Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Antiserum against rat androgen-dependent secretory epididymal protein DE (raised in rabbit) was added to suspensions of rat spermatozoa from the cauda epididymidis which were used for artificial insemination. While control spermatozoa fertilized 41.6% of oocytes, those exposed to antiserum to protein DE fertilized only 6.6% (P less than 0.01). An equal amount of normal rabbit serum (NRS) did not cause inhibition (33.1%). To study the entry of antibodies into the epididymis, caudal tubules were cultured for 24 h and the fertility of the contained spermatozoa was assessed by artificial insemination. Culture in Medium 199 alone or with NRS resulted in spermatozoa which fertilized 52% of oocytes while the presence of antiserum to protein DE in the culture medium yielded spermatozoa which fertilized only 16.6% of oocytes (P less than 0.01). These results suggest (1) that the epididymal protein DE might be part of a sperm structure involved in the fertilization process, and (2) that, at least under the present culture conditions, immunoglobulins penetrate the epididymal epithelium in sufficient numbers to reduce fertility significantly.
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PMID:Antibodies against epididymal glycoproteins block fertilizing ability in rat. 639 45

A rat epididymal protein (MW 32000) was isolated and purified from the rat caudal epididymal fluid. Mono-specific antiserum against this protein was raised in rabbits, purified and labelled with 125I. The labelled IgG was infused intravenously into anaesthetized male rats, and the transfer of the labelled IgG across the luminally perfused cauda epididymidis was studied. It was found that during the 2 h infusion period, radioactivity in blood rose, but no radioactivity could be detected in the perfusates, irrespective of whether the epididymis was perfused with Krebs bicarbonate solution or a solution which resembled the rat caudal fluid in ionic composition. In some experiments, rats were given a single intravenous injection of labelled IgG and radioactivity in the epididymal content was measured 10 days later. It was found that despite a high IgG level in blood and liver, no radioactivity could be detected in epididymal fluid and sperm. It is concluded that the blood-epididymis barrier restricts the passage from blood to lumen, an immunoglobulin directed against an epididymal protein.
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PMID:Restricted entry of an anti-rat epididymal protein IgG into the rat epididymis. 641 28

The fertility of spermatozoa from the different epididymal segments of hamsters was tested by in-vivo insemination. Caput and proximal corpus spermatozoa were non-fertile; spermatozoa from the distal corpus epididymidis fertilized 13% (38/290) oocytes and those from the proximal and distal cauda epididymidis 71 and 87%, respectively. When tested by in-vitro insemination, distal corpus spermatozoa penetrated 44% of oocytes while those from the distal cauda fertilized 87% of oocytes. Spermatozoa from the distal corpus recovered in Medium BMOC fertilized 13% (28/219) of oocytes in vivo, while those mixed with an epididymal protein preparation (0.8 mg protein/ml) fertilized 24% (49/204; P less than 0.01) of oocytes. When distal corpus spermatozoa were inseminated in vivo with 0.8 mg epididymal protein preparation 34% (31/90) oocytes were fertilized and only 22% (23/103; P less than 0.05) oocytes were fertilized when the proteins were obtained from epididymides of animals castrated for 30 days. When distal corpus spermatozoa were preincubated for 5 h in medium without (control) or with protein preparation (0.8 or 1.6 mg protein/ml), a significant increase in in-vitro oocyte penetration was found (25 compared with 45%; P less than 0.05) when the protein was present at 1.6 mg/ml. These results confirm and extend previous observations suggesting a role for androgen-dependent glycoproteins secreted by the epididymis in the acquisition of fertilizing ability that occurs during sperm maturation.
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PMID:Addition of an androgen-free epididymal protein extract increases the ability of immature hamster spermatozoa to fertilize in vivo and in vitro. 674 52

Functional development of the sex accessory tissues was studied in the male rat. Three potentially crucial developmental periods (neonatal, prepubertal and pubertal) were examined, and then the functional integrity of the accessory tissues was investigated in the adult, when the animals would have been expected to display normal function. Four accessory tissues (the seminal vesicles, ventral prostate and caput and cauda epididymides) were used because of their different embryological origins and responses to androgens in the adult. Synthesis and secretion of previously characterized tissue-specific androgen-dependent proteins were taken as indicators of normal function. Development was perturbed by using oestradiol benzoate, since this was known to affect gross development of the seminal vesicles and ventral prostate when given to neonatal rats. Treatment during the first 5 days after birth severely restricted development of the seminal vesicles and ventral prostate. Protein secreted by the former was only 1% of the normal amount, and in many cases several major secretory proteins were essentially missing. Prostatic protein secretion was less than 20% of normal, but all the major proteins were detectable. In both tissues overall protein synthesis per cell was quantitatively normal, but the proportion devoted to specific major secretory proteins was markedly depressed, i.e. the response is differential. In contrast, treatment during the prepubertal period was without noticeable effects. Development of the seminal vesicles and prostate was somewhat inhibited by treatment at puberty, but these changes were minor compared with those after neonatal exposure to oestradiol benzoate. No effects on epididymal protein synthesis or secretory proteins were observed, and epididymal weight and DNA content were only moderately decreased regardless of when oestradiol benzoate was administered during sexual maturation. Hence the neonatal period is not so critical for epididymal development. The substantial changes elicited by oestrogen treatment during neonatal life in seminal-vesicle and prostatic protein synthesis and secretion were compared with those evoked in sexually mature males by either oestrogen treatment or castration. Both these latter treatments resulted in a general decrease in seminal-vesicle protein synthesis and secretion, but the marked differential effects on major proteins after neonatal exposure were absent. Castration did, however, evoke a differential prostatic response, but this was not seen after oestrogen treatment of adults.
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PMID:Functional development of sex accessory organs of the male rat. Use of oestradiol benzoate to identify the neonatal period as critical for development of normal protein-synthetic and secretory capabilities. 730 31

The possibility that alpha-chlorohydrin, 6-chloro-6-deoxyglucose (6CDG) and cyproterone acetate (CPA) might affect epididymal protein secretion or acquisition of sperm surface proteins as the cause of their antifertility action in male rats was investigated. Daily administration of 9 mg/kg alpha-chlorohydrin for 7--14 days and 24 mg/kg 6CDG for 14--21 days induced sterility in male rats and imparied the capacity of the cauda epididymal spermatozoa to initiate motility. Treatment with CPA (30 mg/kg/day) for 21--28 days, however, was found to have no effect on fertility and initiation of sperm motility, although the epididymis of the treated animals underwent a loss in weight. The antifertility effects of alpha-chlorohydrin or 6CDG did not seem to be attributed to an interference with epididymal protein secretion. The cauda epididymal fluids of the alpha-chlorohydrin, 6CDG and CPA treated animals have similar protein patterns compared to those of the control animals. However, when the surface proteins of the spermatozoa were labelled with radioactive iodine, the sperm surface proteins alpha-chlorohydrin and 6CDG treated animals were found to differ from those of the control animals. Two peaks (MW 32 000 and 70 000) and one peak (70 000) were significantly reduced in the alpha-chlorohydrin treated and 6CDG treated animals, respectively. Additional bands appeared on the surface of the treated (infertile) animals. In contrast, CPA treatment did not affect the surface protein pattern of the epididymal spermatozoa. It was concluded that the antifertility affects of alpha-chlorohydrin and 6CDG are not due to an interference with epididymal secretion of specific proteins but to an intervention of the subsequent acquisition of these proteins by epididymal spermatozoa. This results in a decrease in the capacity of the epididymal sperm to initiate motility and hence a loss of fertilizing capacity.
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PMID:Effects of antifertility drugs on epididymal protein secretion, acquisition of sperm surface proteins and fertility in male rats. 731 53

The proteins of epididymal luminal fluid and of spermatozoa recovered from different regions of the rat epididymis were examined by polyacrylamide gel electrophoresis under non-denaturing and denaturing conditions. Albumin (A) and four major pre-albumin bands (B-E) were observed in epididymal fluid from the cauda on non-denaturing gels. By comparing the migration of these bands with that of standard globular proteins on denaturing gels, the molecular weight of Bands B and C was estimated to be 16 000, Band D was 30 000 and Band E was 32 000. Bands D and E were apparently glycoproteins since they stained with periodic acid-Schiff's reagent and were bound by an affinity column of Concanavalin A. The pre-albumin proteins (B-E) were of epididymal origin since they (a) were not detected in blood serum, (b) were not detected in testicular extracts and (c) were still found after ligation of the efferent ducts. From the incorporation of radioactive methionine, Bands B and C were shown to be synthesized in the initial segment and caput. The regional distribution of luminal proteins indicated that protein D was added in the caput and cauda and protein E in the cauda. This regional origin of luminal proteins was confirmed by the altered protein profiles consequent upon the reduced fluid flow through the epididymis brought about by ligation of the efferent ducts. The androgen-dependence of epididymal protein synthesis was also investigated using radioactive methionine. Castration had little effect on total protein synthesis but resulted in the specific reduction of the synthesis of proteins B and C. Several changes were observed in the relative amounts of specific proteins extracted from spermatozoa from different regions of the epididymis and several of these proteins had molecular weights identical with those in luminal fluid. However, there was no evidence for any substantial binding to spermatozoa of the pre-albumin proteins (B-E) of luminal fluid.
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PMID:Characterization and androgen-dependence of proteins associated with luminal fluid and spermatozoa in the rat epididymis. 743 Dec 93

The motility of ejaculated spermatozoa (% of progressive spermatozoa) has been evaluated visually on 26 adult rams. Half the animals were immunized with a secretory epididymal protein (prealbumin epididymal-specific (PES) ovine) injected according to immunizing protocols (Freund or Hunter adjuvant) intraperitoneally or intradermally (Freund or Hunter adjuvant) or intramuscularly (Hunter adjuvant or PES only). The other animals received the same product without the protein (controls). The product resulted in a strong asthenospermia which parallels the transient presence of anti-PES antibodies in the seminal plasma. A study with 64 ewes showed that the fertility of 10 immunized rams that had recovered sufficient forward motility to ensure fertilization, did not differ from that of control rams.
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PMID:[Autoimmune asthenospermia induced by an epididymal protein, ovine prealbumin (oPES)]. 754 33

During epididymal transit, mammalian spermatozoa acquire new surface antigens that may participate in gamete interaction. We have previously described a 26-kDa (P26h) epididymal hamster sperm protein that we propose to be involved in fertilization. In this study, we have searched for an antigenically related protein in the human, and have found that an anti-P26h antiserum recognizes a 34-kDa (P34H) protein on Western blot of human sperm proteins. Immunostaining showed that this protein is localized on the acrosomal cap of human epididymal spermatozoa but not on testicular gametes. The effect of the anti-P26h antiserum on the fertilizing ability of human spermatozoa was evaluated by use of a human zona pellucida binding assay. Compared to the preimmune serum, the antiserum caused a highly significant decrease in the number of sperm bound per zona pellucida. This inhibition was not due to the induction of a premature acrosomal reaction nor to an effect on the motility of the spermatozoa. The antiserum recognizing the P34H human sperm protein had no effect on gamete fusion as determined by the zona-free hamster test. Our results suggest that the human spermatozoon acquires an epididymal protein that shares a common epitope(s) with the P26h hamster sperm protein. The possible involvement of this human sperm antigen in the binding to the zona pellucida is discussed.
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PMID:Human sperm-zona pellucida interaction is inhibited by an antiserum against a hamster sperm protein. 781 37

The present report identifies epididymal boar anti-agglutinin and examines its effect on sperm motility. Boar spermatozoa from the cauda epididymidis were washed and incubated in modified Krebs-Ringer bicarbonate at 37 degrees C (5% CO2 in air). In the samples washed three or five times and then incubated for 3-5 h, higher rates (72-79%) of spermatozoa were associated with one another at the acrosomal region, mainly in groups of 2-5 cells (head-to-head agglutination), and many cells exhibited intensively flagellant and/or circular types of movement but rarely progressive motility. The addition of epididymal plasma or 25 kDa protein purified from it markedly inhibited the occurrence of head-to-head agglutination in washed spermatozoa, whereas heat treatment and subsequent removal of insoluble materials reduced the anti-agglutination activity of epididymal plasma. The percentages of progressively motile cells in the samples incubated with epididymal plasma or 25 kDa epididymal protein rose coincident with the reduction of sperm agglutination. These findings demonstrate that the 25 kDa epididymal protein is an anti-agglutinin for the cauda spermatozoa and that it effectively functions to maintain progressive motility of the cells in vitro.
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PMID:Identification of anti-agglutinin for spermatozoa in epididymal boar plasma. 801 28

The sperm coating lizard epididymal secretory protein (LESP) family forms a complex of nine elements that are specifically synthesized under androgenic control and secreted by the epididymal epithelial cells of the lizard Lacerta vivipara. We report here the cloning and sequencing of an 806-base pair full-length cDNA (C731) encoding one of the elements of the LESP family. Southern blot hybridization analysis of lizard total genomic DNA revealed a complex band pattern, suggesting that LESPs are encoded by a multigenic family. The cDNA open reading frame of 516 nucleotides, starting at an ATG codon, encodes a protein precursor of 172 amino acids with a calculated M(r) = 19,500. The corresponding mature form of M(r) = 17,200 and pI = 5.2 has been identified as the element LESP IV, and presents significant similarities to the different members of the large lipocalin protein superfamily, and especially to mouse epididymal protein ESP I. Lipocalins are extracellular proteins that share a common basic framework for the transport of small hydrophobic molecules like retinoids, thus suggesting that LESPs could be such transporters into the epididymal fluid during the sperm maturation.
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PMID:LESP, an androgen-regulated lizard epididymal secretory protein family identified as a new member of the lipocalin superfamily. 848 91


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