggests that AEG is a metalloprotein.
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PMID:Molecular cloning of complementary deoxyribonucleic acid for an androgen-regulated epididymal protein: sequence homology with metalloproteins. 246 Jul 53

1. The distribution of phosphatidylinositol3, phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate hydrolysis or phosphatidylinositol-specific phospholipase C (PI-PLC), activity in the bull reproductive system showed the highest specific activity in the isolated spermatozoa (SZ) followed by testis and different epididymal segments. Both the head and tail fractions of SZ were active. 2. The optimal solubilization of the enzyme from SZ was obtained with 0.2% Triton X-100 or at 0.05% detergent concentration when combined with a 60 sec sonication. The sucrose gradient centrifugation showed that PI-PLC was enriched in membrane fraction distinct from mitochondria and acrosomes. 3. The enzyme was purified by ammonium sulphate precipitation and fractionations by hydrophobic interaction chromatography, gel filtration, Con A-Sepharose affinity and chromatofocusing columns. The purified enzyme was able to hydrolyse all phosphatidylinositol substrates with optimum at pH 7.0 and activation by Ca2+, Cd2+ and Mn2+ but not phospholipids lacking the inositol residue. 4. In PAGE (8-25% gradient) the purified (aggregated) enzyme did not enter the gel. In SDS-PAGE two closely located bands were found with Mr-values of 15,000 and 18,000. Isoelectric focusing showed a wide band at pl 4.5-5.1. 5. Gel filtration resulted in a broad elution peak indicating multiple molecular forms (aggregates); the basic form had an apparent molecular weight of 100,000. The binding of the enzyme to Con A-Sepharose indicated that the enzyme is a glycoprotein.
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PMID:Purification and characterization of phosphatidylinositol-specific phospholipase C from bovine spermatozoa. 255 6

Sulfated glycoprotein-1 is one of the major protein secretion products of rat Sertoli cells in culture. This 70,000 Mr protein shares substantial sequence similarity with human prosaposin, the precursor of lysosomal saposins. Saposins are known to enhance the activity of lipid modifying enzymes presumably by solubilizing the lipids. We report here the immunolocalization of sulfated glycoprotein-1 in the cells and fluid of the male reproductive tract. The protein is present in secondary lysosomes of Sertoli cells and also in the luminal fluid of seminiferous tubules and epididymis. The highest concentrations of the protein are in seminiferous tubule fluid and rete testis fluid, while relatively low amounts are found in cauda epididymal fluid and serum. Sulfated glycoprotein-1 is believed to be involved in degradation of lipids in residual bodies and may also assist in modification of membrane lipids during sperm maturation.
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PMID:Sulfated glycoprotein-1 (saposin precursor) in the reproductive tract of the male rat. 262 58

Blood sera of humans, rats, goats, and buffalo have been shown to possess a forward motility-stimulating factor (FMSF) that markedly stimulated goat cauda epididymal sperm forward motility, as assayed by a microscopic method in the presence of epididymal plasma (1.2 mg protein/ml) that had sufficient anti-sticking activity to eliminate the possibility of cell-sticking artifacts in motility assays. The specific activity of FMSF was greatest in buffalo blood serum compared to the sera of the other species. Buffalo serum at a concentration as low as 8.5 mg protein/ml induced forward motility in nearly 45% of the cells. The buffalo serum FMSF was heat-stable, nondialyzable, and sensitive to the action of trypsin. Purified proteins--casein, serum albumin, ovalbumin, myoglobin, and beta-lactoglobulin--showed little or relatively low FMSF activity. FMSF is a glycoprotein, as it binds with high affinity to concanavalin A-agarose. A major portion of the serum protein (approx. 70%) did not bind to the affinity matrix, and this unretained serum protein fraction showed little FMSF activity. The FMSF activity of buffalo serum was confirmed by estimating sperm forward motility spectrophotometrically: an objective method of assessing sperm motility.
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PMID:Stimulation of forward motility of goat cauda epididymal spermatozoa by a serum glycoprotein factor. 262 73

The epididymis of stallion castrated during the breeding and non breeding seasons were subdivided into six regions and their ultrastructural and cytochemical characteristics were studied in order to provide a better understanding of the structure-function relationship of this androgen target organ. Even when the stallion has been postulated to be a seasonal breeder, our results do not show significant ultrastructural or cytochemical differences in both seasons. The pseudostratified epithelium is composed mainly of principal and basal cells and intraepithelial lymphocytes. The principal cells show morphological features of protein or glycoprotein secretion, especially in the caput epididymidis. Although PAS, CFH and AB positive substances were found throughout the epididymis, the reactivity was maximal in the caput region. This positive reaction can be ascribed to acidic glycoproteins. In stallion tissues, 4.0 acetylated sialic acid occurs in relatively high amount and is possible that the acid glycoprotein observed in our material have also this characteristic. The principal cells of the distal caput and corpus epididymides also display morphological hallmarks of absorptive and anabolic activity. These results are consistent with the histological reactions that demonstrate that the enzymes involved in active transport showed the strongest reaction in the corpus region. The acid phosphatase reaction was also strongest in these segments. In the cauda region, where the spermatozoa are stored ready for ejaculation, morphological signs of metabolic activity were also observed, but less notorious than in the more proximal segments. Resorption of non ejaculated spermatozoa was also observed in this region. It is difficult to evaluate the functional meaning of the spermatophagy in the epididymis because the images of sperm phagocytosed by epithelial cells were seen only in one or two cases. The chemical composition of the epididymal fluids changes along the length of this organ, concomitantly with the sperm maturation process, and it is possible to assume that some of these changes are a result of the secretory and absorptive activities of the principal cells.
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PMID:Cytochemical and ultrastructural characteristics of the stallion epididymis (Equus caballus). 270 7

A polypeptide with molecular mass of 17 kDa has been partially purified and identified as a major secretory glycoprotein in the rat epididymis. It is phosphorylated and contains high mannose-type oligosaccharides with 5 and 6 mannose units predominantly. These sugar residues are sufficiently exposed in the molecule to be released by endo-beta-N-acetylglucosaminidase H without prior denaturation or protease digestion. Specific binding of the glycoprotein to testicular spermatozoa was demonstrated with Ka 0.2 x 10(9) M-1 and 17,200 sites per cell, while no binding to epididymal spermatozoa was detectable. Direct labeling of surface proteins on cauda epididymis spermatozoa revealed the presence of a major band of 16.2 kDa, which may be equivalent to GP17. The interaction of the epididymal secretory protein with sperm suggests a possible role in the maturation process.
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PMID:Identification of a major secretory glycoprotein from rat epididymis: interaction with spermatozoa. 272 28

Acidic epididymal glycoprotein (AEG), an androgen-regulated secretory protein of rat epididymis, was quantitated by RIA in epididymal extracts of rats of increasing age. Although detectable at 1 day of age, significant concentrations of AEG were not measured until 20 days; concentrations increased steadily, so that by 120 days of age, AEG represented 10% of total soluble protein. AEG mRNA was detected by Northern blot analysis of RNA from epididymides of 5-day-old animals and rapidly increased in amount between 20 and 35 days, reaching a maximum at 45 days. Using immunohistochemistry, AEG was localized in epididymal epithelial cells at 1 day of age. The number of cells staining for AEG increased markedly after 15 days. At 120 days, the immunoreactivity was predominantly localized to the lumen of the epithelial duct. To delineate factors that may influence AEG expression in the developing epididymis, we measured concentrations of androgen and androgen receptor mRNA in tissue extracts prepared from animals of various ages. Androgen receptor mRNA was detectable in epididymal extracts isolated from 1- to 90-day-old animals. Epididymal androgen concentrations were high at all ages (range, 6.0-31.2 ng/g tissue). The marked increase in AEG mRNA concentration at 20 days of age was not associated with an increase in either androgen or androgen receptor mRNA concentrations, suggesting that other factors may be necessary for AEG expression.
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PMID:Developmental expression of an androgen-regulated epididymal protein. 275 86

Male English springer spaniel dogs affected with fucosidosis, a lysosomal storage disorder, were found to be infertile while females with the disease reproduced successfully. Ejaculates of semen collected from affected dogs had reduced total sperm output and morphologically abnormal spermatozoa. A high proportion of ejaculated spermatozoa had midpiece droplets, bent tails and poor motility. Severely vacuolated epididymal epithelial cells were observed by light microscopy. Electron microscopic examination revealed membrane-bound vacuoles of variable size containing scanty amounts of granular to fibrillar material in epididymal epithelial cells, smooth muscle, myoid cells and Sertoli cells. Male infertility is believed to result from lysosomal storage of fucosyl-linked substrates in cells of the reproductive system. The extensive lesions in the epididymis may have interfered with maturation and transport of spermatozoa. Also, deficiency of alpha-L-fucosidase activity could have impaired the shedding of cytoplasmic droplets from spermatozoa and altered the surface glycoprotein composition of the sperm during epididymal transit.
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PMID:Reproductive abnormalities in canine fucosidosis. 276 Feb 71

This paper explores the relationship between the galactose oxidase-sensitive glycoproteins from rat caudal epididymal sperm and fluid and, in addition, their relatedness to the 32,000-Da major acidic secretory glycoproteins of caudal epididymal fluid. The major acidic secretory glycoproteins were purified by a combination of high-resolution anion-exchange (Mono Q) and gel permeation (Bio-Sil TSK 125) chromatographic steps. Immunoprecipitation studies, peptide mapping, and the inability to label the purified glycoprotein by galactose oxidase/sodium boro[3H]hydride clearly established that the galactose oxidase-sensitive fluid and membrane glycoproteins were not related to these acidic secretory glycoproteins. Membrane and fluid tritium-labeled glycoproteins were shown to be closely related, but not identical, polypeptides. Sugar analysis indicated that both glycoproteins contain N- and O-linked saccharide chains and that the galactose oxidase-sensitive residue was present only on O-linked sugars. It was also found that efficient labeling of the 32,000-Da fluid glycoprotein was possible only if protease inhibitors were omitted from all buffers used in the isolation of caudal epididymal fluid and subsequent labeling procedures. This suggests that the fluid glycoprotein was acquired by the unintentional proteolysis of the membrane glycoprotein. Polyclonal antibodies raised against caput sperm plasma membranes immunoprecipitated tritium-labeled glycoproteins from both caudal epididymal fluid and sperm membrane, suggesting that a precursor form of the caudal galactose oxidase-sensitive glycoprotein may be present on caput sperm.
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PMID:Characterization of the maturation-associated galactose oxidase-sensitive glycoproteins of rat caudal sperm plasma membrane and epididymal fluid. 293 Jan 87

During epididymal transit, the mouse sperm flagellum acquires a surface glycoprotein (SMA4) from epididymal fluid that functions as a sperm antiagglutinin. To determine the origin of this molecule, testes and epididymides of male mice were sectioned for light microscopy and stained with wheat germ agglutinin (WGA)-peroxidase, a probe that has been used previously to examine the biology of SMA4. WGA reactivity was localized to the cytoplasm in a small population of cells in the distal caput epididymis. Testis cells and principle cells of the caput were nonreactive with WGA, while stereocilia were stained on principle cells in the corpus and cauda. The WGA-positive cells in the distal caput were identified as holocrine cells on the basis of morphology, distribution, and PAS + reaction. At high magnification, intense WGA reactivity was due to the presence of numerous apical granules in the cytoplasm. The location of the cells in distal caput coincided exactly with the region of tubule in which sperm first acquired SMA4 on their flagellae. These data suggest that holocrine cells near the junction of caput and corpus epididymis are the source of the sperm antiagglutinin SMA4.
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PMID:Maturation antigen of the mouse sperm flagellum: II. Origin from holocrine cells of the distal caput epididymis. 303 4


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