SEARCH · Search PubMed

Results for “EPIDIDYMITIS”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

SourceResearch connectionFrom yearThrough year

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 973 records · Page 54Linked to original sources

PubMed1989

Androgenic control of antagglutinin secretion in the boar epididymal epithelium. An immunocytochemical study.

Antagglutinin, a specific protein synthesized by the boar epididymis, was secreted by the principal cells of the initial segment, the caput and the corpus, but was not detectable in the caudal cells. Castration completely abolished the synthesis and secretion of antagglutinin in all epididymal cells. Androgen replacement suggests that the epithelial cells from different segments have differential regulatory mechanisms. The proximal zone appeared refractory to exogenous testosterone; the median zone was a typical androgen-dependent region; and the caudal cells, where an unusual secretion of antagglutinin was detected, revealed still a different reaction pattern. It is postulated that these latter cells depend not solely on androgen but also or exclusively on other factors. Our results, which demonstrate a primary role of the Golgi complex in the secretory process in the epididymal cells, also suggest that the apical smooth endoplasmic reticulum may be implicated in the intracellular transport of glycoproteins to the cell surface.

Androgens↗

PubMed1985

Synthesis of highly unsaturated phosphatidylcholines in the development of sperm motility: a role for epididymal glycerol-3-phosphorylcholine.

Interpretation of the experimental literature on epididymal glycerophosphorylcholine metabolism according to a recently proposed de novo pathway for the synthesis of acyl-specific phosphatidylcholine suggests that epididymal glycerophosphorylcholine is an intermediate of this proposed pathway. This glycerophosphodiester is postulated to be utilized by spermatozoa to synthesize docosahexaenoic phosphatidylcholine, proposed to be required for the development of sperm motility. A defect in glycerophosphorylcholine synthesis might be responsible for some forms of asthenozoospermia.

Animals↗

PubMed1993

An isoform of protein disulfide isomerase is expressed in the developing acrosome of spermatids during rat spermiogenesis and is transported into the nucleus of mature spermatids and epididymal spermatozoa.

We have purified an isoform of protein disulfide isomerase (EC 5.3.4.1) from rat liver, and raised a specific antibody against the purified protein in rabbit. Immunohistochemical studies using this antibody on rat testis sections, at both light and electron microscopic levels, showed a specific localization of the isoform of protein disulfide isomerase in the developing acrosome of the spermatids. The protein was transferred to the acrosomic vesicle from the Golgi apparatus at late Golgi phase, and remained present in the acrosome of spermatids during cap phase, acrosome phase, and maturation phase. In addition to the acrosome, the protein appeared in the nucleus of spermatids during maturation phase, and was localized in the nucleus of epididymal spermatozoa. By immunoblot analysis, almost all of the isoform of protein disulfide isomerase in the testis was found to be extractable by an isotonic buffer. On the contrary, detergent extraction was required for complete solubilization of the protein in the epididymis. These results suggest that the isoform of protein disulfide isomerase is a new intra-acrosomal soluble protein, and that the protein begins to enter the nucleus of mature spermatids in the testis and tightly binds to the nuclear components in epididymal spermatozoa.

Acrosome↗

PubMed1995

Immunocytochemical localisation of some lysosomal hydrolases, their presence in luminal fluid and their directional secretion by human epididymal cells in culture.

The way in which the human epididymis modifies spermatozoa during their sojourn in this structure might be clarified by knowledge of the nature of its secretions. We have examined the presence of several lysosomal hydrolases in human epididymal tissue and fluids, and their synthesis and secretion by monolayer cultures. Tissues were obtained from men undergoing orchidectomy for prostatic carcinoma. The enzymes cathepsin D and acid alpha-glucosidase were localised in the lysosomes of epithelial cells from the corpus epididymidis, by an immunocytochemical technique. Cathepsin D was also found in epithelial cells of the efferent ducts within lysosomes, apical vesicles and multivesicular bodies. No immunolocalisation of acid glucosidase in the efferent ducts or on the microvilli of the corpus was demonstrable. Cathepsin D, beta-hexosaminidase (N-acetylglucosaminidase) and alpha-glucosidase were measurable in the luminal fluid from the human corpus epididymidis; beta-hexosaminidase was secreted into the culture medium by confluent monolayers of epididymal and efferent duct cells. Immunoprecipitation of cell extracts and culture medium of these cultures incubated with 35S-methionine revealed that the precursors of cathepsin D and beta-hexosaminidase were synthesized and secreted by such monolayers. Thus, active lytic enzymes are secreted by the human epididymis and could modify sperm membranes.

Adult↗

PubMed1994

Biphasic short-circuit current response to noradrenaline mediated by Ca2+ and cAMP in cultured rat epididymal epithelium.

A study was carried out to investigate the short-circuit current (Isc) response to noradrenaline (NA) and the signal transduction mechanisms involved in cultured rat cauda epididymal epithelium. In normal Krebs-Henseleit solution, NA (10 mumol.l-1) added basolaterally elicited a biphasic Isc response consisting of a transient spike followed by a second sustained response. The biphasic response was almost abolished by removing ambient Cl-. Preloading the tissues with a cell-permeant Ca2+ chelator, 1,2-bis(2-aminophenoxy) ethane-N,N,N',N',-tetraacetic acid acetoxymethyl ester (BAPTA/AM), or pretreating them with thapsigargin (Tg), a microsomal adenosine triphosphatase inhibitor abolished the initial spike in the Isc response to NA, but had little effect on the second component. Pretreating the tissues with a non-selective beta-antagonist, nadolol, reduced the second Isc response in a dose-dependent fashion but the initial spike was not affected. Microfluorimetric studies showed that NA (100 mumol.l-1) elicited single Ca2+ spikes in isolated epididymal cells, which could be abolished by prior treatment with Tg. Biochemical assays showed that NA (10 mumol.l-1) increased intracellular cyclic adenosine monophosphate concentration ([cAMP]i) and the response was abolished by prior treatment with nadolol (50 mumol.l-1). The results showed that NA elicited a biphasic Isc response mediated by a rise in intracellular Ca2+ concentration ([Ca2+]i) followed by a rise in [cAMP]i. The Ca(2+)-mediated Isc response had a faster onset and more transient action than the cAMP counterpart. It is suggested that NA released from noradrenergic nerve endings regulates transepithelial Cl- secretion in the epididymis thereby providing the specialized millieu vital for sperm storage and maturation.

Animals↗

PubMed1987

Tritiated thymidine autoradiographic study on postnatal development of epididymal adipose tissue in the normal mouse.

Cell proliferation was studied in the developing epididymal adipose tissue of mice by means of 3H-thymidine autoradiography. 4 mice in each age group were killed 30 min after a single injection of 3H-thymidine given at the 6th, 10th, 16th, 21st, 28th, 35th, 42nd, 49th or 56th postnatal day. The labeling index of the adipose tissue was high for several postnatal days but it was highest on the 6th day. The labeling index decreased thereafter, and cell proliferation appeared to almost cease after 56 days. Another 16 mice were given a single injection of 3H-thymidine at 6 days old; pairs of animals were killed at 30 min, 2, 4, 6, 8, 10, 14 and 18 days later. From the 2nd to 6th days of pulse labeling, the number of labeled fat cells increased significantly, whereas the number of labeled poorly differentiated mesenchymal cells decreased reciprocally. The labeling index of fat cells remained unchanged from the 6th to the 18th day. These results suggest that there is a population of fat cell-precursor cells in the mesenchymal tissue of the new born mouse, and that it takes 2-6 days for the precursor cells to become mature fat cells in the epididymal fatty tissue.

Adipose Tissue↗

PubMed2002

[Isolated epididymal torsion in dissociation of testis-epididymis].

Complete dissociation of testis and epididymis is rare. An isolated torsion of the epididymis has not been reported so far. We report two cases: a 6-month-old boy who was admitted with fever and swollen hemiscrotum and an 18-year-old youth with acute onset of pain in the left hemiscrotum. Immediate inguinal surgical exploration of the baby showed a complete infarction of the epididymis due to an isolated epididymal torsion with dissociation of testis and epididymis. Epididymectomy was carried out and the testis was sutured down. In the case of the youth, the surgical exploration also showed an isolated epididymal torsion due to dissociation of testis and epididymis. The epididymis could be rescued by raising the torsion. The isolated torsion of the epididymis should be included in the differential diagnosis of acute scrotum in childhood.

Acute Disease↗

PubMed2005

Intake of conjugated eicosapentaenoic acid suppresses lipid accumulation in liver and epididymal adipose tissue in rats.

It has been reported that consumption of CLA and EPA alters lipid metabolism. CLA contains conjugated double bonds, and EPA is an n-3 PUFA. Based on the possibility that a molecule with both of these structures might have interesting physiological effects, we prepared conjugated FA from EPA by alkaline isomerization and examined the effects of the conjugated EPA (CEPA) on lipid metabolism in rats. Rats were fed by oral gavage every day for 4 wk with 200 mg of FA including linoleic acid, EPA, CLA, or CEPA. Compared with other groups, rats fed CEPA showed a significant weight loss in epididymal adipose tissue and significant decreases in the levels of liver TAG and total cholesterol (TC), indicating reduced accumulation of lipid in the liver and adipose tissue. The plasma levels of TAG, TC, FFA, and tumor necrosis factor-alpha in rats fed CEPA were reduced, as was the activity of the FA synthesis system in the liver, whereas the FA-beta-oxidation system was activated by CEPA. These results suggest that intake of CEPA suppresses lipid accumulation in the liver and epididymal adipose tissue while increasing lipid catabolism in rats.

Adipose Tissue↗

PubMed1988

Rat epididymal alpha-D-mannosidase: purification, carbohydrate composition, substrate specificity, and antibody production.

Two alpha-D-mannosidases have previously been identified in rat epididymis. This communication reports the purification and characterization of the "acid" alpha-D-mannosidase. The enzyme was purified over 1000-fold to near homogeneity by acetone and (NH4)2SO4 precipitation followed by ion-exchange and hydroxylapatite chromatography. The molecular weight of the enzyme was estimated to be 220,000 by gel filtration. Polyacrylamide gel electrophoresis of the native enzyme under two conditions of buffer and pH showed a single band when stained for protein while electrophoresis under denaturing conditions resulted in bands of apparent Mr 60,000 and 31,000. The enzyme is a glycoprotein containing about 5.6% hexose. In addition to mannose (3.1%) and glucosamine (2.0%), the enzyme also contained small amounts of glucose, fucose, and galactose. Chemical analysis indicated the absence of sialic acid. The substrate specificity of the purified enzyme was investigated using linear and branched mannose-containing oligosaccharides. The enzyme cleaved linear oligosaccharides [Man(alpha 1-2)Man(alpha 1-2)Man(alpha 1-3)Man(beta 1-4)GlcNAc and Man(alpha 1-2)Man(alpha 1-3)Man(beta 1-4)GlcNAc] very efficiently. However, little or no activity was observed toward high mannose oligosaccharides (Man9GlcNAc through Man5GlcNAc) or the branched trimannosyl derivative Man3GlcNAc. This specificity is very similar to that observed with rat kidney lysosomal alpha-D-mannosidase. Additional evidence that the epididymal enzyme is essentially a lysosomal alpha-D-mannosidase is the fact that polyclonal antibody prepared against the purified epididymal enzyme cross-reacted with lysosomal alpha-D-mannosidase from several rat tissues and with acidic alpha-D-mannosidase of a human cell line, results suggesting that the antibody will be useful in studying the biosynthesis and turnover of lysosomal alpha-D-mannosidases in at least two species.

Animals↗

PubMed1990

Partial purification and characterization of an acetylcarnitine hydrolase from bovine epididymal spermatozoa.

We previously reported that intact epididymal spermatozoa from bulls and hamsters oxidize [1-14C]acetyl-L-carnitine to 14CO2 at about the same rate as they oxidize [1-14C]acetate. In addition, we showed that acetylcarnitine is hydrolyzed by a hydrolase present in the plasma membrane and that the carnitine moiety does not enter the cell. Here we report the partial purification of the acetylcarnitine hydrolase from bovine spermatozoa and describe some of its properties. The detergent-extracted enzyme was purified by FPLC using an anion-exchange Mono-Q column. The hydrolase activity eluted from the column with the application of 0.22 to 0.30 M NaCl and was separated from acetylcholinesterase activity, which eluted with 0.35 to 0.40 M NaCl. Specific inhibitors of acetylcholinesterase had little effect on acetylcarnitine hydrolase but p-hydroxymercuriphenylsulfonate was a potent inhibitor of the hydrolase. Kinetic studies of the hydrolase yielded a K'm of 6-10 mM for acetylcarnitine and a V'max of 0.16 nmol min-1 mg protein-1. Similar studies with the acetylcholinesterase yielded a K'm for acetylcholine of about 300 microM and a V'max of 165 nmol min-1 mg protein-1. Acetylcarnitine was a poor substrate for the acetylcholinesterase. Several acyl-L-carnitines were tested as substrates for the hydrolase and the preferred substrate was acetylcarnitine. The role of acetylcarnitine hydrolase in the metabolism of acetylcarnitine by epididymal spermatozoa is discussed.

Acetylcholinesterase↗

PubMed1975

Hormone action at the membrane level. IV. Epinephrine binding to rat liver plasma membranes and rat epididymal fat cells.

[3-H]Epinephrine binding to isolated purified rat liver plasma membranes is a reversible process. An initial peak in binding occurs at about 15 min and a plateau occurs by 50 min. Optimal binding occurred at a membrane protein concentration of 125mug. Rat liver plasma membranes stored at-70 degrees C up to 4 weeks showed no difference in epinephrine binding capacity as compared to control fresh membranes. Epinephrine binding to liver plasma membranes was decreased by 79% by phospholipase A2 (phosphatide acylhydrolase EC 3.1.1.4), 81% by phospholipase C (phosphatidylcholine choline phosphohydrolase EC 3.1.4.3) and 59% by phospholipase D (phosphatidylcholine phosphatidohydrolase EC 3.1.4.4). Trypsin and pronase digestion of the membrane decreased epinephrine binding by 97 and 47% respectively. In the presence of 10-3M Mg-2+ ions, increasing concentrations of QTP decreased epinephrine binding to liver plasma membranes. A maximal effect was demonstrated with 10-5M GTP, representing an inhibition of 52% of the control. In a Mg-2+ -free system, epinephrine binding was unaffected by GTP. However, in a Mg-2+ -free system, increasing concentrations of ATP cause increasing inhibition of hormone binding. ATP at 10-3 M reduced epinephrine binding to 28% of the control. GRP (10-5 M) was shown to inhibit epinephrine uptake rather than epinephrine release from the membrane. [3-H]Epinephrine binding to isolated rat epididymal fat cells shows an initial peak within 5 min followed by a gradual rise which plateaus after 60 min. Epinephrine binding increased nearly linearly with increasing fat cell protein concentration (40-200 mug protein). GTP (10-5 M) and ATP (10-4 M) decreased epinephrine binding to rat epididymal fat cells by 41%. Nearly complete inhibition of binding was demonstrated with 10-2-10-3M ATP. Epinephrine analogs that contain two hydroxyl groups in the 3 and 4 position on the benzene ring act as inhibitors of [3-H]epinephrine binding to rat adipocytes. Alteration of the epinephrine side chain has relatively little influence on binding. Analogs in which one of the ring hydroxyl groups is missing or methylated are poor inhibitors of [3-H]epinephrine binding. Alpha-(phentolamine and phenoxybenzamine) and beta-(propranolol and dichorisoproterenol) adrenergic blocking agents were tested with respect to their ability to influence [3-H]epinephrine binding and their influence on epinephrine-stimulated lipolysis. Only dichloroisoproterenol significantly inhibited epinephrine binding (by 25%). The two beta-adrenergic blocking agents caused an inhibition of epinephrine-stimulated glycerol release, with propranolol being most effective. Phentolamine and phenoxybenzamine had no significant effect on the epinephrine stimulation of glycerol release by fat cells.

Adipose Tissue↗

PubMed1980

The relationship between the transport of glucose and cations across cell membranes in isolated tissues. X. Effect of glucose transport stimuli on the efflux of isotopically labelled calcium and 3-O-methylglucose from soleus muscles and epididymal fat pads of the rat.

(1) The relationship between Ca2+ and sugar transport has been studied by comparing the washout of 45Ca and 3-O-[14C]methylglucose from preloaded isolated rat soleus muscles and whole epididymal fat pads. (2) In soleus muscle, nine different agents with well established stimulating effects on glucose transport were all found to produce a marked increase in 3-O-[14C]methylglucose washout, which in each instance was preceded by or coincided with a rise in the washout of 45Ca. (3) Trypsin, 2,4-dinitrophenol, p-chloromercuriphenylsulfonic acid, H2O2 and hyperosmolarity all produced dose-dependent stimulation of the washout of 45Ca and 3-O-[3H]methylglucose. Regression analysis showed a highly significant correlation between the increases in the two parameters (P < 0.001). (4) Depolarization and Na+ influx induced by veratrine were found to be associated with a marked rise in 45Ca release followed by stimulation of 3-O-[14C]methylglucose washout. (5) In epididymal fat pads, six different agents known to stimulate glucose transport were found to produce a highly significant (P < 0.001) increase in the washout of 45Ca and 3-O-[14C]methylglucose. (6) It is concluded that in the major targets for insulin action, activation of the glucose transport system can be elicited by a rise in cytoplasmic Ca2+ concentration brought about by mobilization of Ca2+ from endogenous cellular pools.

4-Chloromercuribenzenesulfonate↗

PubMed1986

Exposure of latent prostaglandin-binding sites in the rat epididymal adipocyte membrane.

The addition of albumin to a suspension of plasma membranes isolated from rat epididymal fat cells increases both the initial binding rate and the maximal specific binding of prostaglandin E2 to these membranes. The presence of albumin affects neither the dissociation rate of bound prostaglandin E2 nor its dissociation constant. The results indicate that the interaction of albumin with the isolated membranes exposes latent prostaglandin-binding sites. Albumin fails to alter the specific binding of prostaglandin E2 to membranes isolated from frog erythrocytes or from rat peritoneal fat cells. These results indicate that the effect of albumin on the specific binding of prostaglandin E2 characterizes a specific molecular property of the prostaglandin receptors in rat epididymal adipocytes.

Adipose Tissue↗

PubMed1979

The lipid composition of plasma membrane and mitochondrial fractions from epididymal adipocytes of cold-acclimated rats.

1. The effects of cold acclimation (5 degrees C) on the lipid composition of plasma membrane and mitochondrial fractions from epididymal adipocytes of rats were studied. 2. The adipocyte plasma membrane fraction of the cold-acclimated rats had lower lipid, phospholipid and cholesterol to protein weight ratios, a lower cholesterol to sphingomyelin molar ratio, and a higher linoleic acid content in the phospholipids than controls. 3. The mitochondrial fraction of the cold-acclimated rat adipocyte had lower ratios of cholesterol to protein (weight), to phospholipid and to cardiolipin (molar), and less sphingomyelin content than did controls. 4. These data, discussed in terms of alterations in physical and biochemical properties, indicate cold-induced changes at the membrane level in rat epididymal adipocytes.

Acclimatization↗

PubMed1975

Changes in phospholipids of ram spermatozoa during migration through the epididymis and possible origin of prostaglandin F2alpha in testicular and epididymal fluid.

A study of the lipid composition of ram testicular and ejaculated spermatozoa was made in an attempt to resolve conflicting results in the literature. Testicular spermatozoa were found to contain more than double the amount of phospholipid present in ejaculated spermatozoa. Most phohpholipid components, including choline plasmalogen, decrease substantially in concentration during migration of the spermatozoa through the male reproductive tract. Phosphatidylserine, ethanolamine phosphoglycerides and cardiolipin components accounted for the greatest relative decreases in concentration, the former decreasing by approximately nine tenths. Of the phospholipid-bound fatty acids the most pronounced change occurs in palmitic during migration of spermatozoa through the reproductive tract. There is a net loss of approx. 500 mug of palmitic acid for every 10-9 spermatozoa. The loss of arachidonic acid was particularly interesting, and prompted a study of the prostaglandin content of testicular and epididymal fluids, since arachidonic acid can act as a precursor of prostaglandin. The concentration of prostaglandin F2alpha found in the testicular and epididymal fluid is considerably in excess of that found in venous plasma of the ram.

Animals↗

PubMed1987

beta-Galactosidase from rat epididymal fluid is bound by a recognition site attached to membranes of the epididymis different from the phosphomannosyl receptor.

In order to know if the beta-galactosidase of the rat epididymal fluid, as other secreted acid hydrolases, carries a marker in its molecule, we studied the binding of this enzyme to cellular membranes of the epididymal tissue. The binding, like that mediated by the phosphomannosyl receptor, was saturable, did not require calcium, had a Kd in the nM range and was inhibited by phosphatase or metaperiodate treatment of the enzyme. However fructose 6-phosphate derivates were more effective competitive inhibitors than mannose 6-phosphate. The binding capacity of the membranes were extractable with Triton X-100 and incorporable into liposomes. Trypsin inhibited the binding capacity of Triton extracts but it did not affect the affinity of intact cellular membranes for beta-galactosidase. The results suggest that a phosphorylated carbohydrate of the enzyme is bound by a recognizing site of the cellular membranes different from the phosphomannosyl receptor.

Animals↗

PubMed1980

Fertility and electrolyte composition of the rat cauda epididymal plasma and spermatozoa before and after castration.

Attempts have been made to assess the changes in Na+ and K+ concentrations in the cauda epididymal plasma and spermatozoa, and to correlate these parameters to changes in fertility shortly after castration in the rat. Fertility was markedly decreased 3 days after androgen withdrawal. By contrast, spermatocrit and Na+ concentration in spermatozoa were increased on day 2 post-castration. Neither Na+ and K+ concentrations in the plasma nor K+ inside spermatozoa were altered. The results are discussed in terms of a reduction in the epididymal secretion of macromolecules which are responsible for an increase in net Na+ influx into sperm cells.

Androgens↗

PubMed1987

Dose and time related changes in LDH-X activity, epididymal carnitine levels and fertility, in gossypol-treated male rats.

Gossypol acetic acid could induce total infertility in male Wistar/NIN strain rats at a dose of 30 mg per kg body weight per day, for 52 days. 20 mg for 52 days and 30 mg for 38 days produced partial infertility. Highly significant correlation between parameters of infertility like reduced cauda sperm count, and implantation sites, and reduction in LDH-X activity of cauda epididymal sperm and carnitine levels in cauda epididymal fluid were observed. Testis remained unaffected.

Animals↗