There are over 200 secretive proteins in the epididymis. Spermatozoa are generally considered to become mature and full-functional after interacting with secretive proteins in the epididymis. This review is aimed at summarizing some aspects of the biochemical, molecular and functional characterization of some new proteins recently detected in human epididymis, and is expected to contribute to further researches on the mechanism of epididymal reproduction and contraception.
Epididymis ; secretion ; Humans ; Male ; Proteins ; metabolism ; Spermatozoa ; metabolism ; Sugar Alcohol Dehydrogenases ; metabolism

OBJECTIVESTo detect the changes of DNA ploidy of spermatogenic cells in testis and epididymis.

METHODSRight epididymides and testes from 15 fertile youth donors who died of accident were collected. Samples of spermatogenic cells in different regions of epididymis (caput, corpus and cauda) and tests were collected. DNA of spermatogenic cells were detected by flow cyctometry (FCM).

RESULTSThe haploid(1n), diploid(2n) and tetraploid(4n) spermatogenic cells were existed in different regions of epididymis and testis. The 1n cells increased from (24.87 +/- 7.28)% in testis to (96.33 +/- 1.58)% in epididymis cauda, there were significant differences among regions of testis and epididymis caput, corpus(P < 0.01), and the difference among regions of epididymis corpus and epididymis cauda were also significant(P < 0.05). While the percentages of 2n and 4n cells decreased from (63.07 +/- 8.96)% and (9.43 +/- 3.83)% in tesits to (2.47 +/- 0.93)% and (1.17 +/- 0.95)% in epididymis respectively. There was significant difference of 2n cells between testis and epididymis caput, corpus(P < 0.01), and was also remarkable difference between epididymis corpus and cauda (P < 0.05). There was no difference of 4n cells between testis and epididymis caput(P > 0.05). There were significant difference among regions of epididymis caput, corpus and cauda(P < 0.05).

CONCLUSIONSThe percentage of immature spermatogenic cells decreased along with passing through the epididymis.

Adult ; DNA ; analysis ; Epididymis ; metabolism ; Flow Cytometry ; Humans ; Male ; Spermatogonia ; metabolism ; Testis ; metabolism

OBJECTIVETo investigate the expression and the role of nitric oxide synthase (NOS) in the testis and epididymis of macaca fascicularis.

METHODSThe immunohistochemical ABC method was used to observe the localization of nitric oxide synthase in the testis and epididymis of the macaca fascicularis.

RESULTS(1) nNOS immunoreactivity was found in the spermatogenic cells of seminiferous tubules, the epithelia of epididymal efferent ducts, sperm and the endothelia of blood vessels; (2) iNOS was expressed in the epididymal efferent duct, the sperm inside the duct, and the myoid cells and endothelia of blood vessels; (3) eNOS immunoreactivity was detected in the interstitial cells of the testis, the epididymal efferent duct, the sperm inside the duct, and the myoid cells and endothelia of blood vessels.

CONCLUSIONNOS is extensively expressed in the testis and epididymis of the macaca fascicularis and it may play an important role in such processes as spermatogenesis, sperm maturation and testosterone secretion.

Animals ; Epididymis ; metabolism ; Immunohistochemistry ; Macaca fascicularis ; Male ; Nitric Oxide Synthase ; biosynthesis ; physiology ; Testis ; metabolism

OBJECTIVETo identify the specific protein in the epididymal luminal fluid that may play a role in sperm epididymal maturation or modification on the surface of spermatozoa.

METHODSWe compared the differential protein components in the lumen fluids from the caput and cauda segments of the epididymis of normal rats as well as from the cauda segment of experimental left varicocele (ELV) rats by SDS-PAGE or 2D-electrophoresis. The protein spots of interest were selected for MS identification, and the target proteins further characterized by immuno-blot assay.

RESULTSMS analysis showed that one of the most prominent proteins, M(r) 22 000, was identical to the phosphatidylethanolamine-binding protein (PBP), and it was further identified as PBP by immuno-blot assay.

CONCLUSIONPBPs were present in a variety of molecular forms in the epididymal luminal fluid, including the glycosylated form, and ELV markedly elevated the PBP level in the cauda luminal fluid of the rats. Thus, the association of this molecule with sperm surface modification remains an interest for future investigation.

Animals ; Disease Models, Animal ; Epididymal Secretory Proteins ; isolation & purification ; Epididymis ; metabolism ; Male ; Rats ; Varicocele ; metabolism

Human epididymis protein 4(HE4) is a secretory glycoprotein found in human distal epididymis epithelial cells. It is often used in the early diagnosis, efficacy evaluation and monitoring of ovarian cancer, and also has been considered as an effective serum marker for many other types of cancer. However, its function in the process of sperm maturation is not fully unknown. The maturation of sperm in epididymis is characterized by the acquisition of motility and fertilization. As a member of the whey acid protein (WAP) family, several studies proposed the importance of HE4 in the maturity of sperm in epididymis. This article reviews the effect of HE4 on spermatozoa maturation in epididymis, which provides basis for the evaluation of male reproductive ability, early detection, early diagnosis and pathogenesis of male infertility.
Epididymis/metabolism* ; Humans ; Male ; Semen ; Sperm Maturation ; Sperm Motility ; Spermatozoa/metabolism*

Lectins are glycoproteins of plant and animal origin that have the ability to bind specific carbohydrate residues of cell glycoconjugates, particularly in terminal positions. In this study, the binding of lectins, Dolichos biflorus agglutinin (DBA), soybean agglutinin (SBA), Bandeiraea simplicifolia BS-1 (isolectin B4), Triticum vulgaris (WGA), Arachis hypogaea (PNA), and Ulex europaeus (UEA-I), was studied in the reproductive systems of male thoroughbred horses.DBA was detected in the stereocilia of the caput and corpus epididymis, and in the vas deferens. It was weakly detected in connective tissue of the corpus epididymis. Strong SBA staining was seen in epithelial cells in the testis, stereocilia of the corpus and cauda epididymis, and in the vas deferens. There were intense positive reactions for isolectin B4 in interstitial cells in all tissue and serosa of the vas deferens. PNA staining was seen only in stereocilia in the caput and corpus epididymis, and in the vas deferens. Strong WGA staining was seen throughout the testis, except in Sertoli cells, stereocilia, and connective tissue. UEA-I was detected in secondary spermatids, stereocilia, and epithelial cells of the cauda epididymis.These results show that degenerating cells in the testis, epididymal tubules, and vas deferens have differential affinities for lectins, and suggest that lectins play a role in the reproductive system of the horse. The heterogeneity of the lectin staining pattern in the reproductive tubules of adult horses suggests that the carbohydrate composition of each cell type is region specific.
Animals ; Epididymis/cytology/*metabolism ; Horses/*metabolism ; Immunohistochemistry/veterinary ; Lectins/*metabolism ; Male ; Testis/cytology/*metabolism ; Vas Deferens/cytology/*metabolism

OBJECTIVETo investigate the effects of experimental varicocele on mitochondria calcium and cytochrome C of the epididymal cells in adolescent rats.

METHODSForty male adult Wistar rats were divided into two groups randomly: varicocele group (VG) and sham operation group (SOG) by partial ligation or exposure of the left renal vein. Bilateral epididymides were removed after ten

RESULTSThe content of mitochondria weeks. Mitochondria calcium and cytochrome C levels of the epididymal cells were detected. calcium decreased (P < 0.001 ) while that of cytochrome C increased (P < 0.05) markedly in the experimental group compared with SOG.

CONCLUSIONCalcium dyshomeostasis and mitochondrial damage of the epididymal cells caused by varicocele may play an important role in leading to subfertility.

Animals ; Calcium ; metabolism ; Cytochromes c ; analysis ; Epididymis ; metabolism ; Infertility, Male ; etiology ; Male ; Mitochondria ; metabolism ; Rats ; Rats, Wistar ; Varicocele ; metabolism

OBJECTIVETo investigate the expressions of leptin and its receptor in the epididymis of experimental varicocele (EV) rats.

METHODSForty male Sprague-Dawley rats were randomly divided into four groups: 4-week EV (n = 12), 8-week EV (n = 12), 4-week control (n = 8), and 8-week control (n = 8). EV models were established by partial ligation of the left renal vein. The expressions of leptin and its receptor in the rat epididymis were measured by immunohistochemistry, and their mRNA expressions determined by real-time quantitative PCR.

RESULTSThe expressions of leptin and its receptor in the epididymis were significantly higher in the 4- and 8-week EV groups than in the 4- and 8-week control groups (P < 0.01), with no significant difference between the two EV groups (P > 0.05). So were their mRNA expressions in the former two than in the latter two groups (P < 0.01), with no significant difference between the former two (P > 0.05).

CONCLUSIONThe expressions of leptin and its receptor are markedly increased in the epididymis of varicocele rats. Leptin may be involved in the mechanisms of varicocele inducing male infertility.

Animals ; Disease Models, Animal ; Epididymis ; metabolism ; Leptin ; metabolism ; Male ; Rats ; Rats, Sprague-Dawley ; Receptors, Leptin ; metabolism ; Varicocele ; metabolism

OBJECTIVETo study the expression and regulation of heat shock protein 90β (HSP90β) in the testis, epididymis and sperms of mice.

METHODSThe localization and expression of HSP90β mRNA and protein were investigated in the testis, epididymis and sperms of mice, and the regulation of HSP90β in the male reproductive system was explored.

RESULTSHSP90β was expressed at a higher level in the epididymis than in the testis. In the sperms of the mice, HSP90β was localized in the acrosome area. The expression of HSP90β in mouse epididymis decreased after castration and recovered the normal level after testosterone treatment. HSP90β expression in the testis and epididymis also underwent changes during the postnatal development of the mice.

CONCLUSIONHSP90β may play an important role in spermiogenesis and fertilization, and its expression pattern in the epididymis after castration and during the postnatal development suggests its regulation by hormones and development.

Animals ; Epididymis ; metabolism ; HSP90 Heat-Shock Proteins ; metabolism ; Male ; Mice ; Mice, Inbred Strains ; Spermatozoa ; metabolism ; Testis ; metabolism

OBJECTIVETo evaluate the correlation of neutral alpha-glucosidase in seminal plasma with the location of epididymal obstruction in azoospermia men.

METHODSWe detected neutral alpha-glucosidase activity in the seminal plasma of 59 men with obstructive azoospermia followed by determining the location of epididymal obstruction by scrotal exploratory surgery. Then we analyzed the correlation between neutral alpha-glucosidase and the location of epididymal obstructive azoospermia.

RESULTSAmong the total number of patients, there were 25 cases of bilateral cauda epididymal obstruction, 15 bilateral corpus, 12 bilateral caput, 4 unilateral caput-opposite cauda, and 3 unilateral corpus-opposite cauda. The neutral alpha-glucosidase levels in the seminal plasma of bilateral cauda, corpus and capus epididymal obstructions were (4.1 +/- 1.9), (13.8 +/- 4.4) and (46.8 +/- 19.3) mU per ejaculate, respectively, with statistically significant differences among the three groups (P < 0.05).

CONCLUSIONNeutral alpha-glucosidase activity is significantly correlated with the location of epididymal obstruction in azoospermia men, which helps to locate epididymal obstruction, evaluate surgical prognosis and reduce the time of scrotal exploratory surgery.

Adult ; Azoospermia ; enzymology ; pathology ; Epididymis ; pathology ; surgery ; Humans ; Male ; Semen ; enzymology ; alpha-Glucosidases ; metabolism