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)

A case of epididymal metastasis from prostatic carcinoma is presented. The initial histologic findings were suggestive of adenomatoid tumor, but a diagnosis of metastatic adenocarcinoma of prostatic origin has been established by prostatic acid phosphatase and prostate-specific antigen immunoperoxidase staining.
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PMID:Epididymal metastasis from prostatic adenocarcinoma mimicking adenomatoid tumor. 170 Oct 66

The predominant protein in human semen, semenogelin, was characterized by lambda gt11 clones isolated from a seminal vesicular cDNA library. One clone, carrying a cDNA insert of 1606 nucleotides and a polyadenylated tail, coded for the entire semenogelin precursor. An open reading frame of 1386 nucleotides encodes a signal peptide and the mature protein of 439 amino acid residues, in which residues 85-136 are identical with a previously characterized semenogelin fragment. The polypeptide chain displays a most conspicuous region of internal sequence homology where 46 of the 58 amino acid residues at positions 259-316 are repeated at positions 319-376. An abundant seminal vesicular transcript of 1.8 kilobases (kb) codes for semenogelin. Two additional transcripts, one seminal vesicular 2.2-kb species and one epididymal 2.0-kb species, code for related proteins that have a close structural relationship as well as antigenic epitopes in common with semenogelin. Semenogelin and the semenogelin-related proteins are the major proteins involved in the gelatinous entrapment of ejaculated spermatozoa. Antigenic epitopes common to these proteins are localized to the parts of the spermatozoa involved in locomotion. The spermatozoa become progressively motile as the gel-forming proteins are fragmented by the kallikrein-like protease, prostate-specific antigen, and the gel dissolves.
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PMID:Semenogelin, the predominant protein in human semen. Primary structure and identification of closely related proteins in the male accessory sex glands and on the spermatozoa. 291 89

Semenogelin I and II (Sgl, Sgll) are two separate gene products of chromosome 20 with extensive (80%) identity in primary structure. They are mainly responsible for immediate gel formation of freshly ejaculated semen. Degradation of Sgl and Sgll is due to the proteolytic action of prostate-specific antigen (PSA); it results within 5-15 minutes in liquefaction of semen and release of progressively motile spermatozoa. By means of cDNA cloning and Northern blots, Sgl and Sgll transcripts have previously been shown to be abundant in human seminal vesicles, but Sgll alone is suggested to be expressed at low levels in the epididymis. To characterize the expression and tissue distribution of Sgl and Sgll in greater detail, we produced monoclonal immunoglobulin Gs (lgGs for immunocytochemistry (lCC) and specific [35S]-, digoxigenin-, or alkaline phosphatase-labeled 30-mer antisense probes to Sgl and Sgll for in situ hybridization (lSH). Immunocytochemical staining for both Sgl and Sgll, and lSH detection of both Sgl and Sgll transcripts, were demonstrated in the cytoplasm of seminal vesicle epithelium. lSH showed Sgll alone to be expressed in the epithelium of the epididymal cauda. Neither lCC nor lSH yielded any evidence of Sgl or Sgll expression in caput or corpus epithelium or in any stromal cells of the epididymis. Consistent with our previous findings using polyclonal lgG, monoclonal anti-Sgll Sgll lgGs identified epitopes on the posterior head, midpiece, and tail of ejaculated spermatozoa. Spermatozoa in the epididymal cauda were also immunoreactive, but those in the caput or corpus region of the epididymis as well as those in the testis were negative. As shown by lCC, neither Sgl nor Sgll were expressed in the testis, the prostate, the female genital tract, or other normal human tissue specimens. Although the significance of Sg attachment to epididymal and ejaculated spermatozoa remains to be established, monoclonal anti-Sg lgG might prove useful in establishing the origin of seminal vesicle tissue components in prostate core biopsies or other biopsy specimens.
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PMID:Distribution and tissue expression of semenogelin I and II in man as demonstrated by in situ hybridization and immunocytochemistry. 883 37

Protein C inhibitor (PCI) is a heparin-binding plasma serine protease inhibitor that was originally identified as an inhibitor of activated protein C. PCI has a broad protease specificity, inhibiting several proteases in hemostasis and fibrinolysis by acting as a suicide substrate. Recently it has been reported that proteases of the reproductive system, such as acrosin, prostate-specific antigen, and tissue kallikrein, can also be effectively inhibited by PCI. However, a direct relation between PCI and physiological events during fertilization has not yet been established. An attempt was made to monitor and localize the inhibition of the sperm protease acrosin by PCI. Localization experiments for PCI on epididymal spermatozoa showed that PCI is present on the acrosomal cap of human spermatozoa, which demonstrates the early presence of PCI in the male reproductive tract. Induction of the acrosome reaction in ejaculated human spermatozoa resulted in the disappearance of PCI from the plasma membrane overlying the acrosomal head and the appearance of a strict distribution at the equatorial segment of human spermatozoa. The activity of acrosin in sperm extracts could be effectively inhibited by PCI. Zona-binding assays showed that active PCI is able to block sperm-egg binding in a concentration-dependent manner. The combination of the potent inhibition of acrosin and sperm-egg binding by PCI and the localization studies suggested that PCI may protect spermatozoa against premature acrosome reaction and degradation, thereby modulating the acrosin activity so that it can coincide with binding to the oocyte.
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PMID:Protein C inhibitor may modulate human sperm-oocyte interactions. 951 Sep 55

Trypsinogen is a serine proteinase produced mainly by the pancreas, but it has recently been found to be expressed also in several cancers such as ovarian and colon cancer and in vascular endothelial cells. In this study, we found that trypsinogen-1 and -2 are present at high concentrations (median levels, 0.4 and 0.5 mg/L, respectively) in human seminal fluid and purified them to homogeneity by immunoaffinity and anion exchange chromatography. Purified trypsinogen isoenzymes displayed a M(r) of 25 to 28 kd in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting. Most of the trypsinogen-1 purified from seminal fluid was enzymatically active whereas trypsinogen-2 occurred as the proform, which could be activated by enteropeptidase in vitro. Immunohistochemically, trypsinogen protein was detected in the human prostate, urethra, utriculus, ejaculatory duct, seminal vesicles, deferent duct, epididymal glands, and testis. Expression of trypsinogen mRNA in the same organs was demonstrated by in situ hybridization. Trypsinogen mRNA was also detected in the prostate and seminal vesicles by reverse transcriptase-polymerase chain reaction and Northern blotting. Isolated trypsin was shown to activate the proenzyme form of prostate-specific antigen. These results suggest that trypsinogen isoenzymes found in seminal fluid are produced locally in the male genital tract and that they may play a physiological role in the semen.
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PMID:Expression and characterization of trypsinogen produced in the human male genital tract. 1110 74

Serum and seminal biologic substances that are produced either by normal or abnormal tissues of the organism and that can be used to diagnose pathological conditions are usually referred as markers. The aim of this article is to briefly review the most relevant clinical features of the main genital markers in the male dog: alkaline phosphatase (AP), carnitine and canine prostate-specific arginine esterase (CPSE). Carnitine and AP are markers for the presence of epididymal fluid in the ejaculate and their measurement in azoospermic dogs has been used as an indicator of tubular patency of the ductal network. Although AP is not present in high concentrations in the testis, this does not preclude the possibility that testicular cells might secrete some AP. If this were true, AP could also reflect, at least in some degree, germ cell function in this species. Prostate-specific arginine esterase, the major secretory product of the canine prostate, is a known marker of gland secretion in the dog. Tumor markers frequently used in human medicine, such as prostatic acid phosphatase and prostate-specific antigen, are is still controversial in the diagnosis of prostatic carcinoma of the dog. Although further research is necessary to define the exact role of CPSE, it seems to be a promising diagnostic tool in nonneoplasic canine prostatic disorders. Future studies should also address the quantitative relationship among serum and prostatic androgen levels, prostatic androgen-dependent problems and how these are affected by anti-androgen treatment. The aim of this article is to briefly review the most relevant clinical features of three main genital markers of the male dog.
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PMID:Serum and seminal markers in the diagnosis of disorders of the genital tract of the dog: a mini-review. 1201 48

Aberrant prostatic tissue occurs commonly in the adult male urethra and bladder. Ectopic prostatic tissue occurring outside the urinary system is rare. One case with scattered prostate-type glands in epididymis has been reported in the literature. We report a related case, in which the presence of prostate gland-like epithelium was recognized in epididymal glands in routine histology and was confirmed by subsequent immunohistochemical analysis using prostate-specific antigen. We then examined 23 additional orchiectomy specimens for the presence of prostate-like epithelium. The possibility of this being true ectopia versus an unusual metaplastic change is discussed.
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PMID:Prostate gland-like epithelium in the epididymis: a case report and review of the literature. 1504 74

Previous studies from our group have shown that Foxa1 is expressed in the prostate and interacts with the androgen receptor (AR) to regulate prostate-specific genes such as prostate-specific antigen (PSA) and probasin (PB). We report here that Foxa2 but not Foxa1 is expressed in the epididymis. Further, Foxa2 interacts with the AR to regulate the mouse epididymal retinoic acid binding protein (mE-RABP) gene, an epididymis-specific gene. Binding of Foxa2 to the mE-RABP promoter was confirmed by gel-shift and chromatin immunoprecipitation (ChIP) assays. Overexpression of Foxa2 suppresses androgen activation of the mE-RABP promoter while overexpression of Foxa2 with prostate-specific promoters activates gene expression in an androgen-independent manner. GST pull-down assays determined that both Foxa1 and Foxa2 physically interact with the DNA binding domain of the AR. The interaction between Foxa proteins and AR was further confirmed by gel-shift assays where Foxa protein was recruited to AR binding oligomers even when Foxa binding sites were not present, and AR was recruited to Foxa binding oligomers even in the absence of an AR binding site. Given that Foxa1 and Foxa2 proteins are expressed differentially in the prostate and epididymis, these data suggest that the Foxa proteins have distinct effects on AR-regulated genes in different male reproductive accessory organs.
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PMID:Foxa1 and Foxa2 interact with the androgen receptor to regulate prostate and epididymal genes differentially. 1646 59

We wanted to investigate the origin of seminal plasma albumin and its relation to the male reproductive parameters. Semen samples from 916 men, under infertility assessment, were analysed according to guidelines of the World Health Organization. Seminal plasma constituents, i.e. albumin, markers of the epididymal (neutral alpha-glucosidase, NAG), prostatic (prostate-specific antigen, PSA, and zinc) and seminal vesicle function (fructose), as well as levels of reproductive hormones in plasma were measured. The sperm chromatin structure assay (SCSA) was applied on 267 of the 916 samples. A negative correlation was seen for seminal albumin and plasma follicle-stimulating hormone (r=-0.1, P=0.02) and a positive correlation for seminal albumin and serum inhibin B (r=0.2, P=0.004). Albumin exhibited positive correlations with the epididymal marker, NAG (r=0.5, P<0.001) and with the prostatic markers, PSA and zinc (r=0.1, P=0.001; r=0.2, P<0.001 respectively) as well as with age (r=0.2, P<0.001). A negative significant association was seen for seminal albumin and semen volume (beta=-0.60; 95% CI -0.80 to -0.30). The opposite trend was found regarding sperm concentration (beta=0.34; 95% CI 0.30-0.40), total sperm count (beta=0.30; 95% CI 0.20-0.40), and percentage morphologically normal spermatozoa (beta=0.70; 95% CI 0.10-1.0). No association was found between albumin and sperm motility, SCSA parameters, or fructose, the marker of seminal vesicles. Our results suggest testicular, epididymal and prostatic origin of seminal plasma albumin, in addition to the contribution from blood. This is the first study to demonstrate an association between seminal plasma albumin and sperm morphology. Further studies are needed to elucidate the role of seminal albumin in sperm morphology.
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PMID:Seminal plasma albumin: origin and relation to the male reproductive parameters. 1743 Apr 25

This study aimed to examine the association between the interval from ejaculation to analysis and epididymal and accessory sex gland function in relation to sperm motility. Ejaculates from 1079 men assessed for infertility were analyzed according to World Health Organization guidelines. Biochemical markers were measured in semen to assess the function of the epididymis (neutral alpha-glucosidase [NAG]), prostate (prostate-specific antigen [PSA] and zinc), and seminal vesicles (fructose). Three groups were defined according to time from ejaculation to analysis: G(< or =30) (24-30 minutes), G(31-60) (31-60 minutes), and G(>60) (63-180 minutes). The proportion of progressively motile sperm was significantly lower in G(>60) than in G(< or =30) (mean difference, 8.0%; 95% confidence interval [CI], 2.0%-13%) or G(31-60) (mean difference, 6.0%; 95% CI, 1.0%-12%). The proportion of rapid progressive sperm motility was significantly higher in G(< or =30) compared with G(31-60) (mean difference, 3.0%; 95% CI, 1.0%-5.0%) and G(>60) (mean difference, 6.0%; 95% CI, 1.0%-10%). Sperm morphology and viability did not vary significantly between the groups. However, PSA levels in G(>60) were 29% and 31% significantly lower than in G(< or =30) (95% CI, 3.0%-54%) and G(31-60) (95% CI, 7.0%-58%), respectively. Moreover, men in G(>60) had 29% and 17% significantly lower zinc compared with those in G(< or =30) (95% CI, 4.0%-69%) and G(31-60) (95% CI, 4.0%-64%), respectively. Levels of NAG and fructose did not differ significantly between the groups. There were negative associations between the ejaculation-to-analysis interval and sperm motility and levels of PSA and zinc. In male infertility assessments, semen analysis should be performed within 60 minutes of ejaculation.
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PMID:Effects of ejaculation-to-analysis delay on levels of markers of epididymal and accessory sex gland functions and sperm motility. 1755 11


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