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)

We have used perifusion organ culture of proximal and distal caput epididymal tubules of the rat to study the secretion of proteins by epididymal epithelium and uptake of the luminal radioactive proteins by sperm. The amount of incorporation of L-[35S]methionine into luminal fluid proteins was time dependent and completely inhibited by cycloheximide. The association of labeled proteins with cultured sperm was also dependent on time and continuous, with sperm still acquiring labeled luminal proteins after protein synthesis was arrested. A Mr = 46,000 molecule was found to be heavily labeled in luminal fluid and sperm extracts. Fluorograms of all L-[35S]methionine extracts immunoprecipitated using an antiepididymal alpha-lactalbumin antibody (Klinefelter and Hamilton, 1984) showed labeling of an Mr = 18,000 molecule and, in addition, the Mr = 46,000 molecule, but immunostaining was specific only for the Mr = 18,000 molecule and the heavy chain of the immunoglobulin. We suggest that the Mr = 46,000 molecule may be galactosyltransferase. Galactose oxidase-NaB[3H]4 labeling of the cultured caput sperm cell surface revealed a Mr = 23,000 molecule that was able to be immunoprecipitated with antiepididymal alpha-lactalbumin antibody. Our data suggest that this cell surface molecule is similar to one component of the fluid epididymal alpha-lactalbumin-like complex and, in addition, show that glycosylation of the sperm surface can occur in the caput epididymidis.
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PMID:Synthesis and secretion of proteins by perifused caput epididymal tubules, and association of secreted proteins with spermatozoa. 408 28

Autoantibodies raised in guinea pigs (GP) by hyperimmunization with epididymal sperm recognize antigens present on the plasma membrane of intact sperm and antigens associated with acrosome-reacted sperm. Plasma membrane autoantigens were characterized by SDS-PAGE analysis of immune precipitates from detergent extracts of radiolabeled epididymal sperm. Three major protein bands with approximate molecular weights (MW) of 69,000, 62,000 and 40,000 daltons were exhibited. Galactose oxidase and periodate oxidation followed by tritiation revealed two major plasma membrane glycoprotein autoantigens with MWs of 35,000 and 32,000 daltons and one sialoglycoprotein of 34,000 daltons. Antigenic molecules of similar MW were also detected by autoantisera to guinea pig testicular homogenates. Immune precipitates of radiolabeled detergent extracts of acrosome-reacted sperm analyzed by SDS-PAGE exhibited two major carbohydrate-containing peaks, one with a MW of approximately 42,000 daltons and one of 6,000 daltons. Since the 6,000 dalton peak was immunoprecipitated from the organic phase of both chloroform:methanol 2:1 and n-butanol extracts, the antigen may be a glycolipid. The possible existence of glycolipid autoantigen in GP sperm was further supported by the reaction in a solid phase radioimmunoassay of autoantibodies to GP sperm with glycolipid extracts from GP testis. This study demonstrates the presence of multiple autoantigenic specificities in the sperm-plasma membrane, acrosome-reacted sperm and testis of guinea pigs. It also demonstrates for the first time glycolipid autoantigens in testis and sperm.
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PMID:Immunochemical analysis of guinea pig sperm autoantigens. 703 3

Dietary carbohydrate activates the sympathetic nervous system (SNS). As the mechanisms underlying this response are not fully characterized, studies were undertaken to compare SNS responses to ingestion of glucose, fructose, and galactose. SNS activity was examined using techniques of [(3)H]norepinephrine ([(3)H]NE) turnover in brown and white fat. In addition, gene expression for several sympathetically related proteins was also analyzed in these tissues. [(3)H]NE turnover in interscapular brown adipose tissue (IBAT) and retroperitoneal fat increased in response to glucose and fructose in the diet, whereas [(3)H]NE turnover in epididymal fat did not respond to either monosaccharide. Galactose feeding, by contrast, decreased [(3)H]NE turnover in IBAT, but increased it in epididymal, though not retroperitoneal, fat. Expression of GLUT4 was more abundant in IBAT and retroperitoneal fat from glucose- and fructose-fed animals than from diet- or galactose-fed rats. Chemical sympathectomy abolished the GLUT4 response in retroperitoneal fat, but was without effect on GLUT4 in epididymal fat. These studies are consistent with activation of a neural pathway by oral glucose or fructose, leading to SNS activation in IBAT and retroperitoneal fat and enhanced GLUT4 expression.
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PMID:Effects of dietary monosaccharides on sympathetic nervous system activity in adipose tissues of male rats. 1511 96

To understand the cytochemical properties of epididymal epithelial cells, the characteristics of glycoconjugates in the mouse epididymis were examined using the technique of lectin histochemistry combined with immunohistochemistry. Characteristic staining patterns depending on the type of lectins were observed in the epididymal epithelium. Principal cells expressed N-acetyl-D-galactosamine (GalNAc), N-acetyl-D-glucosamine (GlcNAc), and Fucose in the proximal region of the epididymis and Mannose, Glucose, and Galactose in the distal region of the epididymis. Basal cells expressed Mannose, Glucose, Galactose, and GlcNAc in the proximal region and Galactose in the distal region. On the other hand, clear cells expressed various sugar residues and differences among regions were not observed. Interestingly, principal cells, clear cells, and basal cells specifically reacted with Ulex Europaeus-Agglutinin I (UEA-I lectin), Maackia Amurensis-Lectin I (MAL-I lectin), and Griffonia simplicifolia Lectin I-B4 (GS-I B lectin), respectively. These findings indicate that the selectivity in lectin reactivity for distinct cell types and segment-dependent staining in the epididymis may be related to cellular and regional differences in function. Furthermore, because some lectins stain particular cells or cellular compartments selectively, these lectins could be useful markers for histopathological evaluation of diseases or diagnosis of male infertility.
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PMID:Cell- and region-specific expression of sugar chains in the mouse epididymal epithelium using lectin histochemistry combined with immunohistochemistry. 2264 5

Using lectin histochemistry combined with immunohistochemistry, we recently demonstrated that the principal, clear, and basal cells in the adult mouse epididymis specifically react with UEA-I, MAL-I, and GS-IB lectins, respectively. The present study examined the distribution of the lectin-binding sites for some lectins on the epididymal epithelium during postnatal development. Galactose staining with GS-IB was first detected in some of the undifferentiated epithelial cells in mice aged 1 week, and this characteristic became specific to basal cells in mice aged 2 weeks and above. Fucose staining with UEA-I was first detected in the principal cells in mice aged 3 weeks. Staining of sialic acid with MAL-I was first detected in all undifferentiated epithelial cells in mice aged 1 week, and this characteristic became specific to the narrow and clear cells in all regions and to the principal cells in regions IV and V in mice aged 3 weeks. The results indicate that epididymal differentiation is characterized by the expression of cell- and region-specific sugar chains that appear early during postnatal development before the sperm arrives in the epididymis.
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PMID:Changes in lectin-binding sites on epididymal cells during postnatal development of the mouse. 2264 7