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)

Autologous or allogeneic spermatozoa in amounts of 10(8), 10(7), 10(6) or 10(5) incorporated in complete Freund's adjuvant were injected into hemiorchidectomized Hartley guinea-pigs. The course of autoimmune aspermatogenic orchi-epididymitis, delayed hypersensitivity and humoral responses to autologous and allogeneic spermatozoa and to spermatozoa autoantigens S, P and T (isolated from a large pool of spermatozoa) were investigated after 1,2,3 or 4 weeks of evolution. Testicular and epididymal lesions and the cellular and humoral responses to autoantigens S and T were nearly identical in autoimmunized and alloimmunized guinea-pigs; but the delayed hypersensitivity responses to whole spermatozoa was more frequent in alloimmunized than in autoimmunized guinea-pigs. This latter result might not be due to the addition of two responses on to autoantigens and one to alloantigens (both present in allogeneic spermatozoa) since the positive responses of the alloimmunized guinea-pigs to autologous spermatozoa compared to allogeneic were found more frequent. From the technical conditions of the experiments, especially due to the use of complete Freund's adjuvant, a helper effect originating in allotypic determinants on allogeneic spermatozoa seems an unlikely explanation. Autoimmunization or alloimmunization in incomplete Freund's adjuvant instead of complete adjuvant provoked a weak response. However, the antibody response to antigen S was significantly more frequent in alloimmunized than in autoimmunized animals; in this case allotypic determinants in autoantigen S responsible for a helper effect might be the cause.
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PMID:[Comparative study of immunopathogenic ability of autologous and allogeneic spermatozoa in Hartley guinea-pigs (author's transl)]. 43 85

In vitro delayed type hypersensitivity was demonstrated with peritoneal exudate cells from guinea pigs of the Rockefeller and Hartley strains, immunized with different preparations of the guinea pig male reproductive tract (RMT) emulsified in complete Freund's adjuvant-H37Ra. The RMT preparations were purified guinea pig spermatozoal autoantigens S, P, and T; whole guinea pig spermatozoa, and extract from epididymal tissue. The cellular sensitivity in vivo was demonstrated by injecting the proper antigen into the skin of the tested animals and in vitro by the macrophage inhibition technique. Peritoneal exudate cells from guinea pigs sensitized with whole guinea pig spermatozoa cells were inhibited in vitro by the specific antigen, epididymal extract, and autoantigen-T. Autoantigen-S was found to be a weak immunogen. However, the migration of peritoneal exudate cells from guinea pigs sensitized with large amounts of antigen-S was inhibited by whole spermatozoa in vitro. This cross-reactivity revealed the possibility that the immunogenicity of purified autoantigen-S might be connected to its molecular size. According to the immunizing dose of the antigens, testicular lesions of either the aspermatogenic or orchitis type were found in the testes of sensitized guinea pigs. Lesions in the testes of the guinea pigs were not detectable by cross-immunization with heterologous human or rat spermatozoa, although some degree of in vitro cross-reactivity was detected by skin test studies.
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PMID:Studies on sperm antigenicity. 2. In vivo and in vitro cellular reactivity in guinea pigs sensitized to homologous and heterologous spermatozoal autoantigens. 110 39

High affinity TSH binding has been reported in a variety of tissues other than the thyroid, most commonly in adipocytes and lymphocytes. This extrathyroidal binding of TSH has been documented most carefully in the guinea pig epididymal fat pad, where it has been postulated to be due to the presence of the TSH receptor (TSH-R). Extrathyroidal TSH-R expression has also been theorized to account for the associated dermopathy and ophthalmopathy seen in some patients with Graves' disease. We have isolated a cDNA encoding a fragment of the guinea pig TSH-R and have used this as a probe to study the distribution of TSH-R mRNA in the guinea pig. We show here that TSH-R mRNA is expressed in most white adipose tissues and in all brown adipose tissues tested. However, no expression was detectable by Northern analysis or in most polymerase chain reaction experiments using guinea pig retroorbital tissues, bringing into question the proposed role of the TSH-R as an autoantigen in autoimmune ophthalmopathy. The presence of significant amounts of TSH-R mRNA in most adipose tissues suggests a more important role for TSH in lipolysis and thermogenesis than previously thought.
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PMID:Thyrotropin receptor messenger ribonucleic acid is expressed in most brown and white adipose tissues in the guinea pig. 154 15

Temporal changes in the specificity of post-vasectomy autoantibodies to SDS-PAGE separated sperm antigens were investigated in Lewis rats. Sera were obtained from nine vasectomized animals prior to vasectomy, every two weeks for 14 weeks, and less frequently thereafter, up to 41 weeks. Changes in antisperm autoantibodies over time were assessed by ELISA and western blot assay and compared to antisperm isoantiserum and normal Lewis rat serum. A "biphasic" pattern of autoantibody production over time was observed in a majority of individuals. This pattern was characterized by early phase autoantibodies, produced between 0 and 6 weeks after vasectomy, which bound antigens at the stacking, separating and ionic fronts and by late phase autoantibodies, produced after 4 weeks following vasectomy which bound antigens at 86, 63, 52, 43, 31 and 26 kDa. Previous work suggested that some high molecular weight autoantigens were disulfide-bonded polymers of the polypeptides at 86, 63, and 43 kba (Handley, et al., 1988). Indirect immunofluorescence with monospecific isoantisera to the 86 kDa autoantigen suggested that its corresponding high molecular weight polymer was located in the tail of cauda epididymal spermatozoa. This polymer possessed several characteristics of T cell independent autoantigens. These data show a change in the specificity of autoantibodies produced over time after vasectomy which may reflect a shift from T cell independent to T cell dependent autoantibody production by the Lewis rat.
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PMID:Biphasic production of antisperm autoantibodies follow vasectomy of the Lewis rat. 218 36

Active experimental allergic orchitis (EAO), characterized by inflammation of the testes (autoimmune orchitis), aspermatogenesis, epididymitis and vasitis was induced in mice using a panel of tissue antigens as immunogens. Immunization with allogeneic murine tissue homogenates emulsified in complete Freund's adjuvant (CFA) accompanied by the injection of pertussigen revealed that only adult murine testicular and epididymal homogenates are capable of eliciting murine EAO. All other tissue antigens studied including prepubertal mouse and epididymal homogenates failed to elicit significant disease. Immunization with xenogeneic testicular antigens also failed to elicit significant disease indicating that the major murine aspermatogenic autoantigen(s) is also highly species specific. Sensitization with allogeneic mouse testicular homogenates (MTH) from different disease resistant strains was for the most part no less potent in inducing significant disease than was immunization with mouse testicular homogenates from disease susceptible strains. However, testicular homogenates from NZB/B1NJUnm and MRL/MpJ-/+Unm mice were significantly less potent at inducing autoimmune epididymitis as compared to other strains, indicating possible interstrain differences in the immunogenicity of the aspermatogenic autoantigen(s) relevant to eliciting epididymitis. Attempts at solubilization and purification of the major murine aspermatogenic autoantigen(s) utilizing techniques employed for the purification of aspermatogenic autoantigens such as AP3 from guinea pig (GP) testes were unsuccessful. Additional extraction procedures resulted in solubilization of the relevant autoantigen(s) only after reduction in the presence of 6 M guanidine hydrochloride. These data suggest that: (1) there may be a much more limited number of aspermatogenic autoantigens in murine testes as compared to GP testes; (2) the disease inducing determinant(s) may be expressed as either a sequential antigenic determinant(s) or as an antigenic determinant(s) in the carbohydrate portion of a glycoprotein or glycopeptide; and (3) the disease inducing autoantigen(s) may be present in situ in a highly insoluble form requiring active processing within the target organ in order to generate soluble antigen capable of being seen by immune reactants.
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PMID:Experimental allergic orchitis in mice: IV. Preliminary characterization of the major murine testis specific aspermatogenic autoantigen(s). 350 Oct 13

A soluble aspermatogenic autoantigen (AP2) capable of inducing experimental allergic orchitis (EAO) in the guinea pig has been isolated from the soluble acrosomal contents (SAC) released from guinea pig cauda epididymal sperm during the in vitro Ca+2 ionophore A23187-induced acrosome reaction. AP2 purification was achieved by heat inactivation of SAC enzymatic activity, followed by chaotropic solubilization and ultracentrifugation, gel filtration on Sephadex G-50, preparative isoelectric focusing, and SDS-polyacrylamide gel electrophoresis. Approximately 80 micrograms of AP2 was obtained from 1 to 2 x 10(10) cauda epididymal sperm. AP2 has a m.w. of 9500 +/- 1500 as determined by unreduced SDS-PAGE and an isoelectric point of 5.52 +/- 0.11. Amino acid analysis of AP2 indicates that it is a protein. AP2 has no detectable hexose or hexosamine as determined by gas liquid chromatographic analysis and is therefore probably not a glycoprotein. Five micrograms of AP2 are capable of inducing severe EAO in 100% of guinea pigs tested, whereas 0.5 to 2.0 micrograms induces mild lesions consisting primarily of aspermatogenesis in 66% of guinea pigs tested.
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PMID:Acrosomal autoantigens of guinea pig sperm. I. The purification of an aspermatogenic protein, AP2. 684 85

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

We have cloned and sequenced cDNAs encoding autoantigen 1 (AA1), a testis-specific protein and the major autoantigen of the guinea pig sperm acrosome. The cDNA predicts a precursor protein of 244 amino acids including a 21 amino acid hydrophobic, secretory signal sequence. The mature polypeptide is predicted to have a molecular mass of 24,891 Daltons which agrees with the experimentally determined molecular weight of 25,000. Consistent with previous studies demonstrating that AA1 is not a glycoprotein, the predicted amino acid sequence contained no canonical sites for N-linked glycosylation. Comparison with other sequences showed that AA1 is the guinea pig homologue of the testis-specific protein Tpx-1 in mice and TPX1 in humans. AA1 also showed significant amino acid sequence homology with other cysteine-rich secretory proteins (CRISP's): rat and mouse acidic epididymal glycoproteins (AEG; also known as proteins D/E in rats) and helothermine, a toxin from the Mexican beaded lizard. In addition, AA1 had a lesser degree of homology with antigen 5 (vespid wasp venom), PR-1 (a plant pathogenesis related protein), and GliPR (a protein identified in human gliomas). Northern analysis of RNA from purified guinea pig spermatogenic cells showed that a 1.5 kb message was first detected in pachytene spermatocytes, was strongest in round spermatids, and was detected at a low level in condensing spermatids. Immunoblot analysis and metabolic labeling data of AA1 in spermatogenic cells showed that the protein was synthesized as early as the pachytene spermatocyte stage of spermatogenesis. Thus, the patterns of AA1 mRNA and protein expression during spermatogenesis are similar to the expression of other acrosomal mRNAs and proteins that are first detected meiotically.
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PMID:Autoantigen 1 of the guinea pig sperm acrosome is the homologue of mouse Tpx-1 and human TPX1 and is a member of the cysteine-rich secretory protein (CRISP) family. 911 20

A cDNA encoding an acidic epididymal glycoprotein (AEG)-like, CRISP1 (cysteine-rich secretory protein) protein from the monkey (Macaca mullata) epididymis has been cloned and sequenced. The monkey AEG (mAEG) has an open reading frame that encodes a protein containing 249 amino acids with a deduced molecular mass of 28 kDa. The mAEG protein sequence is 85% identical to human and 44% identical to mouse CRISP1, including all 16 conserved cysteine residues. mAEG also shows a significant amino acid homology with other CRISP proteins, rat AEG/DE, human TPX1/CRISP2, and guinea pig acrosomal autoantigen 1 (AA1). In addition, mAEG shows somewhat less homology to a toxin from the Mexican beaded lizard and to a human glioma pathogenesis-related protein. Northern blot analysis shows that the mRNA for mAEG is expressed in all the regions of the epididymis except the caput and was not detected in the testis, prostate, seminal vesicle, and brain. In castrated animals, mAEG gene expression in the epididymis is significantly diminished; however, testosterone enanthate replacement restored the normal level of expression, demonstrating that expression of mAEG is androgen dependent. Western blot analysis of monkey epididymal regions using mouse antirecombinant human AEG identified a 28-kDa protein only in the caudal region. Immunohistochemical analysis identified mAEG only in the principal cells of the cauda epididymal epithelium. Immunofluorescence analysis identified mAEG on the principal piece of the sperm tail and as small patches over the middle piece and head regions. The results described in the present study suggest that mAEG (CRISP1) is secreted in the monkey epididymis, regulated by androgens and present on epididymal spermatozoa.
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PMID:Cloning and characterization of an androgen-dependent acidic epididymal glycoprotein/CRISP1-like protein from the monkey. 1038 18

Thioredoxins compose a growing family of proteins that participate in different cellular processes via redox-mediated reactions. We report here the cloning, developmental expression, and location of murid Sptrx-2. Mouse and rat SPTRX-2 proteins display a high homology to their human ortholog in the thioredoxin and NDP kinase domains, and the coding genes are located at syntenic positions. Northern blotting and in situ hybridization confirmed the testis-specific expression of murine Sptrx-2 mRNA, mostly in round spermatids. Immunohistochemical analysis of the 19 steps of rat spermiogenesis showed that SPTRX-2 expression becomes prominent in the cytoplasmic lobe of step 15-18 spermatids and diminishes in step 19 just before spermiation. However, in the spermatid tail, SPTRX-2 immunoreactivity increased from step 15 to 19 and was confined to the principal piece. By immunogold electron microscopy, SPTRX-2 was first detected scattered throughout the cytoplasm of the axoneme in step 14-15 spermatids, but began to be incorporated by step 16 into the fibrous sheath (FS). During steps 17-18, the labeling increased over the ribs and columns of the assembled FS. It peaked in step 19 and remained in the FS of epididymal spermatozoa. Immunoblots of isolated FS obtained from spermatozoa confirmed that SPTRX-2 is an integral component of the FS and a post-obstruction autoantigen in vasectomized rats. Our data indicate that SPTRX-2 incorporation into the FS lags well behind FS assembly, suggesting it is required during the final stages of sperm tail maturation in the testis and/or epididymis, where extensive disulfide bonding of FS proteins occurs.
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PMID:Cloning and developmental analysis of murid spermatid-specific thioredoxin-2 (SPTRX-2), a novel sperm fibrous sheath protein and autoantigen. 1290 33


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