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Query: UNIPROT:P56851 (epididymal)
 11,273 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The partial purification and characterization of specific rat epididymal proteins (SEP) is reported. Starting from the cytosol fraction obtained from epididymal homogenates, protein C was purified 15-fold and proteins D--E were purified 19-fold. The molecular weight, determined by molecular sieving, of protein C was 22,400 while that of D--E was 37,000. These proteins stained as glycoproteins with periodic acid--Schiff reagent. The isoelectric point of protein D was 5.13 while that of protein E was 4.95. Protein C separated into 3 bands during isoelectric focussing. The major component focussed at 5.56 and the two minor components at pH 5.38 And 5.79. Using a specific antiserum we could confirm the organ specificity of SEP and their androgen-dependence.
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PMID:Isolation and characterization of specific rat epididymal proteins. 10 28

Ultraviolet (UV)-cross-linking and sodium dodecyl sulfate(SDS) polyacrylamide gel electrophoretic (PAGE) analysis were used to identify proteins of nuclear and cytosolic (S100) origin that specifically bind to an in vitro transcribed mRNA sequence for protein D. The coding region of the protein D cDNA was subcloned, in vitro transcribed to [32P]RNA, and incubated with nuclear and cytosolic extracts of enzymatically dispersed epididymal cells. As revealed by UV-cross-linking and SDS-PAGE analysis, two proteins exhibiting a molecular weight mass of approximately 2.5 and approximately 35 Kd that specifically recognize and bind to the in vitro transcribed mRNA sequence for protein D. Our findings suggest that the regulation of protein D gene expression in the rat epididymis may involve novel RNA-binding proteins.
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PMID:Identification of novel RNA-binding proteins that interact in the coding region of protein D sense RNA in vitro. 152 Mar 14

We report the use of a sensitive and specific enyzme-linked immunosorbent assay (ELISA) and polymerase chain reaction (PCR) to study the expression of protein D, a major androgen-regulated sperm-binding glycoprotein at the protein and mRNA level in different anatomical regions of the rat epididymis. The concentration of protein D in the caput, corpus and cauda region of the epididymis was 10.2 +/- 0.67, 7.3 +/- 0.61 and 22.8 +/- 1.34 ng/micrograms total protein, respectively. The total RNA extracted from the caput, corpus and cauda regions of the rat epididymis was amplified by PCR with oligonucleotide primers specific for the 5' and 3' portion of protein D cDNA. Compared to the caput and cauda region, a significant reduction (greater than 82 +/- 3%) in the expression of protein D mRNA levels was observed for corpus epididymal RNA. This data demonstrates regional differences in the concentration of protein D and suggests that protein D expression may be regulated at the level of mRNA within the corpus epididymidis.
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PMID:Protein D is differentially expressed and regulated in the rat epididymis. 156 91

The epididymal tubule is a dynamic structure, in which spermatozoa undergo distinct physiological and morphological changes. The epithelial cells lining the ductuli vary dramatically in their histochemical and cytological properties according to the region of the tubule in which they are located. Additionally, regional variation is observed regarding the biosynthetic, secretory, and absorptive properties of the epithelial cells. Using in situ histochemical analysis, we document here the region-specific expression of a variety of genes that are transcriptionally active in the adult rat epididymis. Radiolabeled antisense riboprobes were used to localize, within the efferent duct/caput epididymis, transcripts encoding protein B/C, protein D/E (acidic epididymal glycoprotein), sulphated glycoprotein 1, sulphated glycoprotein 2, cellular retinol-binding protein, and the neuroendocrine peptide precursor proenkephalin. Each species of mRNA exhibits a unique pattern of hybridization, revealing that gene transcription within the efferent duct/caput epididymis is also highly region specific. This observation may partially elucidate the molecular basis underlying the phenomenon of regional alterations in the composition of protein factors within the tubule lumen.
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PMID:In situ histochemical analysis of region-specific gene expression in the adult rat epididymis. 178 83

Specialization among the principal epithelial cells of the epididymal tubule is documented following the analysis of transcriptional activity of four distinct species of mRNA. In situ histochemical analysis revealed a unique pattern of expression for each transcript. This observation supports the concept that region-specific patterns of transcriptional expression along the epididymal tubule serve as the major molecular basis underlying region-specific patterns of luminal proteins within the tubule. Additionally, multiple testicular factors appear to regulate expression of these mRNAs. The transcript encoding peptidyl-prolyl cis-trans isomerase is constitutively expressed. Those encoding the major secretory proteins, protein B/C and protein D/E, are directly regulated by testicular androgen. That encoding the opioid peptide precursor, proenkephalin, is regulated by a non-androgen testicular factor(s), specifically, spermatozoa or a spermatozoa-related factor. Thus, a complex array of nuclear events and signals received by the principal cells serve to determine the transcriptional status of genes expressed within this epididymal cell type.
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PMID:Differential patterns of regulated gene expression in the adult rat epididymis. 178 82

Two acidic secretory epididymal glycoproteins, protein D of 27,000 daltons and protein E of 28,000 daltons, have been purified and antisera prepared against each separately. Both proteins were found to share common immunological determinants when tested by double immunodiffusion and tandem crossed immunoelectrophoresis. By selective immunoprecipitation, protein D was shown to be synthesized and secreted by all regions of the epididymis with the exception of the initial segments. In contrast, the synthesis and secretion of protein E was restricted to the corpus and proximal cauda.
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PMID:Purification of rat epididymal proteins "D' and "E', demonstration of shared immunological determinants, and identification of regional synthesis and secretion. 717 30

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 mammalian epididymis is the site where spermatozoa are matured and then stored. Though many studies have described epididymal functions and their regulation, little is known about how aging affects this tissue. The Brown Norway rat, which does not show the many age-related pathologies common to other rat strains, was used as a model to study aging of the epididymis. The present study was designed to determine the effect of aging on the mRNA levels for selected markers of epididymal function. Brown Norway rats ranging in age from 6 to 30 months were examined at 6-month intervals; epididymides were sectioned into caput-corpus and cauda regions. Relative mRNA concentrations were assessed using Northern blot analysis and specific cDNAs for the rat 5 alpha-reductase isozymes, types 1 and 2; proenkephalin; the androgen receptor; epididymal proteins B/C and D/E; and sulfated glycoprotein-2 (SGP-2, clusterin). Northern blots were quantitated by densitometric scanning. In the caput-corpus epididymidis, 5 alpha-reductase type 1 and type 2 mRNA levels decreased significantly by 43% and 33%, respectively, between 6 and 12 months and by 64% and 40%, respectively, between 6 and 30 months. No significant change, however, was found in the expression of the 5 alpha-reductase mRNAs in the cauda epididymidis. Interestingly, proenkephalin mRNA was only detected in the caput-corpus epididymidis of 6-month-old rats. In marked contrast to the 5 alpha-reductase isozymes and proenkephalin, no significant age-related changes were observed in the mRNA levels for the androgen receptor, protein B/C, or protein D/E. No age-related changes in mRNA expression for SGP-2 occurred in the caput-corpus epididymidis. However, in the cauda epididymidis, SGP-2 mRNA levels rose by twofold between 6 and 18 months and then decreased sharply by 75% between 18 and 30 months. We conclude that as the epididymis ages, the expression of genes for certain specific markers of epididymal function is affected in a region-specific manner. Further, the decrease in the concentrations of the mRNAs for the 5 alpha-reductase isozymes and proenkephalin in the epididymis between 6 and 12 months is thus far the earliest marker for aging in the male reproductive tract of the Brown Norway rat.
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PMID:Gene expression in the aging brown Norway rat epididymis. 755 40

In vivo microperifusion and micropuncture were used to study tubule protein synthesis and proluminal secretion by the male reproductive tract in vivo. Seminiferous and caput and cauda epididymal tubules were perifused for 3 h. with [35S]-methionine. Perifused interstitial fluid (IF), lumen fluid (LF), and tubule extract (TE) were collected. Proteins were separated by SDS-PAGE, and autoradiograms were developed. Trichloroacetic acid precipitable proteins in each fluid were determined and a protein synthesis index (PSI) was calculated. PSI values demonstrated that the cauda epididymis synthesized less protein in vivo than did either seminiferous or caput tubules. Seminiferous tubules synthesized and secreted into the tubule lumen a relatively constant panel of proteins. Epididymal tubules synthesized and secreted proteins in a region-specific manner. In the caput epididymis the most prominent secreted bands were consistent with the heavy and light chains of epididymal clusterin. In the cauda epididymis, the most prominent synthesized and secreted protein was a 25 kDa protein consistent with the protein D. The above approach to studying protein synthesis and secretion will allow direct study of the physiological and pathophysiological effects on this important epithelial function in vivo.
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PMID:Assessment of protein synthesis and secretion by rat seminiferous and epididymal tubules in vivo. 799 57

Epididymis-secreted proteins D and E have been purified to homogeneity and partially characterized, and it is shown that monoclonal antibody (MAb) 4E9 (raised against a detergent extract of rat caudal epididymal sperm [Moore et al., 1994: Mol Reprod Dev 37(2):181-194]) recognizes protein E, but not protein D. The molecular weight of protein D (approximately 30 kD) is approximately 2 kD lower than protein E (approximately 32 kD). The NH2-terminus of each protein is blocked; however, microsequencing of internal peptides confirms earlier reports of significant sequence identity between the two proteins. High performance liquid chromatography tryptic peptide mapping showed peak differences between the two proteins, but it was not possible to obtain amino acid sequence in the peaks that were different. The epitope for MAb 4E9 was localized in the blocked NH2-terminus-CNBr peptide derived from protein E. The epitope was destroyed by protease treatment of protein E. Removal of N-linked oligosaccharides did not destroy the epitope for MAb 4E9 and did not affect the molecular weight difference between the proteins.
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PMID:Identification of the rat epididymis-secreted 4E9 antigen as protein E: further biochemical characterization of the highly homologous epididymal secretory proteins D and E. 886 48


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