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PubMed2001

Analysis of reactive oxygen species generating systems in rat epididymal spermatozoa.

Epididymal sperm maturation culminates in the acquisition of functional competence by testicular spermatozoa. The expression of this functional state is dependent upon a redox-regulated, cAMP-mediated signal transduction cascade that controls the tyrosine phosphorylation status of the spermatozoa during capacitation. Analysis of superoxide anion (O2(-.)) generation by rat epididymal spermatozoa has revealed a two-component process involving electron leakage from the sperm mitochondria at complexes I and II and a plasma membrane NAD(P)H oxidoreductase. Following incubation in a glucose-, lactate-, and pyruvate-free medium (-GLP), O2(-.) generation was suppressed by 86% and 96% in caput and cauda spermatozoa, respectively. The addition of lactate, malate, or succinate to spermatozoa incubated in medium -GLP stimulated O2(-.) generation. This increase could be blocked by rotenone and oligomycin (R/O) in the presence of malate or lactate but not succinate. Stimulation with all three substrates, as well as spontaneous O2(-.) production in +GLP medium, was blocked by the flavoprotein inhibitor, diphenylene iodonium. Diphenylene iodonium, but not R/O, suppressed NAD(P)H-induced lucigenin-dependent chemiluminescence. This NAD(P)H-dependent enzyme resided in the sperm plasma membrane and its activity was regulated by zinc and uncharacterized cytosolic factors. Reverse transcription-polymerase chain reaction analysis indicated that the sperm NAD(P)H oxidoreductase complex is quite distinct from the equivalent leukocyte system.

Animals↗
PubMed2002

Expression of aquaporin 9 in the adult rat epididymal epithelium is modulated by androgens.

Reabsorption of fluid and solutes across the epithelium lining the male excurrent duct is important for adequate sperm maturation, concentration, and storage. Water channels contribute to water movement across epithelia in many tissues. Aquaporin 9 (AQP9) is abundantly expressed in the apical membrane of principal cells that line the epididymis, and in reabsorptive and secretory epithelial cells of the male reproductive tract. In this study we show that the nonsteroidal antiandrogen flutamide, given to adult rats at a dose of 50 mg x kg(-1) x day(-1) for 2 wk via osmotic minipumps significantly decreased the amount of AQP9 in the epididymis. This down-regulation was observed by immunofluorescence of cryostat tissue sections and by Western blotting of epididymal brush border membrane preparations. In addition, castrated adult rats showed lower levels of epididymal AQP9 compared with adult controls, whereas systemic testosterone treatment of castrated adult rats induced a recovery of the expression of AQP9 to control levels. These data indicate that the expression of AQP9, a likely candidate for apical transepithelial fluid and solute transport in several regions of the male reproductive tract, is modulated by androgens in the adult rat epididymis.

Androgen Antagonists↗
PubMed2002

Rabbit epididymal secretory proteins. II. Immunolocalization and sperm association of REP38.

Polyclonal antibody was used to partially characterize REP38, a major rabbit epididymal secretory protein. Western blot analyses and immunohistochemistry indicated that REP38 is only expressed in regions 5 and 6 of the epididymis (corpus epididy-midis) and is localized in the supranuclear region and microvilli of the principal cells in these regions. It was not expressed in other tissues of the body. In region 8 (cauda epididymidis), REP38 was detected in the luminal border and cytoplasm of scattered principal cells, indicating that it may be reabsorbed in this region. This protein accumulated on the sperm plasma membrane downstream of region 5 and was localized predominantly over the acrosomal and postacrosomal regions of the head and the middle piece. Although tightly bound to epididymal sperm, REP38 migrated to the equatorial segment under conditions in vivo that would promote capacitation. When tested in vitro, anti-REP38 IgG reduced the percentage of ova fertilized in a concentration-dependent manner, apparently by blocking sperm-egg fusion.

Animals↗
PubMed2002

Rabbit epididymal secretory proteins. III. Molecular cloning and characterization of the complementary DNA for REP38.

REP38 is a rabbit epididymal secretory protein of 38 kDa that has recently been shown to interact with spermatozoa. A rabbit epididymal cDNA expression library was screened with a polyclonal antibody raised against REP38. A single clone (REP38-c1) with an open reading frame encoding a polypeptide of 666 amino acids was obtained. Cleavage of a 22-amino acid N-terminal signal peptide revealed a mature protein with a theoretical molecular mass of 74.5 kDa. Northern blot analysis revealed the presence of two cross-hybridizing transcripts of approximately 1.3 and 2.5 kilobases that appear to result from alternative mRNA splicing. This finding may explain the discrepancies between the observed (38 kDa) and deduced molecular mass of REP38. Expression of both transcripts was epididymis specific and was detected only in regions 2-6. During development, the expression of REP38-c1 mRNA was initiated between 1 and 2 mo postnatum and therefore precedes the appearance of sperm within the lumen of the epididymis. These findings are in agreement with the immunohistochemical localization of the REP38 protein. Androgen deprivation induced by orchidectomy reduced REP38-c1 mRNA levels below the limit of detection, an effect that was reversed by administration of exogenous testosterone. Although REP38-c1 mRNA was detected only in the rabbit epididymis, database searches indicated homology with two rat testis specific cDNAs, KTT4 and odf2, which encode sperm outer dense fiber proteins.

Amino Acid Sequence↗
PubMed1982

A direct effect of alpha-chlorohydrin on rat epididymal spermatozoa.

The effect of alpha-chlorohydrin (alpha-CH) on rat epididymal spermatozoa was studied in vivo and in vitro. Alpha-CH was injected sc in doses of 5 and 20 mg daily for 16 days. The 20 mg dose resulted in diminished epididymal spermatozoal content (8 +/- 4 vs. 44 +/- 5 million, m +/- SE, n = 5) and motility (13 +/- 7 vs. 74 +/- 4%) as compared to saline injected-controls. Fertility rates were significantly reduced; control-100% (5/5), 5 mg - 25% (1/4), 20 mg - 0% (0/4). Alpha-CH was added to suspensions of spermatozoa in vitro and a level of 132 micrograms/ml depressed motility by 90% (P less than 0.0001) and O2 consumption by 40% (P less than 0.05). Intrauterine insemination of in vitro treated spermatozoa was performed in 61 pro-oestrous rats. Alpha-CH treated spermatozoa (from 5.3 to 26.400 micrograms/ml) were found to be completely infertile compared to untreated spermatozoa which showed a 63% fertility rate. There was almost complete absence of oocytes in the flushed ampullas of recipients of alpha-CH treated sperm, in the lowest dose which did not affect sperm motility. Thus, alpha-CH has direct effect upon spermatozoal function and also has a possible effect on the female reproductive tract.

Animals↗
PubMed1983

Influence of hypothyroidism on epididymal enzymes involved in carbohydrate metabolism. Studies in pubertal and adult rats.

The influence of thyroidectomy on key epididymal enzymes of the Embden-Meyerhof and pentose phosphate pathway have been studied in pubertal and adult animals in relation to the serum hormone profile. Age related differences in the response of epididymal segments were observed with respect to hexokinase activity, although the other 2 key enzymes of the Embden-Meyerhof pathway (6-PFK and PK) were suppressed in all regions of the epididymis in both pubertal and adult rats. The enzymes involved in the pentose phosphate pathway (G-6-PDH and 6-PGDH) remained unaltered. The serum hormone profile revealed that while FSH and testosterone titres were reduced, LH and Prl were unaltered. Replacement of T4 in thyroidectomized animals maintained serum hormone levels and the activities of the enzymes studied at control levels. It is inferred that thyroid hormones may be one part of a complex mechanism that controls carbohydrate metabolism in the epididymis.

Animals↗
PubMed1984

Strain differences in the concentration, motility and morphology of epididymal sperm in relation to puberty in mice.

Changes in the concentration, motility and morphology, of epididymal sperm have been evaluated in males of between 40 and 100 days of age in BALB, CBA, C3H and C57BL strains of mice. Particular attention was paid to sperm morphology, and a multiple entry classification system was used for its quantitation. At 40 days in each of the 4 strains studied sperm were few in numbers with poor motility and highly atypical morphology, particularly in the head region. From 80 days of age values for the 3 parameters were within the normal range. At equivalent ages during puberty the 4 strains differed in the concentration and motility of epididymal sperm, indicating difference in the time of onset of puberty between the strains. However, once adulthood was reached the strains differed only in the percentage of normal forms and in the frequency distribution of sperm with the various morphological abnormalities.

Aging↗
PubMed1986

Forward motility protein (FMP): localization in hamster epididymal spermatozoa.

The presence of FMP was investigated by immunocytochemistry in spermatozoa from the hamster caput and cauda epididymis. Spermatozoa from the caput showed no staining whereas spermatozoa pre-incubated with FMP were stained on the acrosome. Pre-treatment of the same sperm with epididymal plasma induced staining on the principal piece of the flagellum. Spermatozoa from the cauda were stained without previous incubation both on the acrosome and on the principal piece of the flagellum. These results suggest that the action of FMP, which prevents head-to-head agglutination of motile spermatozoa and allows acquisition of forward motility, may be due to at least two proteins. The first localizes to the acrosome during epididymal transit (anti-sticking factor), whilst the second localizes to the principal piece of the flagellum (forward motility initiation factor).

Acrosome↗
PubMed1990

Improvement in the assessment of human epididymal function by the use of inhibitors in the assay of alpha-glucosidase in seminal plasma.

Seminal alpha-glucosidase has been used clinically as a marker of epididymal function. In this study enzyme inhibitors were used to increase the specificity of the human seminal alpha-glucosidase assay and improve its diagnostic value as an indicator of distal epididymal occlusion in cases of azoospermia. Sodium dodecylsulphate was added to the sample to eliminate the interfering acid isoenzyme secreted by the prostate gland, and castanospermine was used with semen pools to provide a semen blank for the assay by eliminating non-glucosidase-regulated degradation of the substrate. With both inhibitors included in the assay, glucosidase activity in semen samples from 17 fathers was measured to provide reference values for the clinic (lower threshold 18 mU per ejaculate). With the improved assay glucosidase was non-detectable in 8 out of 11 cases of proven and 5 out of 8 cases of suspected ductal obstruction; other azoospermic patients with distal occlusion had values below 11 mU per ejaculate.

Acarbose↗
PubMed1994

Affinity sites for N-acetyl-beta-D-glucosaminidase on the surface of rat epididymal spermatozoa.

The binding of N-acetyl-beta-D-glucosaminidase from rat epididymal fluid to the surface of spermatozoa from the cauda epididymis was measured in the presence of sugars, its phosphorylated derivatives, or after treatment of the cells or the enzyme with agents that alter the integrity of proteins or carbohydrates. The binding was saturable, with a Kd in the nanomolar range, was inhibited with phosphorylated derivates of fructose, and did not depend on Ca2+, showing that it is different from the mannose 6-P-recognizing system existing in other tissues for this and other acid hydrolases. Treatment of the cells with sodium periodate or trypsin inhibited the binding, showing that a glycoprotein of the plasmalemma is involved in the affinity site. Fructose or phosphorylated derivates were not detected in the proteins of the epididymal fluid with HPLC. However, with the method used, the presence of these compounds cannot be ruled out, if among the proteins of the fluid there are only a small number of acid hydrolases containing this sugar.

Acetylglucosaminidase↗
PubMed1994

Influence of hypothyroidism induced at prepuberty on epididymal lipids and the number and motility of spermatozoa in rats.

Fifteen prepubertal male rats (age 30 days) were divided into three groups of five each: Group 1, hypothyroid (Tx)--rats were thyroidectomized at day 30; Group 2, T4 (L-thyroxine) replacement therapy (Tx+T4)--rats were thyroidectomized at day 30 and treated daily i.m. with T4 (6 micrograms/100 g body weight/day) for 30 days from day 31 to day 60 post-thyroidectomy (age 90 days); Group 3, control--rats were sham-operated and treated with vehicle. The rats from all groups were killed on day 61 post-thyroidectomy or post-sham operation (age 91 days). The serum levels of testosterone, T4 and T3 decreased in the Tx group (p < 0.001). In the Tx+T4 group the levels of T4 and T3 were restored to control values, whereas testosterone levels remained lower than in the control group. Hypothyroidism caused various changes in the levels of epididymal phospholipids and neutral lipids. These were restored differentially or were altered further in the Tx+T4 group. The number and forward motility of spermatozoa, recovered from the cauda epididymis, were decreased significantly (p < 0.01) in the Tx group and were not restored in the Tx+T4 group. This study shows that chronic hypothyroidism, induced at prepuberty and continued for 60 days, causes various changes in the lipid composition of the caput and cauda epididymis and lowers the quality and quantity of spermatozoa in the cauda epididymis. T4 therapy for 30 days, especially during the postpubertal period, did not restore the quality or quantity of spermatozoa and caused differential changes in the levels of epididymal lipids, depending upon the region.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1990

Stimulation of Ca2+ uptake into epididymal bull spermatozoa by analogues of amiloride.

Certain amiloride analogues 3',4'-dichlorobenzamil 2',4'-dimethylbenzamil and alpha',2'-benzobenzamil hydrochloride (ATBB) stimulate calcium accumulation and motility by epididymal bovine spermatozoa. This stimulation can be seen at a range of 0.1-0.4 mM, while at higher concentration there is inhibition of calcium uptake by these amiloride analogues. The amiloride derivative 5-(4-chlorobenzyl)-2',4'-dimethylbenzamil (CBDMB), which bears a 4-chlorobenzyl substituent on the 5-amino nitrogen atom, did not stimulate calcium uptake. The amiloride analogue 3',4'-dichlorobenzamil inhibits the Na+/Ca2(+)-exchange activity in isolated plasma membrane vesicles, and the stimulatory effect of 3',4'-dichlorobenzamil on calcium uptake into epididymal sperm could be seen in Na(+)-free medium. Thus, the stimulation of Ca2+ accumulation in the cells caused by 3',4'-dichlorobenzamil is not a result of inhibiting the Na(+)-dependent Ca2+ clearance. There is no stimulation of Ca2+ uptake into ejaculated cells by adding 3',4'-dichlorobenzamil, which is not due to the presence of the calcium-transport inhibitor (caltrin) in these cells [Rufo, G.A., Schoff, P.K. & Lardy, H.A. (1984) J. Biol. Chem. 259, 2547-2552]. The stimulatory effect of 3',4'-dichlorobenzamil on Ca2+ uptake is inhibited by the voltage-dependent Ca2(+)-channel blockers nifedipin and diltiazem. This indicates that the stimulation of Ca2+ uptake by the amiloride analogues is due to the activation of a voltage-dependent Ca2+ channel of the plasma membrane.

Amiloride↗
PubMed1994

Isolation and characterization of a small putative zinc finger protein from cuttlefish epididymal sperm cells.

At the end of spermiogenesis, sperm chromatin stabilization is ensured by protamine dephosphorylation and, in mammals, by the formation during epididymal transit, of intra- and inter-molecular disulfide bridges between protamines. In cuttlefish, the nuclear protein transition histones-->spermatid-specific protein T-->protamine Sp is very similar to that occurring in mammals during spermiogenesis. However, in cuttlefish, the protamine Sp is devoid of cysteine residues. The protein complement of cuttlefish epididymal sperm nuclei has been investigated. A minor basic protein, called protein E, has been isolated. Its primary structure was established from sequence analysis and mass spectrometry data of the protein and its fragments. Protein E contains a motif -Cys-Xaa2-Cys-Xaa23-His-Cys-Xaa2-Cys- which is likely to adopt a zinc finger conformation. Reduced protein E does fix zinc whereas alkylation of cysteine residues abolishes this ability. The sequence of protein E does not correspond to that of any known protein, but presents some similarities with a part of ZFY protein, a putative human transcription factor specifically expressed in germinal cells and which could be involved in spermatogenesis.

Amino Acid Sequence↗
PubMedDate not supplied

Epididymal resorption of spermatozoa in the field rat (Millardia meltada).

A study has been made of epididymal resorption of spermatozoa in the field rat (Millardia meltada). At the height of its reproductive activity, many spermatozoa penetrate the epididymal epithelium and intertubular tissue where they undergo fragmentation and resorption. Sperm disposal is maximum in the cauda epididymidis.

Animals↗
PubMedDate not supplied

Epididymal sperm reserve in Buffalo-bulls (Bubalus bubalis).

Epididymal sperm reserve was determined in 6 sexually mature fertile buffalo-bulls having normal process of spermatogenesis. The relative distribution of spermatozoa in the caput, corpus and cauda epididymidis averaged 5.42, 0.75 and 11.45 billion respectively. Total epididymal sperm reserve per bull averaged 36.2 billion. In terms of percentage the caput, corpus and cauda epididymidis contained 30.76, 4.25 and 64.99 per cent sperm respectively.

Animals↗
PubMedDate not supplied

Flutamide as an androgen antagonist on epididymal function in the rat.

The purpose of this study was to investigate whether flutamide (alpha-alpha-alpha--Trifluro-2-methyl-4'-nitro-m-propionatoluidide), a nonsteroidal compound acts as an androgen antagonist at the level of the epididymis. For comparison, cyproterone acetate was also evaluated under identical experimental conditions. The levels of glycerylphosphorylcholine (GPC), sialic acid, total phospholipids were used as functional indices of epididymis and, in addition, weights of the accessory sex organs were recorded. Adult male rats castrated and maintained on testosterone therapy (TP: 250 microgram/rat: i.m.) were treated with flutamide (25 mg/kg, oral) or cyproterone acetate (25 mg/kg, s.c.). Castration caused a reduction in the weight and secretory activity of the epididymis which was restored to near normal following TP replacement therapy. GPC level was found to be the most sensitive index of epididymal secretory function. The two antiandorgens antagonised the action of TP on all the accessory sex organs. These findings are discussed in relation to our previous study which demonstrated the lack of effect of flutamide on the epididymal function of intact rats.

Anilides↗
PubMedDate not supplied

Evidence for the reconstitution of motility by epididymal plasma-protein factor(s) in immotile washed spermatozoa from goat cauda epididymis.

Approx. 90% of the highly motile goat cauda-epididymal spermatozoa lose motility completely due to removal of the surrounding epididymal plasma (EP) by washing with a modified Ringer's solution. Motility can however, be reconstituted in approx. 80% of these washed cells that lost motility during washing, with the addition of goat cauda-EP. The activity of the EP-factor(s) that cause reconstitution of motility in the washed immotile spermatozoa, is nondialysable and sensitive to the action of trypsin. The activity of the factor(s) is not dependent on exogenous Ca2+ (1 mM), Mg2+ (1.2 mM), cyclic AMP (5 mM) or dibutyryl cyclic AMP (5 mM). The novel system may thus serve as an excellent analytical tool to yield an insight into the molecular basis of the regulation of spermatozoal motility.

Animals↗
PubMedDate not supplied

Occurrence of specific glycoprotein factor(s) in goat epididymal plasma that prevent adhesion of spermatozoa to glass.

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.

Animals↗