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)

The presence of prion protein in sperm and fluids collected from different parts of the ram genital tract was investigated by immunoblotting with monoclonal antibodies. A slightly immunoreactive 25- to 30-kDa protein was recognized on Western blots of testicular and epididymal sperm extracts. Immunoreactivity increased on ejaculated sperm extracts and 2 other bands at 35 and 43 kDa also reacted. Seminal plasma showed several immunoreactive bands, the main bands being detected at 43 and 35 kDa, whereas less reactive bands were observed at 30, 25, 20, and <14 kDa. All these bands strongly decreased in the seminal plasma after vasectomy, indicating a testicular or an epididymal origin. Testicular fluid showed almost no reactivity, whereas caudal epididymal fluid contained the 2 strong immunoreactive bands at 43 and 35 kDa and in some cases a faint 30-kDa band. The 43-kDa band was also found in the fluid from the proximal caput, whereas the 35-kDa band appeared in the distal caput. Immunoprecipitation of (35)S-labeled proteins secreted in the epididymal fluid indicated that the 43-kDa form was synthesized in caput and caudal regions and the 35-kDa form in the distal caput to the distal corpus. Treatment of caudal fluid and seminal plasma by N-glycosidase resulted in the formation of 3 bands: 1 highly reactive at about 25 kDa, a second less reactive at about 28 kDa, and a third at approximately 20 kDa. The pattern of prion protein distribution in epididymal fluids was found to be similar in scrapie-infected rams to that of healthy rams. Cauda epididymal fluid and seminal plasma from infected animals could not be treated directly with proteinase K, because of the presence of protease inhibitors. However, the prion protein immunoprecipitated from these fluids was completely cleaved by proteinase K, whereas in the same conditions this from an infected sheep brain gave the usual resistant band pattern.
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PMID:Prion protein is secreted in soluble forms in the epididymal fluid and proteolytically processed and transported in seminal plasma. 1213 72

The prion-like Doppel protein (Dpl) has many biochemical and structural properties in common with the cellular prion protein (PrP(c)), and the physiological role of neither protein is known. Experimental data suggest either direct or indirect interaction between the two proteins. In this study, we investigated the expression pattern and biochemical characteristics of Dpl in human tissues and in Chinese hamster ovary cells transfected with wild-type or variant human Dpl gene constructs. Human Dpl appears to be a glycosylphosphatidylinositol-anchored glycoprotein with N- and O-linked sugars. It was found on Sertoli cells in the testis, on the flagella of epididymal and mature spermatozoa, and in seminal plasma. Dpl coexists only with N-terminally truncated isoforms of PrP(c) on mature spermatozoa. The localization of human Dpl on both Sertoli cells (somatic cells) and spermatozoa (germinal cells) strongly suggests that this protein may play a major role in human male fertility. Finally, our data indicate that spermatozoa are thus an interesting model for studies of the potential interaction between Dpl and PrP(c).
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PMID:The human "prion-like" protein Doppel is expressed in both Sertoli cells and spermatozoa. 1220 Apr 35

Cellular prion protein (Prp(C)) is a glycoprotein usually associated with membranes via its glycosylphosphatidylinositol (GPI) anchor. The trans-conformational form of this protein (Prp(SC)) is the suggested agent responsible for transmissible neurodegenerative spongiform encephalopathies. This protein has been shown on sperm and in the reproductive fluids of males. Antibodies directed against the C-terminal sequence near the GPI-anchor site, an N-terminal sequence, and against the whole protein showed that the Prp isoforms were compartmentalized within the reproductive tract of the ram. Immunoblotting with the three antibodies showed that the complete protein and both N- and C-terminally truncated and glycosylated isoforms are present within cauda epididymal fluid and seminal plasma. Moreover, we demonstrate that in these fluids, the Prp(C) isoforms are both in a soluble state as well as associated with small membranous vesicles (epididymosomes). We also report that only one major glycosylated 25 kDa C-terminally truncated Prp(C) isoform is associated with sperm from the testis, cauda epididymis, and semen, and this form is also present in the sperm cytoplasmic droplets that are released during maturation. In sperm, this C-terminal truncated form was found to be associated with membrane lipid rafts present in the mature sperm, suggesting a role for it in the terminal stages of sperm maturation.
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PMID:Compartmentalization of prion isoforms within the reproductive tract of the ram. 1516 17

Mass spectrometric analysis of a prion protein (PrP)-containing complex isolated from ram cauda epididymal fluid revealed a protein that showed homology to a carboxylesterase-like protein previously identified in cat urine (cauxin). Using anti-cauxin antibodies, immunoreactive bands were detected in corpus and cauda epididymal fluid from all mammals tested (ram, boar, mouse, and cat). In the ram, the protein was also present in seminal fluid but not found to be associated with sperm. The bands reacting with the anti-cauxin antibody coincided with those having esterase activity in a zymographic assay and its levels paralleled the esterase activity of native epididymal fluids. A partial nucleotide sequence of 1143 bp, corresponding to 380 amino acids, was obtained by RT-PCR amplification from total RNA from the corpus epididymis (zone 6). The deduced protein sequence shows a high degree of homology (up to 90%) with the different cauxin proteins found in databases but only up to 60% with other known carboxylesterases. By PCR, strong mRNA expression was found in the corpus and cauda epididymis, while the testis, kidney, and caput epididymis had low expression. No mRNA was detected in the lung, heart, or liver. These data demonstrate that an epididymal form of the cauxin enzyme is secreted into mammalian epididymal fluid. In the ram, it is associated with a high molecular-weight PrP-associated complex and may be responsible for the majority of the esterase activity in the cauda epididymal fluid of this species.
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PMID:An epididymal form of cauxin, a carboxylesterase-like enzyme, is present and active in mammalian male reproductive fluids. 1625 97

Scrapie is the most common transmissible spongiform encephalopathy (TSE) in livestock. Natural contamination in sheep flocks is presumed to occur by maternal transmission to offspring. However, horizontal prion transmission from animal to animal exists and may be significant in sustaining and spreading contagion in the field. Artificial insemination is widely used in modern farming, and as large amounts of prion protein have been found in sheep sperm membrane, epididymal fluid and seminal plasma, horizontal transmission by this route was hypothesized since no clear information has been obtained on possible sexual transmission of TSE. We therefore tested the contamination levels of semen from scrapie-infected rams at different stages of incubation, including the clinical phase of the disease. We report here that under our experimental conditions ram semen did not transmit infectivity to scrapie-susceptible transgenic mice overexpressing the V(136)R(154)Q(171) allele of the sheep prion (PRNP) gene. These results suggest that artificial insemination and natural mating have a very low or negligible potential for the transmission of scrapie in sheep flocks.
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PMID:Semen from scrapie-infected rams does not transmit prion infection to transgenic mice. 1829 35