Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Autoregulation of androgen receptor (AR) mRNA was investigated using Northern blot analysis with AR cDNA fragments as probes. The amount of AR mRNA increased 2- to 10-fold with androgen withdrawal and decreased below control levels after androgen stimulation in rat ventral prostate, coagulating gland, epididymis, seminal vesicle, kidney, and brain, and in a human prostate cancer cell line, LNCaP. In rat ventral prostate, AR mRNA increased 2- to 3-fold within 24 h after castration and remained elevated for 4 days. Treatment with testosterone propionate beginning 24 h after castration reduced ventral prostate AR mRNA 4-fold within 8 h of androgen replacement. Administration of estradiol 24 h after castration had no significant effect on prostatic AR mRNA. Androgens, including testosterone and the synthetic androgen methyltrienolone (R1881), or the antiandrogen cyproterone acetate down-regulated AR mRNA in vitro in LNCaP cells, whereas estradiol was without effect. Administration of testosterone propionate to rats with androgen insensitivity did not decrease AR mRNA. Down-regulation of AR mRNA by androgen is therefore a receptor-mediated process which occurs in vivo in rat tissues that differ in androgen responsiveness and in cultured human prostate cells.
Mol Endocrinol 1990 Jan
PMID:Autologous down-regulation of androgen receptor messenger ribonucleic acid. 232 67

The level of SH-group oxidation in spermatozoa from the cauda epididymis was measured by a cytofluorometric method in chromosomally normal mice and two chromosome mutants. The first one, a tertiary trisomic karyotype (Ts(1(13]7OH), is characterized by severe oligospermia and high levels (approximately 75%) of malformed spermatozoa. The second, a hybrid between two European feral mouse stocks, is heterozygous for multiple Robertsonian translocations and produces exclusively aneuploid spermatozoa. Neither the severe teratospermiogenesis nor the severe aneuploidy was reflected in total SH-group fluorescence values nor in free SH-group fluorescence. It is concluded that both the production of protamines and protamine cross linking by S-S bridge formation are rather autonomous processes during spermatogenesis because 1) the increased DNA variance of the aneuploid spermatozoa is not reflected in an increased variance of the total and free SH-groups, 2) aneuploidy for the protamine gene carrying chromosome 16 is not reflected by the SH-group values for individual spermatozoa, and 3) protamine production and cross linking are independent of the mild to severe terataspermiogenesis in the tertiary trisomic karyotype.
Mol Reprod Dev 1990 Mar
PMID:Protamine amount and cross linking in mouse teratospermatozoa and aneuploid spermatozoa. 233 77

The synthesis and secretion of proteins in the different regions of the human epididymis were studied in vitro. Epididymal tissues obtained from patients undergoing castration for prostatic carcinoma or from cadavers were incubated in the presence of [35S]methionine, and the resulting radiolabeled proteins were analysed on SDS-PAGE. The corpus region was found to be the most active segment in total protein synthesis. Significant qualitative and quantitative changes were observed in the pattern of proteins secreted from the different epididymal regions. To establish those epididymal proteins that interact with maturing sperm, the secreted products were immunoreacted with antibodies raised against a Triton X-100 extract of ejaculated human sperm heads. The antibodies react mainly with the head region of ejaculated spermatozoa as judged by indirect immunofluorescence. Protein A-gold labeling of freeze-fracture images showed gold particle distribution on the sperm plasma membrane. Western blot analysis of the secreted proteins revealed four bands (66, 37, 32, and 29 kDa) in the proximal regions and six additional bands (80, 76, 48, 27, 22, and 17 kDa) in the distal part of the epididymis. Immunoprecipitation of the secreted proteins with these antibodies revealed six radioactive bands of 170, 80, 76, 60, 48, and 37 kDa, which indicates that certain proteins of epididymal origin bind to the sperm plasma membrane.
Mol Reprod Dev 1990 May
PMID:Protein synthesis and secretion in the human epididymis and immunoreactivity with sperm antibodies. 234 42

Disruption of normal calcium homeostasis has been implicated in the development of cell injury by certain chemicals. Furthermore, calcium channel blockers, which may prevent such a disruption, were shown to protect against this type of cellular damage in some excitable and nonexcitable tissues. Therefore, the present work was designed to address the role of calcium in the pachytene cell death caused by ethylene glycol monomethyl ether (EGME) by investigating the effect of the calcium channel blockers, verapamil and diltiazem, on the pathogenesis of such lesions. Male F344 rats were treated with a single gavage dose of 200 or 300 mg EGME/kg. Other groups of rats were treated with the same doses of EGME in combination with one, two, three, or four doses of verapamil or diltiazem. Twenty-four hours after administration of EGME, the animals were sacrificed, and the left testis and epididymis were excised, fixed in Bouin's solution, embedded in paraffin, sectioned, and stained with PAS-H. The sections were evaluated "blind" and scored for the number of lesioned stage XIV tubules. At 200 mg/kg, EGME produced a moderately severe lesion as characterized by pachytene spermatocyte cell death in stage XIV semniferous tubules. Verapamil was protective against this lesion with the protection being directly proportional to the number of verapamil doses administered and was maximum in rats treated with three doses. At 300 mg/kg, EGME caused a severe lesion in the testis, and verapamil was not as effective in protecting against this lesion as against the low dose of EGME. In contrast, diltiazem was not as effective as verapamil at either dose of EGME. These studies show, for the first time, that verapamil protects rats against EGME-induced testicular toxicity.
Exp Mol Pathol 1990 Jun
PMID:Calcium channel blockers protect against ethylene glycol monomethyl ether (2-methoxyethanol)-induced testicular toxicity. 236 34

The fertilization antigen (FA-1) isolated from murine testes demonstrated its dimeric form of 49,000 +/- 2,000 molecular weight (M.W.) or a monomer of 23,000 M.W. on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The FA-1 was immunogenic in all three female rabbits tested and raised a high-titer antisera [enzyme-linked immunosorbent assay (ELISA) titers; 1:1,024 to 1:4,096]. The rabbit anti-FA-1 antisera predominantly recognized the dimeric form of 49,000 +/- 2,000 M.W. on the Western blot of lithium diiodosalicylate (LIS)-solubilized murine testes. None of the antisera reacted with any somatic tissue, indicating germ-cell specificity of FA-1. To determine the cellular localization of the immunoreactive FA-1, a novel ultrasensitive immunogold-silver staining (IGSS) procedure was developed. The anti-FA-1-IgG showed intense staining in the luminal region of the seminiferous tubules containing spermatids and spermatozoa. No reaction was observed in the peripheral area of the tubules containing Sertoli cells, spermatogonia, leptotene, and zygotene spermatocytes. The biodistribution studies of 125I-labeled anti-FA-1 IgG in mice revealed that the antibodies do not bind to somatic tissues such as blood cell, liver, heart, kidney, muscle, and gastrointestinal tissue and do not transudate into testes and seminal vesicle. However, the antibodies preferentially transudate into epididymis (especially corpus or cauda regions) and vas deferens to bind to sperm cells. In conclusion, our data indicate that FA-1 can induce an immune response that is germ cell-specific, directed against later stages of spermatogenesis. The antibodies to FA-1 interact with sperm after penetration through epididymis (especially corpus and cauda regions) and vas deferens rather than through testes and seminal vesicles.
Mol Reprod Dev 1990 Jun
PMID:Antibodies to sperm surface fertilization antigen (FA-1): their specificities and site of interaction with sperm in male genital tract. 237 99

Acidic epididymal glycoprotein (AEG) is a 31,000 molecular weight secretory protein of the rat epididymis. Screening of a rat epididymal cDNA library with affinity-purified AEG antiserum yielded cDNA for AEG. Identity of the clones was verified by comparison of amino acid sequence of the purified protein with the sequence derived from the nucleotide sequence of the cDNA isolates. Two classes of AEG cDNA, approximately 1500 base pairs (bp) and 950 bp in length, differed by 538 bp in the 3'-untranslated region and by four single nucleotide mismatches, one of which was in the coding region. Northern blot hybridization of epididymal RNA revealed two species of AEG mRNA, corresponding in length to each type of cDNA. Analysis of RNA from individual animals provided evidence that the two mRNA species are the products of allelic genes. In vivo studies demonstrated that the level of total AEG mRNA is regulated by androgen. Amino acid sequence homology of AEG with metal-binding domains of several proteins suggests that AEG is a metalloprotein.
Mol Endocrinol 1988 Oct
PMID:Molecular cloning of complementary deoxyribonucleic acid for an androgen-regulated epididymal protein: sequence homology with metalloproteins. 246 Jul 53

Flow cytometric measurements were made on acridine orange (AO) and 7-diethylamino-3-(4'-maleimidylphenyl)-4-methyl-coumarin (CPM)-stained epididymal- and vas deferens-derived spermatozoal nuclei to follow the course of chromatin condensation and oxidation of free sulfhydryl groups, respectively, during passage through mouse and rat posttesticular reproductive tracts. Alterations of mouse and rat spermatozoal chromatin during transition from a testicular elongated spermatids to epididymal caput spermatozoa resulted in a threefold loss of DNA stainability with AO. Passage of spermatozoa from the caput to corpus epididymis was accompanied by an approximate 15% loss of DNA stainability, which was maintained at that level throughout passage into the vas deferens. AO stainability of epididymal spermatozoal nuclei was generally independent of -SH group stainability. CPM stainability of rat spermatozoal nuclei free -SH groups was 83%, 18%, and 11% of caput spermatozoal values for corpus, cauda epididymis, and vas deferens, respectively. Comparable values for mice were 69%, 20%, and 18%. CPM stainability was relatively homogeneous for these mouse and rat reproductive tract regions, except mouse corpus epididymis spermatozoal nuclei stained very heterogeneously. Rat spermatozoa detained by ligature up to 7 days in the caput, corpus, and cauda epididymi had CPM staining values equal to or below those of normal vas spermatozoa, indicating that disulfide (S-S) bonding is intrinsic to the spermatozoa and is independent of the epididymal environment. These data suggest that chromatin condensation and loss of spermatozoal DNA stainability during passage from the testis to the vas deferens are independent of S-S bonding.(ABSTRACT TRUNCATED AT 250 WORDS)
Mol Reprod Dev 1989
PMID:Flow cytometric analysis of rodent epididymal spermatozoal chromatin condensation and loss of free sulfhydryl groups. 248 18

The mRNA for the opioid peptide precursor proenkephalin is widely distributed throughout the male and female reproductive systems of rodents. In the present studies, the concentrations of proenkephalin-derived peptides in selected reproductive tissues of the rat have been determined. When compared with previously characterized tissues such as brain, the peptide contents in reproductive tissues were unexpectedly low relative to the abundance of proenkephalin mRNA. This suggested that either translation of proenkephalin mRNA is relatively inefficient in reproductive tissues or that the turnover of proenkephalin products occurs at a higher rate, or both. To distinguish between these possible mechanisms, the polysomal distributions of proenkephalin mRNA in different rat reproductive tissues and in rat brain were determined. In adult rat testis, in which the predominant proenkephalin RNA is the 1700-nucleotide form present in spermatogenic cells, the transcript was found to be mainly associated with translationally inactive ribonucleoprotein fractions. In contrast, the 1450-nucleotide form of proenkephalin mRNA appeared to be translated to a similar extent in rat brain, epididymis, ovary, and somatic cells of the immature rat testis. It therefore appears that inefficient translation of proenkephalin mRNA in spermatogenic cells is a major determinant of the low ratio of proenkephalin peptides to RNA in the adult rat testis, while posttranslational mechanisms (most likely peptide turnover) are involved in the rat epididymis, ovary, and presumably other reproductive tissues. These findings also indicate that mRNA and/or translation product concentrations within a given tissue are not always accurate indicators of the level of peptide or protein production.
Mol Endocrinol 1989 Aug
PMID:Translational status of proenkephalin mRNA in the rat reproductive system. 257 Oct 79

Lizard epididymis is an androgen-dependent tissue which produces notably ten related secretory proteins (L-proteins, Mr 19,000) during the reproductive period. These proteins were synthesized in vitro as preproteins (Mr 25,000, 24,000, 23,500). A cDNA library in the plasmid pBr322 was constructed and two cDNA clones were isolated by differential hybridization according to the differential expression of the mRNAs in stages 1 and 6 of the annual reproductive cycle. Translations of mRNAs hybrid-selected by two clones (LV123, LV132) yielded proteins which were immunoprecipitated by the L-antiserum. These preproteins were processed in vitro into six peptides; four were encoded by mRNAs selected with the LV123 clone, the others by the LV132 clone. Only three bands were detected using Northern blot analysis suggesting that the L-family could be derived from various mRNAs and from post-translational maturations. Southern analysis of genomic DNA suggests that the L-mRNAs were encoded by at least two distinct genes which could exist in numerous copies. The L-gene expression was studied under various physiological conditions and was found to be androgen-dependent. Furthermore, the results suggest the presence of a translational regulation in the newly differentiated epithelial cells.
Mol Cell Endocrinol 1989 Mar
PMID:Molecular cloning of two cDNAs for related secretory proteins in lizard epididymis: gene expression during androgen-induced cell growth and secretion. 274 23

Androgen-binding protein (ABP) is a testicular Sertoli cell secretory protein that acts as a carrier of androgen in the male reproductive tract. ABP has been characterized from a wide range of animal species, including man, rabbit and rat. However, it has been widely accepted that mice do not produce testicular ABP. We have used immunological and molecular biological techniques to demonstrate that the ABP gene is expressed in the CD1 mouse. Steroid-binding, radioimmunoassay and immunocytochemical studies demonstrated that ABP is present in mouse testis and epididymis, but at 1/50 to 1/25 the level of rat epididymis. A 1.7 kilobase mRNA, homologous with rat ABP cDNA, was identified in mouse testis and Sertoli cells by Northern blot hybridization, but at a much lower level than in the rat. An ABP cDNA was isolated from a mouse testis cDNA library and encoded a protein (403 residues) with 89% of the amino acid residues identical to rat ABP, including a signal peptide. Our results indicate that ABP is expressed in the mouse and past failures to detect androgen-binding activity were due to the low level of ABP protein.
Mol Cell Endocrinol 1989 May
PMID:The androgen-binding protein gene is expressed in CD1 mouse testis. 275 30


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