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)

Rat peri-renal and epididymal pre-adipocytes in culture undergoing triglyceride (TG) accumulation were incubated with oleic (18:1), linoleic (18:2), alpha-linolenic (18:3 omega 3), arachidonic (20:4) and 4,7,10,13,16,19-docosahexaenoic (22:6 omega 3) acids in the presence of 0.8 microM insulin. The fatty acids were incorporated in cellular TG with relative enrichments over control from 1.4-fold for 18:1 to greater than 40-fold for 18:3 omega 3. Greater than 80% of fatty acids taken up were incorporated into cellular TG. The balance was distributed, in decreasing amounts, into phospholipids, unidentified intracellular constituents, and ketone bodies. The P/S ratio of cellular TG was at least an order of magnitude lower than that of the external milieu for both cell types and for all treatment groups, including controls. Doubling the concentration of treatment fatty acid increased its incorporation into cellular TG. However, it did not affect the accumulation of the other fatty acids in TG. Epididymal cells consistently acquire a higher proportion of treatment fatty acids in cell TG than peri-renal cells. Pre-adipocytes with polyunsaturated fatty acids (PUFA)-enriched TG is a potential model for the study of PUFA metabolism in these types of cells.
Lipids 1991 Sep
PMID:Modulation of polyunsaturated fatty acid content of triglycerides in rat pre-adipocytes in culture. 176 15

The distribution of [14C]oleate label in rat tissues in the 6 hr after intravenous administration of sucrose octa[14C]oleate (7.5 mg; SuO8) was compared with that observed after administration of [14C]triolein. The [14C]oleate label, whether injected as triolein emulsion, or as chylomicrons obtained from donor animals, rapidly cleared from the serum; only 10% or less remained in the serum 15 min after injection. Labeled SuO8 disappeared less rapidly from the serum; about one-third of the dose was present after 15 min, and after 120 min 14% remained. In the liver, there was an initial greater accumulation of fatty acid label when an emulsion of either triolein or SuO8 was given rather than the chylomicrons. The octaester continued to accumulate in the liver throughout the 6 hr of study, and 78% of the initial dose was present at that time. By contrast, although one-third of the triolein, as of SuO8, was found in the liver shortly after injection, levels subsequently decreased; at 6 hr, 12% of the label remained associated with that organ. A small portion, up to 8% of the acid label, whether administered as chylomicrons or as a triolein emulsion, was found in the epididymal fat pads. Smaller amounts, usually 1% or less, of the [14C]oleate label were found in fat pads following the injection of labeled SuO8. In a separate study, the levels of acid label in the liver and spleen were monitored for 21 days following the intravenous administration of [14C]SuO8. There was an initial accumulation of approximately half of the injected lipid label in the liver and one-quarter in the spleen. By day 21, the level in the liver had decreased to one-third of that administered, while the level in spleen remained at one-quarter.
Lipids 1991 Sep
PMID:Distribution among tissues of intravenously administered sucrose octaoleate. 176 22

The epididymal tubule is a dynamic structure, in which spermatozoa undergo distinct physiological and morphological changes. The epithelial cells lining the ductuli vary dramatically in their histochemical and cytological properties according to the region of the tubule in which they are located. Additionally, regional variation is observed regarding the biosynthetic, secretory, and absorptive properties of the epithelial cells. Using in situ histochemical analysis, we document here the region-specific expression of a variety of genes that are transcriptionally active in the adult rat epididymis. Radiolabeled antisense riboprobes were used to localize, within the efferent duct/caput epididymis, transcripts encoding protein B/C, protein D/E (acidic epididymal glycoprotein), sulphated glycoprotein 1, sulphated glycoprotein 2, cellular retinol-binding protein, and the neuroendocrine peptide precursor proenkephalin. Each species of mRNA exhibits a unique pattern of hybridization, revealing that gene transcription within the efferent duct/caput epididymis is also highly region specific. This observation may partially elucidate the molecular basis underlying the phenomenon of regional alterations in the composition of protein factors within the tubule lumen.
Mol Reprod Dev 1991 Sep
PMID:In situ histochemical analysis of region-specific gene expression in the adult rat epididymis. 178 83

Clusterin (sulfated glycoprotein-2) is a heterodimeric glycoprotein synthesized and secreted by rat Sertoli cells. An antigenically similar form is synthesized and secreted by the epididymis. The goal of this study was to define the epididymal regions in which clusterin is present and the regions in which clusterin is secreted and interacts with developing spermatozoa. Seminiferous tubule (STF), caput, corpus, and cauda fluids were collected by micropuncture and/or microperfusion and two-dimensional Western blot analysis was performed with a polyclonal antibody directed against Sertoli cell clusterin. Clusterin was found in both STF and epididymal fluid. STF contained predominantly the clusterin heavy chain (45 kd); however, a 70 Kd heterodimer was present under nonreducing conditions. Two subunits of clusterin with lower molecular weights (41 kd, heavy chain; 32 kd, light chain) and higher isoelectric points were present in the luminal fluid of all epididymal regions. The intraluminal levels of the heavy and light chains decreased from caput to cauda. Analysis by two-dimensional gel electrophoresis of proteins secreted directly into the epididymal luminal fluid revealed that clusterin was secreted by caput epithelium and not by the corpus and cauda epithelium. Western blots of membrane extracts from testicular, caput, and cauda spermatozoa revealed that testicular clusterin was associated with testicular sperm and epididymal clusterin with predominantly caput sperm. Our findings suggest that clusterin is secreted into the caput epididymal lumen, where it binds to sperm and then dissociates from sperm to be endocytosed by cells of the distal epididymal epithelium.
Mol Reprod Dev 1991 Sep
PMID:In vivo secretion and association of clusterin (SGP-2) in luminal fluid with spermatozoa in the rat testis and epididymis. 178 89

Seasonal changes in reproductive activity in the adult male vizcacha (Lagostomus maximus maximus), a South American rodent, were investigated. Monthly, for 2 yr, the animals were killed and decapitated during the night near their burrows in the vicinity of San Luis, Argentina. The testes, epididymides, and pineal glands were removed and used for biochemical and structural studies. Significant changes associated with seasonal cycles were found. 1) In July-August (winter in South America), a short hibernal period of sexual quiescence, decline in testicular and epididymal weights, arrest of spermatogenesis, and decrease of serum testosterone were observed. The gonads regressed during this period, with regression most pronounced in August. 2) During September-November (spring), a recovery period--without arrest of spermatogenesis--was observed, with significant expression of gonadal activity during April-May (autumn). In this season, gonadal weight was increased and spermatogenesis was complete. These results indicate an increase in sexual activity as well as in the ability to secrete testosterone. A gradual reduction of testicular activity appeared in June-July (early winter). Conversely, in this period, the pineal hydroxyindole-O-methyl transferase activity decreased in contrast to the highest values observed in winter. Our findings indicate that the male adult vizcacha under natural conditions exhibits an annual reproductive cycle. A possible relationship between increased pineal activity and gonadal regression is also suggested.
Biol Reprod 1991 Sep
PMID:Seasonal variations in the testis and epididymis of vizcacha (Lagostomus maximus maximus). 178 99

The present study is to investigate the pathological changes in the epididymis of the rats within a period of 90 days after third degree phosphorus burns involving 30% of TBSA. By light microscopy and electron microscopy and histochemistry, varying degrees of degeneration and necrosis of epididymal epithelial cells, peritubular tissues and luminal spermatozoa and degenerative spermatid were found. The occurrence and development of all these changes might be divided into: the initiation and reaction phase of injury; the advanced phase; and the recovering phase. It is considered that epididymal tissue damage in advanced phase is so extensive and severe that the morphological, physiological and metabolic maturation of the spermatozoa may be affected, and the storing function of the epididymis as well. With the recovery of the burns, there was repair of the damaged tissues, and it could be inferred that the effect of phosphorus burns on the long-term reproductive capacity of male animals is probably mild.
Zhonghua Zheng Xing Shao Shang Wai Ke Za Zhi 1991 Sep
PMID:[Pathological changes in epididymis of rats after phosphorus burns and mechanism of development]. 178 88

A well-developed Golgi apparatus and rough and smooth endoplasmic reticulum in the principal cells of the mouse epididymis indicate active protein synthesis. Studies have shown that epididymal secretions are essential for sperm maturation. In a previous study, two wheat-germ agglutinin (WGA)-binding glycoproteins, GP-49 and GP-83, were identified on the surface of mature mouse sperm. In this study, synthesis and secretion of these two glycoproteins were investigated. Apparent WGA-binding was found on the stereocilia and in the apical region of principal cells in the corpus and cauda of epididymis. Post-fixation and pre-embedding cytochemical localization revealed that WGA-binding sites were situated in the Golgi apparatus, multivesicular bodies and stereocilia of principal cells. GP-49 and GP-83 were identified in the Nonidet P-40 homogenates of corpus and cauda epididymidis. In the epididymides of which ductuli efferentes had been ligated for more than 4 weeks, no sperm were found in the lumina of epididymal tubules. WGA-binding sites were present in the corpus and cauda; GP-49 and GP-83 were identified in tissue homogenates of the corpus and cauda as well. These findings suggest that GP-49 and GP-83 of mature sperm may be secreted by the principal cells of the corpus and cauda. These two molecules apparently conjugate to sperm whilst sperm transit through the epididymis.
Cell Tissue Res 1991 Sep
PMID:The secretion of two sperm maturation-related glycoproteins in BALB/c mouse epididymis. 178 90

The detection and the isolation of a zinc-protein from the secretion of the rat dorsolateral prostate is described. The purification procedure, based on gel filtration and cationic exchange chromatography, allowed to separate a minor protein (Mr approximately 66,000) from free zinc ions and other secretory components. Two zinc ions were estimated to be associated with one molecule of isolated protein. The zinc-protein was labelled with 125I and then incubated at 37 degrees C with spermatozoa from rat epididymal cauda. Time-dependent in vitro binding of the radioactive protein to sperm cells was demonstrated. This binding was not affected by the presence of proteins from the seminal vesicle during the incubation, while it was blocked in the presence of an excess of unlabelled zinc-protein. After binding, the labelled spermatozoa were treated with a buffer containing 0.5% sodium deoxycholate and 40 mM EDTA; only very small amounts of label were removed from the cells, thus suggesting that the zinc-proteins were kept on the plasma membrane by interactions which do not involve merely hydrophobic bonds.
J Exp Zool 1991 Sep
PMID:Zinc-protein from rat prostate fluid binds epididymal spermatozoa. 191 65

To determine whether the presence of sexually active females influences the reproductive processes of the male bandicoot, plasma testosterone concentrations were monitored in males isolated from females. Blood samples were obtained weekly from 8 male bandicoots housed with females and from 12 male bandicoots in an enclosure without females. Reproductive tracts were obtained from 7 of the male bandicoots of the latter group during the breeding season. In both groups plasma testosterone increased prior to the start of the breeding season and was not influenced by the absence of adult females. There was no significant difference in testosterone concentrations between groups at any time of year. Testicular, epididymal, and prostatic weights of males housed without females were similar to those reported for male bandicoots housed with adult females during the breeding season. These results demonstrate that the seasonal change in reproductive function in the male are not mediated via the female.
Gen Comp Endocrinol 1991 Sep
PMID:Effect of the presence of females on plasma testosterone concentration of male marsupial bandicoots, Isoodon macrourus, housed in enclosures. 193 27

1. Most of the cyclic-nucleotide-independent acetyl-CoA carboxylase kinase activity in an extract of rat epididymal adipose tissue was evaluated from a Mono Q column by 0.175 M-NaCl at pH 7.4. The activity of the kinase in this fraction (fraction 1) was increased after exposure of intact tissue to insulin. 2. Incubation of purified adipose-tissue acetyl-CoA carboxylase with [gamma-32P]ATP and samples of fraction 1 led to the incorporation of up to 0.4 mol of 32P/mol of enzyme subunit. Most of the phosphorylation was on serine residues within a single tryptic peptide. This peptide, on the basis of two-dimensional t.l.c. analysis, h.p.l.c. and Superose 12 chromatography, appeared to be the same as the acetyl-CoA carboxylase peptide ('I'-peptide) which exhibits increased phosphorylation in insulin-treated tissue. 3. Phosphorylation of purified acetyl-CoA carboxylase by the kinase in fraction 1 was found to be associated with a parallel 4-fold increase in activity. However, increases in both phosphorylation and activity were much diminished if fraction 1 was treated by Centricon centrifugation to remove low-Mr components. Among these components was a potent inhibitor of acetyl-CoA carboxylase activity which appeared to be necessary for the kinase in fraction 1 to be fully active. 4. The inhibitor remains to be identified, but inhibition requires MgATP, although the inhibitor itself does not cause any phosphorylation of the carboxylase. No effects of insulin were observed on the activity of the inhibitor. 5. It is concluded that the kinase probably plays an important role in the mechanism whereby insulin brings about the well-established increases in phosphorylation and activation of acetyl-CoA carboxylase in adipose tissue.
Biochem J 1990 Sep 15
PMID:Protein-serine kinase from rat epididymal adipose tissue which phosphorylates and activates acetyl-CoA carboxylase. Possible role in insulin action. 197 70


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