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Query: UNIPROT:P06889 (Mol)
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Recently, a new head-to-head sperm association was described in the rat during epididymal transit. This association was called a rosette and a filamentous and PAS-positive material was also described joining the sperm heads. The beginning of rosette formation in the epididymis and the linking material between heads have remained unclear. Epididymides of adult rats were fixed by vascular perfusion and thin sections of the principal regions were studied by transmission electron microscopy (TEM). The first evidence of rosette formation was observed in the distal corpus. Rosettes were isolated from the distal corpus and processed for immunogold and immunofluorescence microscopy to detect an epididymal glycoprotein called DE. This glycoprotein is secreted by the corpus epididymis and appears to be involved in sperm maturation. Colloidal gold marks and fluorescence were observed in the linking material between the sperm heads. The results presented here show that rosettes begin to appear following the sites of DE secretion and permit us to postulate that DE is involved in rosette formation and constitutes another example of gamete-epididymal interaction.
Mol Reprod Dev 1994 May
PMID:Epididymal glycoprotein involved in rat sperm association. 804 64

The principal galactose oxidase/NaB[3H]4-labeled membrane protein of rat caudal epididymal spermatozoa was isolated by hydrophobic interaction chromatography. The protein is released from the membrane by the action of phosphatidylinositol specific phospholipase C, and thereby its properties are transformed from those of a protein anchored to the hydrophobic membrane to those of a hydrophilic solution protein. Because it is the only membrane-associated protein released by the enzyme which did not absorb to a propylaspartate resin, a simple, single step purification procedure was devised. Although the amino terminus of the protein is blocked to Edman degradation, the majority of the protein structure was determined from a series of tryptic peptides and from limited acid hydrolysis. Approximately 65% of the protein mass is carbohydrate which is primarily attached through O-glycosidic bonds to the 18 threonines. The molecular weight of the glycoprotein was estimated to be 16,600, considerably smaller than the M(r) = 26,000 to 37,000 previously determined by gel electrophoresis. The anomalous electrophoretic behavior is undoubtedly due to the large percentage of carbohydrate. The distribution of carbohydrate on the protein side chains suggests the protein may form a positively charged, specialized scaffolding for the presentation of the carbohydrate moieties. Because the appearance of the ability to label the protein with galactose oxidase is correlated with sperm maturation in the epididymis, the glycoprotein structures may be an important component in the fertilization process. The combination of linkage by glycosylphosphatidylinositol and low molecular weight mucin-like structure indicates this may be a member of a new class of membrane proteins.
Mol Reprod Dev 1994 Jan
PMID:Characterization of a cell surface glycoprotein associated with maturation of rat spermatozoa. 812 26

In this study we have used acridine orange staining, as described by Evenson (1990), to follow changes in DNA packaging as they occur in hamster spermatozoa which have left the testis and are undergoing maturation in the epididymis. Measurement of the green and red fluorescent intensities of hamster sperm nuclei by flow cytometry demonstrated a decrease in acridine orange binding to DNA as sperm made their way from proximal corpus epididymis to the vas deferens. Using sperm from the cauda epididymis of the mature hamster as the standard, a method was developed for estimating the % of cells in a given sample that have matured with regard to DNA packaging. Staining with bromobimane was used to determine the extent of sulfhydryl oxidation in the nuclei. It was seen that sulfhydryl oxidation occurred mainly in the cauda epididymis whereas another process in chromatin condensation occurred earlier, during sperm passage through the caput epididymis. This earlier process could be mimicked by incubating sperm nuclei with alkaline phosphatase, suggesting that it consists of removal of phosphate in protamine.
Mol Reprod Dev 1994 Jan
PMID:Chromatin condensation in hamster sperm: a flow cytometric investigation. 812 36

The androgen receptor (AR) was localized immunohistochemically after different hormonal treatments in the ventral prostate, coagulating gland, seminal vesicle and epididymis of the adult rat. In the untreated controls AR-immunoreactivity was confined to the cell nuclei. One week after castration or treatment with the gonadotropin-releasing hormone antagonist Cetrorelix (150 micrograms/animal per day) a cytoplasmic staining occurred in the epithelial cells of the ventral prostate and in part of the coagulating gland and seminal vesicle. In contrast, the AR remained exclusively in the nuclei in the epididymal epithelium and the glandular smooth muscle layer even after 2 weeks of androgen depletion. Bolus injections of either dihydrotestosterone (1 mg/kg), the antiandrogen flutamide (40 mg/kg), or the novel non-steroidal antiandrogen casodex (40 mg/kg) to androgen-depleted animals eliminated cytoplasmic AR-immunoreactivity and restored the nuclear staining pattern in the ventral prostate. A sustained 2-week treatment with the antiandrogens resulted in a loss of weight in all organs but did not alter the distribution of AR-immunoreactivity. The data show an apparent cytoplasmic/nuclear ligand-dependent translocation of the AR in the ventral prostate, coagulating gland and seminal vesicle but not in the epididymis of the adult rat.
J Steroid Biochem Mol Biol 1994 Jan
PMID:The effect of androgens and antiandrogens on the immunohistochemical localization of the androgen receptor in accessory reproductive organs of male rats. 813 98

We have previously prepared an anti-mouse sperm monoclonal antibody (A-1) which inhibited sperm penetration into the egg zona pellucida. By indirect immunofluorescence (IIF), the A-1 antibody was shown to recognize an antigen localized in the acrosomal area of sperm. This antibody bound negligibly to fresh sperm, while binding to methanol-fixed sperm was almost complete. After methanol fixation, no sperm that penetrated into the zona were immunoreactive for this antibody. In the present study we examined the localization and fate of A-1 antigen during the acrosome reaction by IIF and flow cytometry (FCM). Cauda epididymal sperm were treated with either calcium ionophore A23187 or zona solution, immunostained indirectly, and subjected to FCM. Treatment with A23187 reduced the percentage of immunoreactive sperm to 59% from the 80% obtained in the untreated sperm. The treatment also reduced the average fluorescence intensity per fluorescence-positive spermatocyte to 65 channels, while this intensity was 89 channels in the untreated sperm. A similar result was obtained from treatment with zona solution. The proportion of sperm that was immunoreactive with A-1 antibody was reduced to 55% by incubation in zona-containing media from the 80% obtained in zona-free media. On the other hand, neither A23187 nor the zona solution affected the immunoreactivity or the fluorescence intensity of caput epididymal sperm, while the A-1 antigen was present in both the immature sperm from the caput epididymis of adult mice and in the mature sperm from the cauda epididymis of the same mice.(ABSTRACT TRUNCATED AT 250 WORDS)
Mol Reprod Dev 1994 Mar
PMID:Flow cytometric analysis of mouse sperm using monoclonal anti-sperm antibody A-1. 818 34

A method to generate a population of motile, acrosome-reacted mouse sperm is described. Sperm retrieved from the cauda epididymis and vas deferens were first capacitated in a 3% bovine serum albumin (BSA) containing medium. Sperm were then resuspended in medium with low BSA content (0.01%) and treated with 30 nM of the calcium ionophore, A23187, which was added as a single dose of 30 nM for 15 min at 37 degrees C; or three sequential 10 nM doses over three 5 min intervals. Approximately 55-60% of the treated sperm population became acrosome reacted. The motility of the treated sperm sample was 40-65%, slightly lower than that of the control sperm, following addition of medium containing 3% BSA. This is in contrast to the < 10% motility observed for capacitated mouse sperm treated with 10 microM 23187, a concentration that had been used by other investigators to induce the acrosome reaction. The ultrastructure of the 30 nM A23187-induced acrosome-reacted sperm was similar to that of the acrosome-reacted sperm induced by solubilized zonae pellucidae. These motile, acrosome-reacted sperm were able to penetrate zona-free mouse eggs at a higher rate than the control sperm. Thus this method of treatment will be useful for further physiological experimentation with acrosome-reacted sperm.
Mol Reprod Dev 1994 Mar
PMID:Production of motile acrosome-reacted mouse sperm with nanomolar concentration of calcium ionophore A23187. 818 38

beta-N-acetylhexosaminidase exhibits a relatively high activity in human epididymis. Its isoenzymatic profile and immunological properties led us to conclude that the increased activity was not due to the expression of an isoform unrelated to the HEX A and B present in other human tissues. Measurement of enzyme levels in the three distinct epididymal regions revealed that in any given sample, activity was higher in the caput than in the corpus or cauda. Moreover, we found a striking correlation between beta-HEX activity in the caput region and concentrations of blood testosterone, suggesting a possible involvement of the hormone in modulating enzyme expression. Since the caput epididymis plays a role in the maturation of sperm cells, our data may be an indication that beta-HEX activity in the caput has a physiological relevance in human epididymis functions.
Biochem Mol Biol Int 1993 Aug
PMID:Blood testosterone levels are correlated with beta-N-acetylhexosaminidase activity in human caput epididymis. 822 Feb 48

Localization of glucocorticoid receptor-like immunoreactivity (GR-LI) was studied in adult rat testis, epididymis, ejaculatory duct, seminal vesicle and prostate by light and electron microscopic immunocytochemistry. In the interstitium of the testis GR-LI was seen in the nuclei of Leydig cells, macrophages, fibroblasts, smooth muscle cells and endothelial cells of blood vessels. Furthermore, GR-LI was observed in zygotene and early pachytene primary spermatocytes of some seminiferous tubules during stages XIII-XIV and I-III of the spermatogenic cycle. Other spermatogenic cells and Sertoli cells were devoid of staining. GR-LI was also found in peritubular myoid cells, fibroblasts and basal cells of the epididymis, vas deferens and prostate. Localization of GR-LI in primary spermatocytes and Leydig cells suggests that glucocorticoids directly affect spermato- and steroidogenesis in the testis. The absence of GR-LI from functional, stromal cells of the male accessory sexual organs suggests that they are not targets for glucocorticoid hormones.
Mol Cell Endocrinol 1993 Sep
PMID:Localization of the glucocorticoid receptor in testis and accessory sexual organs of male rat. 824 1

PSP-I, a 13 kDa protein purified from boar seminal plasma, was found to have about 50% amino acid sequence homology with a family of zona pellucida-binding proteins known as spermadhesins. These proteins are produced by the accessory gland(s) of the male reproductive tract and coat the spermatozoa during ejaculation. In this study, we have investigated the possible biological functions of PSP-I using a solid-phase protein binding assay and its site of synthesis using both Western blot and immunocytochemical analyses. PSP-I was found to bind a number of proteins including endo-beta-galactosidase digested ZP3, soybean trypsin inhibitor, IgA, IgG and alpha-casein, indicating that it may have multiple functions. The protein or carbohydrate structures were not critical in the binding, since polyvinyl sulfate could effectively inhibit the binding of PSP-I to these proteins. Western blot analysis using specific antiserum to PSP-I showed that the protein was present in the seminal vesicle but not in the testes, epididymis or prostate. The protein was revealed by immunocytochemical analysis in the epithelium of seminal vesicles but not in the testes or the epididymis. It is concluded that PSP-I is synthesized by the epithelium of the seminal vesicles, secreted into the semen during ejaculation, and may be involved in various reproductive functions, such as preventing premature acrosome reaction and immunosuppression.
Mol Reprod Dev 1993 Jul
PMID:Binding characteristics and immunolocalization of porcine seminal protein, PSP-I. 835 28

Three tissue-specific gene probes that had been isolated by differential screening from a human epididymal cDNA library--HE1, HE2, and HE5--were employed to investigate regional specializations in the human epididymis. All 3 cDNAs were derived from major transcripts of the epithelial cells lining the epididymal duct. Each mRNA species, however, exhibited a discrete longitudinal pattern of hybridization with maxima in different regions of this organ, suggesting regional specializations of gene expression. The HE5 mRNA, which was recently shown to encode the peptide backbone of the human leukocyte differentiation antigen CDw52, showed maximum levels in the distal corpus epididymidis and in the vas deferens, whereas the HE2 mRNA was found predominantly in the caput and proximal corpus sections of the epididymis. HE1 mRNA was found in high amounts in all parts of the epididymis, displaying a 2-peak expression pattern with maxima in the distal caput and distal corpus of the epididymal duct.
Mol Reprod Dev 1993 Jan
PMID:Region-specific variation of gene expression in the human epididymis as revealed by in situ hybridization with tissue-specific cDNAs. 841 12


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