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PubMed2002

Pro-inflammatory cytokine response of the fluid contents of spermatoceles and epididymal cysts.

The aim of the study was to determine the cellular contents and concentrations of interleukin 6 (IL-6), interleukin 8 (IL-8) and tumour necrosis factor alpha (TNF-alpha) in fluids of patients with spermatocele or epididymal cyst. Twenty-five symptomatic patients, 14 with epididymal cysts and 11 with spermatoceles, were included in the study. Fluids were obtained during surgical excision of the cysts and cytological smears were stained with May-Gruenwald-Giemsa to establish cell components. The concentrations of IL-6, IL-8 and TNF-alpha were measured by chemiluminescent immunometric assay. Cytological analysis of the fluids demonstrated various sperm forms ranging from immature germ cells to degenerated spermatozoa without inflammatory cells such as neutrophils and macrophages. The concentrations (mean+/- SEM, pg/mg protein) of IL-6, IL-8 and TNF-alpha were 13.52 +/- 1.40, 22.20 +/- 2.43, 3.51 +/- 1.43 in spermatocele fluids and 5.76 +/- 0.48, 11.57 +/- 1.89, 2.53 +/- 0.41 in epididymal cyst fluids. Both IL-6 and IL-8 concentrations in the spermatocele group were higher than in the epididymal cyst group (P < 0.0001). There were no differences in TNF-alpha concentrations between the groups (P > 0.05). These findings indicate that local production of pro-inflammatory cytokines is involved in cyst formation. The presence of immunologic activation in these fluids advocates a policy of selective surgical intervention in patients with spermatocele or epididymal cyst.

Adult↗
PubMed2001

Mobility shift assay of calcium-binding proteins of mouse epididymal spermatozoa.

The calcium-binding proteins (CBPs) of mouse epididymal spermatozoa were analysed by mobility changes in the presence of added Ca2+ in two-dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The expression patterns of relatively high molecular weight CBPs (Mr > 20 kDa) were different between caput and cauda epididymal spermatozoa. There was a constitutive expression of low molecular weight CBPs (Mr < 20 kDa) regardless of the epididymal region. Most of the CBPs disappeared after the acrosome reaction (AR) induced by Ca2+ ionophore A23187, suggesting that they originated from the acrosome and/or the plasma membrane overlaying the acrosome. Taken together, it can be suggested that changes in CBPs of spermatozoa are important features of sperm maturation during epididymal transit, and that they may be related to the fertilizing ability of mouse epididymal spermatozoa.

Acrosome Reaction↗
PubMed2001

Epididymal markers in rats exposed to the xenoestrogen p-nonylphenol: no biochemical effects at low dosages.

Harmful micro- and macroscopic effects of the environmental xenoestrogen p-nonylphenol (p-NP) on the male rat reproductive system have been previously reported. In our study, biochemical evidence of epididymal involvement was sought by determining epididymal marker values after exposure at levels below (5, 20 and 50 mg kg-1) and above (100, 250 and 400 mg kg-1) the "no observed adverse effect" level (NOAEL: 50 mg kg-1 day-1). Exposure to p-NL below the NOAEL did not affect biochemical marker values. At levels above the NOAEL, biochemical markers of epididymal function were affected by the exposure of adults, and by maternal exposure (gestational and lactational periods followed by oral exposure until sexual maturity). l-carnitine was unchanged at all levels of exposure. Exposure of adult males to levels above the NOAEL resulted in higher alpha-glucosidase, suggesting increased epididymal secretory activity. This could upset the balance between secretory and reabsorptive function, and could alter the biochemical composition of the epididymal luminal fluid surrounding spermatocytes during the maturation process. Maternal exposure at levels above the NOAEL resulted in higher tartrate-resistant acid phosphatase activity in the caput-corpus epididymidis, which could indicate an oestrogen-mimicking effect.

Acid Phosphatase↗
PubMed2002

Primary culture of the rat epididymal epithelial cells as a source of oestrogen.

Studies were performed on the rat epithelial cells of the caput and cauda epididymidis cultured in a full medium enriched with foetal calf serum without or with exogenous testosterone. After 3 days of culture, the cells formed a monolayer. The cytoplasm of epididymal epithelial cells cultured with testosterone was rich in lipid droplets, glycogen and PAS-positive substances, while their content was decreased in the cytoplasm of cells cultured without testosterone. The activity of 3beta-hydroxysteroid dehydrogenase was observed both in the cytoplasm of cultured epididymal epithelial cells and epithelial cells of epididymal sections. Hormone assays showed very low levels of dehydroepiandrosterone, androstenedione and testosterone, and the absence of progesterone in the media of cells cultured without testosterone and higher testosterone concentrations when the cells were cultured with exogenous testosterone. However, the concentration of 17beta-oestradiol found in the medium of cells was high, and exceeded many-fold its levels in the control media. Lentaron (Formestan), steroidal inhibitor of cytochrome P450 aromatase added to the culture decreased the secretion of oestradiol. RT-PCR analysis yielded cDNA products of 333 bp in length when primers were chosen to amplify a highly conserved sequence in the 3' region of the cytochrome P450 aromatase gene. This study demonstrates the ability of epididymal epithelial cells in vitro to synthesize androgens and mRNA for cytochrome P450 aromatase in the cultured epididymal epithelial cells of the rat as well as the ability to aromatise the synthesized androgen to 17beta-oestradiol.

Androgens↗
PubMed1983

Epididymal functions and their hormonal regulation.

The epididymis is a complex organ which maintains a specific intraluminal environment thought to be important for effecting sperm maturation in proximal regions and sperm storage in distal regions of the duct. The composition of the internal milieu is achieved both by transport between blood and lumen (and vice versa) and by synthesis and secretion into the lumen. Several low-molecular weight organic molecules achieve high concentration in the epididymal lumen, but their functions in the events of sperm maturation and storage still remain unclear. Metabolic processes occurring within epididymal tissue and the absorptive and secretory activity of the epididymal epithelium are regulated by androgens. The synthesis of some, but not all, secretory proteins is also androgen-dependent. In addition to androgens, other hormones and local testicular factors may influence epididymal function. There is now increasing evidence that epididymal-specific and androgen-dependent secretory proteins play a fundamental role in modifying the surface characteristics of sperm in preparation for the events of fertilization.

Androgen-Binding Protein↗
PubMed1993

Proliferation and triglyceride synthesizing activities of fibroblast-like cells derived from epididymal and subcutaneous adipose tissues of rats.

Fibroblast-like cells from subcutaneous adipose tissue and epididymal adipose tissue were prepared from rats and their proliferation and [14C]deoxy-glucose uptake and triglyceride synthesis from [14C]palmitate were investigated. The proliferation of fibroblast-like cells from subcutaneous adipose tissue was greater than that from epididymal adipose tissue. Insulin enhanced the proliferation of fibroblast-like cells derived from subcutaneous adipose tissue, but not from epididymal adipose tissue. The uptake of [14C]deoxy-glucose by fibroblast-like cells from the two sources was similar. Triglyceride synthesis from [14C]palmitate by epididymal fibroblast-like cells was higher than that by subcutaneous fibroblast-like cells. The [14C]deoxy-glucose uptake and triglyceride synthesis from [14C]palmitate by fibroblast-like cells from the two sources were not enhanced by the addition of insulin. These findings suggest the existence of different types of adipocytes in subcutaneous and epididymal adipose tissues in terms of proliferation, and show that the proliferation of fibroblast-like cells from subcutaneous adipose tissue is regulated by insulin. The triglyceride synthesis by immature adipocytes from both adipose tissues was not affected by insulin.

Adipose Tissue↗
PubMedDate not supplied

Secretion of glycosidases in human epididymal cell cultures.

The dynamics of glycosidase secretion was evaluated in human epididymal cell culture. Epithelial cells from caput, corpus, and cauda epididymis were isolated from tissue obtained from patients undergoing therapeutic orchidectomy due to prostatic carcinoma. The activities of alpha-glucosidase, N-acetylglucosaminidase, beta-glucuronidase, and alpha-mannosidase were analyzed in conditioned culture media. Glycosidase activity was significantly higher in corpus and/or cauda than in caput epididymis. There was a time-dependent increase in enzyme activities that was maximal between 10 and 14 days of culture in all epididymal regions. Epididymal glycosidases are secreted by cultured epithelial cell from human epididymis with an increase toward the distal regions of this organ, which may be related to the dynamics of sperm maturation. Cultures from different epididymal regions may represent a valuable tool to study of human epididymal function.

Aged↗
PubMed2002

Chromosome analysis of epididymal and testicular sperm in azoospermic patients undergoing ICSI.

BACKGROUND: Although ICSI provides a way of treating azoospermic men, concern has been raised about the potential risk for transmission of genetic abnormalities to the offspring. We quantified the incidence of chromosomal abnormalities in epididymal and testicular sperm retrieved from azoospermic patients undergoing ICSI. METHODS: Individual testicular sperm were collected from testicular biopsies with an ICSI pipette, and epididymal sperm were retrieved by microsurgical epididymal sperm aspiration. Samples were processed by fluorescent in-situ hybridization (FISH) for chromosomes 18, 21, X and Y and the results compared with those from normal ejaculated samples. RESULTS: The overall aneuploidy rate of 11.4% in men with non-obstructive azoospermia was significantly higher (P = 0.0001) than the 1.8% detected in epididymal sperm from men with obstructive azoospermia and also the 1.5% found in ejaculated sperm. No significant difference was found between the epididymal and ejaculated samples. When the chromosomal abnormalities were analysed, gonosomal disomy was the most recurrent abnormality in both obstructive and non-obstructive azoospermic patients, while autosomal disomy was the most frequent in ejaculated sperm. CONCLUSIONS: Sperm of non-obstructive azoospermic men had a higher incidence of chromosomal abnormalities, of which sex chromosome aneuploidy was the most predominant. Genetic counselling should be offered to all couples considering infertility treatment by ICSI with testicular sperm.

Adult↗
PubMed2002

The dog as a model to study human epididymal function at a molecular level.

Approaches to study human epididymal functions are limited. Therefore, suitable animal models are highly desirable, yet difficult to find among the few species studied on a molecular level to date. This review summarizes our progress in the development of the canine epididymis as an alternative model. Dogs are biomedically a key species because they are subject to many of the same diseases as humans and already serve as a model for a number of human pathologies, including genetic diseases. It is thus consistent that an appraisal of epididymal specific gene expression has been started in the dog, including the molecular cloning and characterization of canine epididymal proteins. These proteins, in addition to a high overall sequence similarity to the human, show a similar tissue distribution, relative abundance and spatial pattern within the epididymis. Moreover, the dog epididymis offers an excellent source for cell culture studies, and immortalization of the canine epididymal duct epithelium has been achieved, encouraging regulatory studies of epididymal gene expression in vitro. Thus, the dog already fulfils many of the criteria of a good model of the human epididymis on a molecular level. Further progress may be expected with the advance of the canine genome project. If there is a genetic basis for male infertility, then the dog provides the advantage of the exploitation of a species that combines a maximum of genetic variation within a species with the capacity to minimize that variation within a defined pedigree.

Animals↗
PubMed1991

Epididymal sperm aspiration in conjunction with in-vitro fertilization and embryo transfer in cases of obstructive azoospermia.

Epididymal sperm aspiration is a new treatment for vasal agenesis. In previous reports, epididymal spermatozoa resulted in pregnancy by utilizing in-vitro fertilization (IVF) or gamete intra-Fallopian transfer (GIFT). We sought to investigate the efficacy of epididymal sperm aspiration in conjunction with IVF in patients with congenital absence of the vas deferens or with secondary extended obstruction of spermatic ducts. Fifty-eight attempts were performed in 23 patients (25-50 years). Eight patients (34.7%) had vasal agenesis and 14 (60.8%) presented with vasal secondary extended obstruction. The sperm count was adequate (greater than or equal 20 x 10(6)/ml) in 13.8% of sperm retrievals and sperm motility of 20% was obtained in 15.5% of sperm retrievals. Fourteen attempts at IVF were performed with epididymal sperm counts of 2-44 x 10(6)/ml and motilities of 0-45%. A mean of six mature oocytes (0-13) were inseminated in each case. Five embryo transfers were performed in five patients' wives (35.7%) and two couples had an early pregnancy loss (14.2%). Epididymal sperm aspiration is an advance in treating such patients, as an adequate number of mature spermatozoa can be obtained and used for IVF. However, spermatozoa directly aspirated from the proximal epididymis and with fertilizing capacity in vitro, gave a high rate of embryo degeneration (greater than 50%) after embryo transfer.

Adult↗
PubMed2003

Secreted epididymal glycoprotein 2D6 that binds to the sperm's plasma membrane is a member of the beta-defensin superfamily of pore-forming glycopeptides.

The plasma membrane of spermatozoa undergoes substantial remodeling during passage through the epididymal duct, principally because of changes in phospholipid composition, exchange of glycoproteins with epididymal fluid, and processing of existing membrane proteins. Here, we describe the interaction of an epididymal glycoprotein recognized by monoclonal antibody 2D6 with the plasma membrane of rat spermatozoa. Our goals have been to understand more about the mechanism of secretion of epididymal glycoproteins, how they interact with the sperm's plasma membrane, and their disposition within it. Reactivity to 2D6 monoclonal antibody was first detectable in principal cells in the distal caput epididymidis and as a soluble high-molecular-weight complex in the secreted fluid. It was not associated with membranous vesicles in the duct lumen. On cauda spermatozoa 2D6 monoclonal antibody recognized a 24-kDa glycoprotein (the subunit of a disulfide cross-linked homodimer of 48 kDa) that was present on the plasma membrane overlying the sperm tail. Binding of 2D6 to immature spermatozoa in vitro was cell-type specific but not species specific, and the antigen could only be extracted from cauda spermatozoa with detergents. Sequencing studies revealed that the 24-kDa glycoprotein was a member of the beta-defensin superfamily of small pore-forming glycopeptides of which several others (ESP13.2, Bin1b, E-2, EP2, HE2) are found in the epididymis. This evidence suggests that some epididymal glycoproteins are secreted into the luminal fluid in a soluble form and bind to specific regions of the sperm's surface via hydrophobic interactions. Given the antimicrobial function of beta-defensins, they have a putative role in protecting spermatozoa and the epididymis from bacterial infections.

Amino Acid Sequence↗
PubMed2006

HOXBES2: a novel epididymal HOXB2 homeoprotein and its domain-specific association with spermatozoa.

The sperm from the testis acquires complete fertilizing ability and forward progressive motility following its transit through the epididymis. Acquisition of these characteristics results from the modification of the sperm proteome following interactions with epididymal secretions. In our attempts to identify epididymis-specific sperm plasma membrane proteins, a partial 2.83-kb clone was identified by immunoscreening a monkey epididymal cDNA library with an agglutinating monoclonal antibody raised against washed human spermatozoa. The sequence of the 2.83-kb clone exhibited homology to the region between 1 and 1097 bp of the homeobox gene, Hoxb2. This sequence was found to be species conserved, as revealed by RT-PCR analysis. To obtain a full-length clone of the sequence, 5' RACE-PCR (rapid amplification of cDNA ends PCR) was carried out using rat epididymal RNA as the template. It resulted in a full-length 1.657-kb cDNA encoding a 32.9-kDa putative protein. The protein designated HOXBES2 exhibited homology to the conserved 61-amino acid homeodomain region of the HOXB2 homeoprotein. However, characteristic differences were noted in its amino and carboxyl termini compared with HOXB2. A putative 30-kDa protein was detected in the tissue extracts from adult rat epididymis and caudal spermatozoa, and a 37-kDa protein was detected in the rat embryo when probed with a polyclonal antibody against HOXB2 protein. Multiple tissue Western blot and immunohistochemical analysis further indicated its expression in the cytoplasm of the principal and basal epithelial cells, with maximal expression in the distal epididymal segments. Northern blot analysis detected a single approximately 2.5-kb transcript from the adult epididymis. Indirect immunofluorescence localized the protein to the acrosome, midpiece, and equatorial segments of rat caudal and ejaculated human and monkey spermatozoa, respectively. In conclusion, we have identified and characterized a novel epididymal homeoprotein different from HOXB2 protein and hereafter referred to as HOXBES2, (HOXB2 homeodomain containing epididymis-specific sperm protein) with a probable role in fertilization.

Acrosome↗
PubMed1985

Development changes occurring in the lipids of ram epididymal spermatozoa plasma membrane.

Ram spermatozoa were obtained from different regions (caput, corpus, and cauda) of the epididymis and their plasma membrane was removed using a nitrogen cavitation treatment (750 psi, 10 min equilibration at 4 degrees C). Membrane was recovered after sucrose gradient centrifugation and identified using 125I-succinylated concanavalin A (125I-succConA) as a surface marker. Based on fluorescein isothiocyanate-succConA (FITC-succConA) labeling and electron microscopy, cavitation removed plasma membrane from the anterior sperm head in the area overlying the acrosome. Cholesterol was the major sterol in plasma membrane, with desmosterol present in sperm entering the epididymis (caput sperm) but negligible in sperm after epididymal transit (cauda sperm). Ethanolamine and choline phosphoglycerides represented 70-80% of membrane phospholipids, with the ethanolamine fraction decreasing relative to choline phosphoglycerides during epididymal transit. The molar ratio of cholesterol to phospholipid increased in the plasma membrane during maturation. The bulk phospholipid-bound fatty acids consisted primarily of palmitoyl acyl groups (16:0) in caput sperm and docosahexaenoyl acyl groups (22:6) in cauda sperm. The choline phosphoglyceride fraction was purified and analyzed. It consisted of a mixture of ether acyl glycero-3-phosphocholine and diacyl phosphoglyceride, with the dominant acyl residue, at all stages of epididymal maturation, being 22:6 throughout epididymal transit. The significance of these findings relative to acquisition of fertilization capacity by sperm during epididymal maturation is discussed.

Animals↗
PubMed1989

Changes in sperm surface membrane and luminal protein fluid content during epididymal transit in the boar.

The surface membrane protein of boar sperm and the proteins in the fluid surrounding the gametes were analyzed during epididymal transit. The present study demonstrated that sequential dramatic changes occur in protein composition of the sperm membrane and epididymal fluid during epididymal transit. The maturation process of the boar sperm surface was characterized by a complex sequential evolution of the composition and orientation of macromolecules in the sperm membrane. Epididymal maturation resulted in the progressive disappearance of most of the surface testicular compounds, which were either renewed or masked by new permanent or transient low molecular weight polypeptides on the boar sperm surface membrane. In the fluid surrounding the spermatozoa, composition of the luminal proteins was altered throughout the epididymal transit and several new compounds were characterized. Very few proteins were correlated either with blood plasma or sperm surface compounds.

Animals↗
PubMed1989

On the proluminal movement of 3H-androgens across the rat epididymal epithelium.

3H-Androgens in rat epididymal interstitium have previously been shown to move into the epididymal lumen against a concentration gradient. This is true especially in the caput epididymidis. The present investigation used the technique of in vivo epididymal perifusion and tubule micropuncture to demonstrate that the proluminal movement of 3H-androgens is subject to competitive inhibition (unlabeled testosterone in the perifusion fluid at 10 times and 100 times the concentration of 3H-testosterone significantly reduced proluminal movement of isotope) and is not energy-dependent (1 mM 2,4-dinitrophenol in perifusion fluid did not reduce the proluminal movement of isotope). Additionally, dry-mount autoradiography demonstrated high intraluminal concentrations of isotope relative to interstitial concentrations after caput tubule incubation in 3H-dihydrotestosterone (3H-DHT), and showed that the high intraluminal concentrations of isotope were not dependent on the presence of spermatozoa, i.e. proluminal movement of 3H-androgens was not due to binding to intraluminal spermatozoa. Isolation of caput epididymidal sperm on filters followed by 3H-DHT binding experiments also failed to demonstrate the presence of specific binding of this androgen to spermatozoa. Finally, it was confirmed that electrophoresed epididymal lumen fluid contains a single 3H-DHT binding peak that is at its highest concentration in the caput epididymal fluid. These data are consistent with the conclusion that intraluminal androgen-binding protein is an important factor in transepithelial androgen movement.

Androgens↗
PubMed1996

Molecular cloning and characterization of EPI-1, the major protein in chimpanzee (Pan troglodytes) cauda epididymal fluid.

A 27-kDa glycoprotein comprises approximately 20% of the total protein in chimpanzee (Pan troglodytes) cauda epididymal fluid. Polyclonal antibodies generated against this glycoprotein react with 27- and 25-kDa components in chimpanzee cauda epididymal fluid and in human, gorilla, chimpanzee, and monkey seminal fluid. According to microsequencing, the 27- and 25-kDa components (chimpanzee EPI-1) are identical to the cloned putative human epididymal protein HE1. Screening of a chimpanzee epididymal cDNA library enabled isolation of a cDNA clone of chimpanzee EPI-1. On the cDNA level, chimpanzee EPI-1 and human HE1 are 99% identical. Northern analysis localized chimpanzee EPI-1 mRNA to the distal caput epididymidis. With EPI-1 primers, polymerase chain reaction of reverse-transcribed rhesus monkey (Macaca mulatta) epididymal RNA enabled isolation of a rhesus monkey EPI-1 cDNA clone. The derived amino acid sequence of rhesus monkey EPI-1 is identical to chimpanzee EPI-1 and to human HE1. Northern analysis localized rhesus monkey EPI-1 mRNA to the distal caput and the proximal corpus epididymidis. Northern analysis also showed that chimpanzee EPI-1 and rhesus monkey EPI-1 gene products are expressed specifically in the epididymis and not in any other tissue examined.

Amino Acid Sequence↗
PubMed1997

Epididymal maturation of chromatin in spermatozoa from control monkeys (Macaca fascicularis) and those treated with Cetrorelix, a gonadotropin-releasing hormone antagonist.

In order to examine changes in sperm chromatin upon epididymal maturation in the macaque epididymis (Macaca fascicularis), spermatozoa were obtained from six regions of the duct and examined for the state of their chromatin condensation by flow cytometry after staining with acridine orange. To see whether changes were affected by androgens, tissue was obtained from five monkeys treated with the gonadotropin releasing hormone (GnRH) antagonist Cetrorelix. Spermatozoa were recovered from treated and control animals after 16 days (at hemicastration) and another 9 days of treatment. Chromatin condensation of epididymal spermatozoa from controls displayed an increase upon maturation. After 16 days of GnRH-antagonist treatment, spermatozoa in the caput epididymidis displayed greater fluorescence than those from controls, but this was reduced during epididymal transit to values found in the distal epididymal regions of the controls. It is concluded that epididymal chromatin condensation 1) is normal in GnRH-antagonist-treated monkeys as long as sperm are being produced and 2) can compensate for poor testis function so that spermatozoa with normal states of chromatin condensation are found in the distal cauda epididymidis and probably the ejaculate.

Animals↗
PubMed1999

Bovine seminal plasma phospholipid-binding proteins stimulate phospholipid efflux from epididymal sperm.

Several studies have shown that sperm capacitation was accompanied by a change in the lipid composition of the sperm membrane. In cattle, the major proteins of (bovine)seminal plasma (BSP proteins: BSP-A1/A2, BSP-A3, and BSP-30-kDa) potentiate sperm capacitation induced by high-density lipoprotein (HDL). Our recent studies indicate that these proteins and HDL stimulate sperm cholesterol efflux during capacitation. In order to gain more insight into the mechanisms of BSP-mediated sperm capacitation, we studied whether or not BSP proteins induce phospholipid efflux from epididymal sperm membrane. By direct determination of choline phospholipids on unlabeled epididymal sperm, the results show that sperm incubated in the presence of BSP-A1/A2 protein lost 34.4% of their choline phospholipids compared with the control (11.5%). Similar results were obtained using labeled epididymal sperm. Labeling was carried out by incubating washed epididymal sperm for 1 h with medium containing [(3)H]palmitic acid. The majority of the label was incorporated into sperm phosphatidylcholine. Studies of sperm phospholipid efflux were done by incubating the labeled sperm with purified BSP proteins, delipidated BSA, or bovine seminal ribonuclease (RNase, control protein). When labeled ([(3)H]phospholipid) epididymal sperm were incubated with BSP proteins (20-120 microg/ml) for 8 h, the sperm lost [(3)H]phospholipid in a dose-dependent manner (maximum efflux of approximately 30%). After the incubation with BSP proteins, the efflux particles were fractionated by size-exclusion chromatography. Analysis of the fractions obtained showed that the [(3)H]phospholipid was associated with BSP proteins. BSA (6 mg/ml) stimulated a specific phospholipid efflux of approximately 22%. In contrast, bovine RNase (120 microg/ml) did not stimulate phospholipid efflux. These results indicate that BSP proteins participate in the sperm cholesterol and phospholipid efflux that occurs during capacitation.

Animals↗