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PubMed1983

Tubule-containing inclusions in the epithelial cells of the mouse epididymal duct.

The mouse epididymis, consisting of a head, body and tail, was examined by electron microscopy. The principal cells of the epididymal duct in the epididymal body have rod-shaped inclusions, 0.3 to 1.0 microns in diameter and 2 to 5 microns in height. The inclusions contain a bundle of tubules, about 40 nm in diameter, with a wall about 6 nm in thickness. The tubules are regularly arranged in a hexagonal pattern. A goniometric study of the inclusions shows evidence that the wall of the tubules consists of filament-like subunits which run parallel to each other and are inclined at about 25 degrees to the axis of the tubules, forming loose spirals. The inclusions occasionally contain material similar to that in the lysosomal bodies. These inclusions were observed in every epididymis examined, and seem to be related to the specific functions of the principal cells in the epididymal body.

Animals↗
PubMed1984

Appearance of peculiar multivesicular bodies in the principal cells of the epididymal duct after efferent duct cutting in the mouse.

Ligation of the efferent duct in the mouse results in appearance of PAS-positive inclusions in principal cells in the duct of the epididymal body, and the inclusions are considered to be formed by absorption of the luminal PAS-positive material produced in the epididymal head (ABE et al., 1982a). For better understanding of the significance of the inclusions, this study examined morphologic changes in the principal cells after efferent duct cutting, by light and electron microscopy. Electron microscopy revealed that the principal cells containing PAS-positive inclusions are characterized by a nipple-like protrusion--micropapilla--on the luminal surface and by peculiar multivesicular bodies in the supranuclear cytoplasm. The micropapilla, 1-2 micron in height, contains ductules of 0.2-0.5 micron thickness which extends from its tip to the multivesicular bodies. The multivesicular bodies, measuring up to 10 micron in diameter, are larger toward the nucleus. They contain numerous vesicles, 40-100 nm in diameter, and an amorphous material that is similar to the luminal material of the epididymal duct. In addition, larger multivesicular bodies are heterogenous in structure and possess bundles of tubules 40 nm thick. There are dense bodies in the basal cytoplasm under the nucleus which appear to be transformed from the multivesicular bodies. In summary, occurrence of the micropapilla and the giant multivesicular bodies are considered to represent an activated breakdown of the material ingested from the duct lumen.

Animals↗
PubMed1988

Changes in distribution and staining reactivity of PAS-positive material in the mouse epididymal duct after efferent duct ligation.

The distribution of spermatozoa and that as well as the staining reaction of PAS-positive material in the epididymal duct were histologically observed in 60 day-old mice and mice 12 h, 24 h, 2 days, and 7 days after efferent duct ligation at 60 days of age. We divided the mouse epididymal duct into five segments; Segments I, II, and III making up the head of the epididymis, Segment IV the body, and Segment V the tail. The cytoplasm of the principal cells in Segment II was PAS-positive. The lumen of the epididymal duct contained spermatozoa and PAS-positive material in the distal portion of Segment I and other segments distal to Segment I. The lumen in Segments IV and V was distended with abundant spermatozoa and PAS-positive material. After efferent duct ligation, spermatozoa disappeared from the lumen in Segments I, II, and III within 2 days, whereas they took 5 days to pass from Segment IV. As spermatozoa disappeared, the luminal material increased in intensity of the PAS-reaction in the distal portion of Segment I and initial portion of Segment II and Segment IV. Segment I became similar in appearance to Segment II 7 days after the ligation. The findings suggest that the PAS-positive material is produced in the distal portion of Segment I and Segment II and accumulates, in the absence of spermatozoa, at the production site and Segment IV, a storage site of spermatozoa; furthermore, Segment I has the capacity of exerting a Segment II-like function, which becomes distinct after blocking the entrance of the testicular fluid.

Animals↗
PubMed1990

Immunohistochemical localization of 54,000 dalton sialoglycoprotein in the epididymal duct of the germ cell-free W/Wv mouse.

A monoclonal antibody T21 specifically recognizes the mouse epididymal sialoglycoprotein of 54,000 dalton (SGP54). The localization of SGP54 was studied in the epididymal duct of germ cell-free WBB6F1W/Wv mutant mice (W/Wv mice) by avidin biotin complex (ABC) immunohistochemistry using T21. None of the testis cells showed immunoreaction. No spermatozoa were present in the epididymal duct lumen. The duct luminal fluid was stained weakly in the proximal corpus epididymidis, and strongly in the cauda epididymidis. Degenerated cells appeared in the duct lumen. The degenerated cells located at the corpus epididymidis showed strong immunostaining in the cytoplasmic region, while the degenerated cells located at the cauda epididymidis showed weak immunostaining. Immunoreaction was also detected between and on microvilli along the epididymis, the intensity being very strong at the distal caput and proximal corpus epididymidis. Invaginations and coated vesicles at the luminal surface of the principal cells were frequently immunostained at the corpus epididymidis. Giant inclusions frequently occurred in the principal cells of the distal caput and corpus epididymidis, with these being very intensely immunostained. These inclusions are ultrastructurally confirmed to be giant multivesicular bodies reported by ABE et al. (1984) in the mouse with the efferent duct cutting. These results suggest that the majority of excess SGP54 are absorbed by the principal cells at the distal caput to corpus epididymidis and catalyzed in the giant multivesicular bodies.

Animals↗
PubMed2001

Application of computer-assisted sperm analysis system to elucidate lack of effects of cyclophosphamide on rat epididymal sperm motion.

A computer-assisted sperm analysis (CASA) system was used to examine the motion of epididymal spermatozoa derived from cyclophosphamide (CP)-treated male rats. Male rats were orally dosed daily for 1 week with 20 mg/kg of CP. Males were euthanized or were mated 3 times with untreated females at 1 day, 3 weeks, and 8 weeks after the final treatment. Significant decreases in testicular and epididymal weights and epididymal sperm counts of the treated animals were noted after 8-week recovery. Histopathological morphometry of the testis revealed minimal damage to spermatogonia at 1 day after the final treatment and to spermatocytes after 3-week recovery in the CP-treated group. On Caesarian section, increased post-implantation losses were found in females mated with CP-treated males in matings starting 1 day and 3 weeks after the final treatment. On the other hand, none of the sperm motion parameters of treated males derived from the CASA system exhibited significant changes at any time points, although the spermatozoa of treated males at 1 day and 3 weeks after the final treatment were damaged at the DNA level, and the spermatozoa of males after 8-week recovery had been the target cells of CP when they were spermatogonia in the testis. It was thus found that damaged spermatozoa could exhibit no changes on their motion when the damage was confined to the nuclei, and that the effect of CP on sperm nuclei was reversible.

Animals↗
PubMed2006

Influence of various permeating cryoprotectants on freezability of Iberian red deer (Cervus elaphus hispanicus) epididymal spermatozoa: effects of concentration and temperature of addition.

With the aim of finding an ideal cryoprotectant (CPA) in a suitable concentration for red deer epididymal spermatozoa cryopreservation, we evaluated the effects of the 3 most commonly used CPAs, glycerol (GLY), ethylene glycol (EG), and propylene glycol (PG), on sperm cryoresistance. The aim of Experiment 1 was to evaluate the influence of 3 different final concentrations (3%, 6%, and 12%) of each CPA on sperm freezability. Sperm samples were diluted to a final sperm concentration of approximately 400 x 10(6) spermatozoa/mL with a Tris-citrate-fructose-EY extender (TCF) prior to freezing. Sperm cryosurvival was judged in vitro by microscopic assessments of individual sperm motility (SMI), viability, and plasma membrane (by means of the HOS test) and acrosome (NAR) integrities. Thawed samples were incubated at 37 degrees C for 2 hours in the freezing medium. At the end of this incubation period, sperm suspensions were again assessed. Our results showed that 12% of any CPA was toxic to red deer epididymal spermatozoa membrane integrity (P < .05). Moreover, regardless of the level of CPA, results indicated that the cryoprotective effects on red deer epididymal spermatozoa of the 3 CPAs after thawing are in the following sequence: GLY > EG > PG (higher symbols mean P < .001). Furthermore, our results also showed an improvement in sperm parameters when the TCF diluent contained 6% of GLY. In Experiment 2 extenders were prepared using GLY 6%. This experiment was designed to investigate the effect of 2 different temperatures of GLY addition -22 degrees C (ambient temperature) and 5 degrees C- on sperm freezability. Our results showed a differential response (P < .05) of motility (SMI) to temperature of GLY addition before freezing, the best being 22 degrees C (81.94 +/- 2.4% vs 72.38 +/- 2.4%). Although there were no statistically significant differences (P > .05) between the 2 temperatures of GLY addition after thawing in terms of sperm quality, after 2 hours of incubation, results tended to be better when CPAs were added at 22 degrees C. In conclusion, our work showed the efficacy of a TCF diluent with 6% of GLY and its addition at 22 degrees C, as an alternative to the more common 3%-4% of GLY and addition at 5 degrees C, in red deer semen freezing protocols.

Acrosome↗
PubMedDate not supplied

In vivo regulation of rat epididymal proteins by retinoids: analysis by two-dimensional electrophoresis.

The role of retinoids in the regulation of epididymal fluid protein expression was investigated. We compared the patterns of two-dimensional electrophoretic gels of proteins from luminal fluids, cytosols and spermatozoa (from control rats only) of control, retinoid-depleted, retinoid-depleted retinoic acid-complemented and retinoid-depleted testosterone-supplemented rats. This study compared the luminal fluid patterns from the 4 diets and observed 13 proteins whose expression was dependent on nutritional status. Eight were either absent or very weakly expressed in retinoid-depleted animals only, while their presence was obvious in control rats and in the retinoid-deficient retinoic acid- and testosterone-complemented groups. The expression of 8 proteins was greatly enhanced in retinoid-depleted testosterone-supplemented fluids as compared to control fluids. Five of the regulated proteins seemed to be captured by spermatozoa as they were observed in sperm protein patterns of control rats. These results clearly show that the synthesis of several epididymal proteins is influenced by retinoids. Since testosterone-supplemented animals on retinoid-free diet elicited the same response as retinol and retinoic acid ones, testosterone is likely to be the mediator of retinoid action on epididymal protein synthesis. Nevertheless, the observation of one protein whose expression is stimulated by retinoic acid only and is totally independent of testosterone also favors the direct influence of this retinoid.

Animals↗
PubMed1991

Purification and partial characterization of rat epididymal retinoic acid-binding protein, and its immunohistochemical localization.

Two types of retinoic acid-binding proteins, designated as epididymal retinoic acid-binding protein (ERABP) types A and B, have been purified to homogeneity from rat genital organs. ERABP types A and B had molecular weights of 19,000 and 18,500 and isoelectric points of 5.72 and 5.90, respectively. The absorption spectrum of ERABP complex with retinoic acid had two peaks at 277 and 354 nm, and showed similar uncorrected fluorescence spectra to that of cellular retinoic acid-binding protein (CRABP). These ERABPs were identified as major androgen-dependent epididymal proteins by amino acid sequences analyses. Furthermore, immunohistochemical examinations revealed that the ERABPs exist in the epithelium of the proximal portion of the epididymis and in the lumen of epididymal canal and seminal tract leading from the epididymis. The existence of ERABP strongly suggests that retinoic acid might be involved in the maturation of spermatozoa.

Amino Acid Sequence↗
PubMed1982

Morphology of the epididymal region of turkeys producing abnormal yellow semen.

Male turkeys producing abnormal yellow-colored semen (YS) had hypertrophied epithelial cells in the ductuli efferentes. The cells were engorged with cytoplasmic, lipid-like (lipoid) droplets, a morphological abnormality found exclusively in this area of the epididymal region. The testes, epididymal region, ductus deferens, and abdominal fat were relatively yellow compared to turkeys producing normal white semen (WS). Adipose tissue within the abdominal cavity and lining the ductus deferens was more abundant in the YS producers. In addition to increased lipoid droplets, nonciliated cells of the ductuli epithelia contained larger and more numerous electron-dense lysosomal bodies than similar nonciliated cells in WS males. Resorption of morphologically normal and abnormal spermatozoa by the epithelia of the ductuli efferentes was prevalent in the YS males but was not observed in the WS turkeys. The seminal fluids in the epididymal region of the YS males contained abnormal spermatids, cellular debris, and increased amounts of electron-dense proteinaceous material.

Animals↗
PubMed1998

Phospholipid content and lamellar structures in the epididymal epithelial cells of rats treated chronically with lead acetate [Pb(II)].

The electron-microscopic observations accomplished covered epididymal epithelial cells of rats receiving lead acetate for five times longer than the duration of one spermatogenesis. These cells were found to possess a large number of vacuoles and conglomerates containing plicated membranes or tightly packed myelin-like lamellar formations. Further observations also revealed the formation of lamellar structures in mitochondria, dilatation of cisternae in the Golgi apparatus, and increased phagocytosis of spermatozoa by epithelial cells. The presence of a large amount of membranous material correlated with the increased content of phospholipids in epididymal epithelial cells. It may be suggested that the presence of such a great quantity of lamellar structures in epididymal epithelial cells of rats treated chronically with lead is the result of several processes, including the augmented synthesis of membranes associated with encircling the deposits of lead, autophagy in the cells, as well as intensified phagocytosis of spermatozoa.

Animals↗
PubMedDate not supplied

Effects of accessory sex gland fluid on viability, capacitation, and the acrosome reaction of cauda epididymal bull spermatozoa.

The effect of accessory sex gland fluid (AGF) on viability and acrosomal integrity of spermatozoa was examined with cauda epididymal spermatozoa and AGF from the same Holstein bull (n = 6). Surgical cannulation of the vasa deferentia enabled the separate collection of cauda epididymal effluent and AGF from each bull. Cauda epididymal effluent was incubated with either AGF collected from the same bull or medium alone. Following coincubation, spermatozoa (5 x 10(7) sperm/mL) were incubated in medium alone or under capacitating conditions (10 microg/mL heparin) for 16 hours. Every 2 hours, an aliquot of spermatozoa was exposed to lysophosphatidylcholine (100 microg/mL) to induce the acrosome reaction in capacitated spermatozoa. Sperm motility decreased over time regardless of treatment. Overall, spermatozoa incubated in AGF had fewer acrosome-intact live spermatozoa than did those not incubated in AGF. Viability was significantly (P < .05) compromised over time when spermatozoa were exposed to AGF, compared with those not preincubated in AGF. Significantly more (P < .05) acrosome-reacted live spermatozoa were seen following exposure to heparin and lysophosphatidylcholine when spermatozoa were not preincubated in AGF. We conclude that exposure of spermatozoa to AGF accelerates cell death and that rapid removal of spermatozoa from seminal plasma is critical for maximal viability.

Acrosome Reaction↗
PubMedDate not supplied

Identification of maturation-related wheat-germ lectin-binding proteins in the culture of human corpus epididymal epithelial cells.

This study is designed to investigate the synthesis of maturation-related wheat germ agglutinin (WGA) binding glycoproteins in the human corpus epididymal epithelial cells by in vitro culture. Epithelial cells were isolated from the corpus of human epididymides and cultured with RPMI 1640 medium supplemented with 10% fetal calf serum in type IV collagen-coated dishes at 37 degrees C. The epithelial nature, presence of fibroblasts, WGA-binding sites, and existence of GP-83 were determined by an indirect immunocytochemical and histochemical staining technique. Proteins in the cultured cells were analyzed by SDS-PAGE and autoradiography. After culturing for 10 days, the cells were shown to be positive with epithelial cell-specific keratins but devoid of fibroblasts. WGA-binding granules and positive binding sites of GP-83 were also detected in the cytoplasm. Immunoblots of cell extracts probed with the anti-GP-83 antibody from seminal fluid revealed the sperm maturation-related glycoprotein GP-83. The results indicate that WGA-binding proteins may be synthesized by the corpus epididymal epithelial cells of human and GP-83 may play an important role in sperm maturation. This culture model may be suitable for the investigation on the biosynthesis and physiology of human epididymal principal cells in vitro.

Animals↗
PubMed2000

Protein profiles in various epididymal segments of normal and castrated rats.

AIM: Epididymal proteins are known to play an important role in the maturation of spermatozoa. We ought to determine if there are regional differences in androgen-dependent epididymal proteins. METHODS: A group of adult rats was castrated and epididymides were removed three days following castration. The epididymides were dissected into caput, corpus and cauda segments, homogenized, and proteins were fractionated by anion exchange HPLC. Proteins in selected fractions were resolved by SDS-PAGE and visualized by silver staining. RESULTS: It was observed that the levels of multiple proteins drastically reduced in the various regions of epididymis of the orchiectomized rats. CONCLUSION: The epididymal proteins appear to be useful markers to study androgenic action in the epididymis.

Androgens↗
PubMed1998

Bacille Calmette-Guerin (BCG) associated epididymitis: a case report and review.

A case of Bacille Calmette-Guerin (BCG)-associated epididymitis that was non responsive to 6 months of antituberculous therapy, but stable after 2 years, is reported. We review the clinical and pathological features of previously reported cases of pathologically diagnosed BCG-associated epididymitis. Surgery has been the primary treatment for BCG-associated epididymitis in all previous cases.

Journal Article↗
PubMedDate not supplied

Leptin secretion from the epididymal fat pad is increased by the sexual maturation of the male rat.

Although leptin has been implicated as an important factor in triggering the onset of puberty in females, much less is known about the role of this adipose tissue hormone in the sexual maturation of males. Previous work in the rat has suggested that the peripubertal rise in testosterone precedes an increase in leptin secretion, and it has been suggested that the testosterone rise induces the leptin increase. These studies examined some of the interactions between leptin secretion and the peripubertal testosterone rise in male rats. Serum leptin concentrations were significantly elevated in young adult male rats compared with immature rats. Cultured epididymal fat pads obtained from adult animals secreted significantly more leptin than did those obtained from immature rats. Castration of immature rats with or without testosterone replacement for 1 week did not result in a significant change in either the serum leptin concentrations or the ability of the epididymal fat pad to secrete leptin. Exposure of epididymal fat to 5 ng/mL of testosterone in vitro resulted in a significantly enhanced secretion of leptin into the media compared with plain media controls. These results confirmed that there is an increase in serum leptin concentrations with sexual maturation in the male rat. They also suggest that this increase is due to an enhanced ability of adipose tissue to secrete leptin. Within a normal physiologic range, testosterone may play a role in inducing this increased ability to secrete leptin.

Adipose Tissue↗
PubMed2001

Percutaneous epididymal sperm aspiration followed by intrauterine insemination--a new approach to achieve a pregnancy in infertility due to obstructive azoospermia.

Standard approach towards treatment of obstructive azoospermia whether congenital or acquired is mostly microsurgical epididymal sperm aspiration (MESA) and to some extent percutaneous epididymal sperm aspiration (PESA) both being followed by intracytoplasmic sperm injection (ICSI). However in the present series for sperm retrieval in case of obstructive azoospermia the author conducted a series of 55 cases of PESA along with only 4 cases of MESA. The epididymal sperm aspiration (ESA) was followed by intrauterine insemination (IUI) (whenever required quantity of motile sperm was collected) in place of ICSI with full consent of the couples. With the help of this ESA-IUI programme it was possible to achieve reasonable success rate viz, 20% pregnancy rate (PR) per cycle for PESA-IUI and 14.28% for MESA-IUI.

Adult↗
PubMedDate not supplied

Lipid diffusion in the plasma membrane of mouse spermatozoa: changes during epididymal maturation, effects of pH, osmotic pressure, and knockout of the c-ros gene.

It is well known that the plasma membranes of mammalian spermatozoa undergo extensive remodeling during maturation in the epididymal duct. In this investigation, we have used fluorescence recovery after photobleaching (FRAP) techniques to: 1) measure rates of lipid diffusion in the plasma membrane of mouse spermatozoa at different stages of maturation; 2) examine the effects of varying external conditions found in the epididymal duct (pH, temperature, and osmotic pressure) on lipid diffusion in mature sperm; and 3) investigate the effects of the c-ros null mutation that causes tail angulation in cauda spermatozoa after ejaculation as a result of cell swelling due to altered membrane function. Our results show that lipid diffusion (as measured using reporter probes 5-(N-octadecanoyl)aminofluorescein [ODAF] and 2-(6-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)hexanoyl-1-hexadecanoyl-sn-glycero-3-phosphocholine [NBD-C6-PC]) is several times faster across the membrane on the sperm head than on the tail and that it increases significantly during passage from caput to cauda. Temperature variations between 20 degrees C and 37 degrees C have a substantial effect on diffusion coefficients, with the sperm head being more responsive than the tail. Changes in external pH (6.5-8.5) or osmotic pressure (202-389 mOsm/kg), however, have little relative effect on lipid diffusion on any region of the sperm. The rate of diffusion of 22-(N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)-23,24-bisnor-5-cholen-3beta-ol (NBD-cholesterol) is 10-fold higher across the head plasma membrane than across the tail and does not change significantly during epididymal maturation. Similarly, lipid diffusion in hairpin-shaped cauda sperm from c-ros (-/-) males is not significantly different from (+/+) controls. These results suggest that temperature and compositional changes are 2 of the important factors that regulate the dynamics of lipid molecules in the mouse sperm plasma membrane.

4-Chloro-7-nitrobenzofurazan↗
PubMedDate not supplied

Binding of protein D/E to the surface of rat epididymal sperm before ejaculation and after deposition in the female reproductive tract.

The objectives of the present investigation were to study the interaction of protein D/E with the surface of rat epididymal spermatozoa and to assess its topology on the spermatozoa surface before and after deposition in the female reproductive tract. Protein D/E, a member of the cysteine-rich secretory protein (CRISP-1) family, has been proposed to be involved in sperm-egg membrane fusion. In vitro competitive photoactivated cross-linking experiments followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot analysis revealed that protein D/E molecules specifically interact with two surface proteins exhibiting an M(r) approximately 120.0 kd and approximately 130.0 kd, respectively, on the sperm surface. In vitro treatment of epididymal spermatozoa with phosphatidylinositol specific-phospholipase C revealed the release of protein D/E molecules over the head region but not the tail region of spermatozoa. Indirect immunofluorescence experiments using polyclonal antibodies generated against a highly purified protein D/E preparation demonstrated that protein D/E molecules were bound to the surface of spermatozoa recovered from the epididymal and female reproductive tracts, even after 7 hours. These results indicate that protein D/E molecules interact with specific membrane proteins, and is subsequently covalently bound to the surface of spermatozoa via a glycosyl-phosphatidyl inositol linkage. In addition, protein D/E molecules remain covalently bound to spermatozoa after deposition in the female reproductive tract, an observation that is consistent with the proposed physiological function of the protein in the fertilization process.

Animals↗