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)

A number of dye-ligand adsorbents have been examined for purifying and characterizing 1,25-dihydroxyvitamin D3-receptor complexes from intestines of vitamin D3-deficient chickens. In particular, several triazinyl dyes--Cibacron blue F3GA, Procion red HE3B, and Green A dye, immobilized to agarose via an ether linkage--retain specifically bound 1,25-dihydroxyvitamin D3-receptor complexes formed at 0-4 degrees which are eluted at high salt concentrations. Moreover, receptor binding to these dye-ligand matrices occurs in the presence and absence of sterol. At least for Cibacron blue, the strength of receptor binding depends critically on the method of dye coupling to matrix. The concentration of KCl required for elution of receptor from the triazine ether-linked matrix is greater than coupling through the amine of the anthraquinone via a 10-atom spacer arm approximately equal to coupling through the amine of the anthraquinone via an isourea bond greater than Cibacron blue dextran. Data are presented which demonstrate that sterol-receptor complexes formed at 25 degrees have reduced affinity for dye-ligands when compared with sterol-receptor complexes formed at 0-4 degrees. It is suggested that this finding is related to proteolytic alterations of the receptor, since limited digestion with trypsin can mimic this phenomenon and several protease inhibitors can reduce the thermal-induced alterations. Biospecific elution of receptor is demonstrated using synthetic polyribonucleotides. Preference for polyguanylic and polyinosinic acid is observed over several other polyribonucleotides and mononucleotides. The data in this study, viewed collectively, suggest that there is a specific interaction between the polynucleotide domain of the 1,25-dihydroxyvitamin D3-receptor and several triazinyl dye-ligands. It is concluded that these dye-ligands should prove to be of considerable interest for facile chromatography to purify and characterize this receptor.
Mol Pharmacol 1984 Jan
PMID:Dye-ligand interactions with 1,25-dihydroxyvitamin D3-receptor complexes from chicken intestine. 632 53

The binding of 1,25-dihydroxyvitamin D3-receptor complexes from chick intestinal cytosol to DNA-cellulose and isolated intestinal nuclei is inhibited by several dye-ligands in a dose-dependent manner. Concentrations of Cibacron blue F3GA, blue dextran, Procion red HE3B, and Green A dye causing 50% competition for receptor binding to DNA-cellulose ranged from 2.8 to 3.6 microM. A structural analogue of the anthraquinone moiety of Cibacron blue F3GA, bromaminic acid, was 111-fold less potent in inhibiting DNA-cellulose binding. Moreover, the inhibitory effects of these dye-ligands is not due to a simple electrostatic effect, since two other polyanions, heparin and poly-L-glutamate, are much less effective. Whereas dye-ligands can cause the release of receptors bound to DNA-cellulose, they do not alter the dissociation of 1,25-dihydroxyvitamin D3 from its receptor nor do they affect the apparent equilibrium binding constant of the receptor or the concentration of available sterol-binding sites. The inhibition of binding by dye-ligands is competitive with respect to DNA-cellulose binding, indicating that the effect of these dyes is at a domain common to polynucleotides.
Mol Pharmacol 1984 Jan
PMID:Specificity of dye-ligand interaction with the polynucleotide binding domain of 1,25-dihydroxyvitamin D3-receptor complexes of chicken intestinal cytosol. 632 54

Human epididymal tubules from 9 patients undergoing orchidectomy were cultured for periods of up to 8 days with preservation of the histological structure of the tissue. Addition of androgens (testosterone, 5 alpha-dihydrotestosterone and 5 alpha-androstane-3 alpha, 17 beta-diol) significantly increased the epithelial height, the incorporation of [3H]amino acids and [3H]thymidine. The effect on protein synthesis was significant 48 h after the onset of treatment and was maximal after 3 days. The effect on DNA replication was maximal during the 3rd day of treatment. In both instances maximal activity was achieved at a concentration of 10(-7) M of testosterone. Cyproterone acetate (10(-5) M) was able to negate all effects of androgens.
Mol Cell Endocrinol 1981 Mar
PMID:The organ culture of hunan epididymal tubules and their response to androgens. 645 2

Dimethyl methylphosphonate (DMMP) is an organophosphorous compound that impairs fertility in male rodents. In previous studies, male rats treated with DMMP had decreased sperm motility and count, and sired fewer litters with fewer pups per litter. The following studies examined the development of the reproductive lesions by light and electron microscopy after treatment with DMMP. Adult male F344 rats were treated po with DMMP, 1750 mg/kg, for up to 12 weeks. Tissues were perfused in situ with Karnovsky's fixative and embedded in glycol methacrylate. After 5 weeks of treatment there were occasional PAS-positive bodies in lumina of tubules in stages XII-III. These were ultrastructurally similar to cytoplasm of step 12-17 spermatids. After 7 weeks of treatment, there was an increase in the number of tubules exhibiting these bodies, as well as an increase in the number of tubules showing delayed or early spermiation, or focal exfoliation of nonnecrotic cap-phase spermatids and some spermatocytes. No multinucleated giant cells were seen. Focal loss of germ cells occurred more frequently as duration of exposure increased, and occupied 5-100% of an affected tubule. Frequently, an area of germ cell exfoliation occurred adjacent to areas of normal tubular epithelium. These lesions were not specific to any particular stages of spermatogenesis. Occasionally, elongating spermatids were without rib elements of the fibrous sheath in the tail; these were not seen in epididymal sections. Animals left to recover for 14 weeks after treatment showed approximately 80% normal tubules; affected tubules varied in their degree of recovery, but all showed the loss of normal epithelial organization, a characteristic of DMMP treatment. Epididymal epithelium was not visibly affected by treatment with DMMP. DMMP produced morphologic alterations in Sertoli cells and elongating spermatids, as well as producing functional defects in spermatozoa.
Exp Mol Pathol 1984 Aug
PMID:Development of reproductive tract lesions in male F344 rats after treatment with dimethyl methylphosphonate. 646 31

Androgen-binding protein (ABP) is present in the guinea-pig testis, epididymis and epididymal fluid. Guinea-pig ABP sediments as an approx. 4.6S species on sucrose gradients containing 0.01 M KCl. Electrophoresis on non-denaturing polyacrylamide gels indicated that specific androgen binding was present in epididymal cytosol, but not in plasma. Time-course studies indicated that binding equilibrium is approached in about 2.5 h; the dissociation half-time of [3H]5 alpha-DHT from guinea-pig ABP is 5.64 +/- 0.62 h (n = 6) at 4 degrees C. The relative affinities of some steroids for guinea-pig ABP in relation to 5 alpha-DHT = 1 are: testosterone = 0.55 +/- 0.13 (n = 4), estradiol = 0.14 +/- 0.03 (n = 4), the anti-androgen cyproterone acetate = 0.0025 +/- 0.0002 (n = 3). Guinea-pig ABP exhibited an equilibrium dissociation constant of 6.34 +/- 0.52 nM (n = 3) at 4 degrees C and there were 3.43 +/- 0.78 (n = 3) pmoles of binding sites per mg of protein when homogenates of the whole epididymis were assayed. The concentration of ABP was lowest in the caput-corpus region of the epididymis, highest in the proximal cauda, and intermediate in the distal cauda. Essentially all of the ABP present in the distal cauda was intraluminal, as evidenced by the fact that flushing of the duct eliminated most of the [3H]5 alpha-DHT binding activity.
Mol Cell Endocrinol
PMID:The presence of androgen-binding protein in the guinea-pig testis, epididymis and epididymal fluid. 689 45

Differential screening of a human epididymal cDNA library led to the isolation and characterization of a major epididymis-specific cDNA clone family, referred to as HE3. More detailed sequence and PCR analysis identified two different but homologous gene transcripts, HE3 alpha and HE3 beta. The former represents an mRNA of ca. 1 kb, encoding a putative small secretory polypeptide of 14903 MW. The HE3 beta transcript was only found as incomplete 3' fragments. Analysis of human genomic DNA by Southern blotting suggested the presence in the human genome of at least three independent HE3-related genes. Isolation of genomic clones for the HE3 alpha gene showed this to contain a single intron of 1.4 kb in the 5' noncoding region. Although genomic clones corresponding to HE3 beta could not be found, a third highly homologous gene, HE3 gamma, was identified as a potential pseudogene. Neither nucleotide nor encoded amino acid sequences of the HE3 gene family are related to any other known sequence in the central databases, and thus represents a novel human gene family, with at least three nonallelic members. Northern hybridization analysis showed that HE3 gene products are specifically expressed in the human epididymis, and not in any other tissue examined. Furthermore, except for the pig, no other nonprimate species has been identified to express homologous sequences in the epididymis. RNase protection assays showed that both the HE3 alpha and HE3 beta, but not the HE3 gamma genes, are expressed in the human epididymis.
Mol Reprod Dev 1994 Feb
PMID:Major human epididymis-specific gene product, HE3, is the first representative of a novel gene family. 751 8

Hyaluronic acid, a major component of the extracellular matrix, plays an important role in the regulation of different cellular processes, e.g., locomotion, cell-cell interaction during morphogenesis, and differentiation. Distribution of hyaluronic acid with respect to the role of sperm hyaluronidase in sperm penetration and gamete interaction is well established. In order to elucidate this mechanism, in our current study we have identified and demonstrated, for the first time, the presence of a 68-kDa cell surface hyaluronic acid binding glycoprotein (HABP) in spermatozoa of different species (rat, mice, bull, and human) by immunoblot analysis and indirect immunofluorescence using the polyclonal antibodies raised against purified HABP. Furthermore, we were able to demonstrate a differential distribution of 68-kDa HA binding protein on the sperm head, midpiece, and tail of different species. To identify its role in sperm function, we observed its declining pattern during epididymal maturation and also the inhibition of sperm-oolemmal adherence by pretreatment of the sperms with anti-HABP antibodies. We have further observed its in vivo phosphorylation in motile spermatozoa. All our data clearly indicate that sperm hyaluronan binding protein may have a specific role in sperm maturation, motility, and fertilization processes.
Mol Reprod Dev 1994 May
PMID:Evidence for presence of hyaluronan binding protein on spermatozoa and its possible involvement in sperm function. 751 32

Galactosyl receptor, a cell surface Ca(2+)-dependent lectin with binding affinity for galactose, was evaluated by immunoblotting, immunoprecipitation, Northern blotting, and immunocytochemistry in human liver, testis, and sperm. Polyclonal antisera raised against the minor asialoglycoprotein receptor variant of rat hepatocytes (designated rat hepatic lectin-2/3, RHL-2/3), and its human liver-equivalent (designated H2), recognize native galactosyl receptor in the testis and sperm in immunoblotting, immunoprecipitation, and immunocytochemical experiments. An equivalent to the major hepatocyte asialoglycoprotein receptor variant (rat RHL-1 and human H1) was not detected. Human testis and sperm galactosyl receptor was resolved, after immunoprecipitation and immunoblotting, as a single protein component of molecular mass 50 kD. The single protein component in human testis and sperm contrasted with the doublet nature of rat testis and sperm galactosyl receptor, consisting of two components of molecular masses of 54 and 49 kD. Northern blotting experiments using radiolabeled H1 and H2 cDNA probes confirmed the presence of H2 mRNA and the lack of H1 mRNA in the human testis. Immunocytochemical studies detected specific antigenic sites on the entire surfaces of spermatogenic cells. However, immunoreactivity in epididymal and ejaculated sperm was confined to head surfaces overlying the acrosome. Results from these studies, and from previous studies in the rat, suggest that the testis/sperm galactosyl receptor is a C-type Ca(2+)-dependent lectin with possible roles in cell-cell interaction during spermatogenesis and sperm-zona pellucida binding at fertilization.
Mol Reprod Dev 1995 Apr
PMID:Galactosyl receptor in human testis and sperm is antigenically related to the minor C-type (Ca(2+)-dependent) lectin variant of human and rat liver. 759 12

In previous studies we identified an epididymal gene that exhibits homology to the cystatin family of cysteine protease inhibitors. The expression of this gene, termed CRES (cystatin-related epididymal and spermatogenic), was shown to be highly restricted to the proximal caput epididymal epithelium with less expression in the testis and no expression in the 24 other tissues examined. In this report, studies were carried out to examine CRES gene expression in the testis as well as to characterize the CRES protein in the testis and epididymis. In situ hybridization experiments revealed that within the testis CRES gene expression is stage-specific during spermatogenesis and is exclusively expressed by the round spermatids of Stages VII-VIII and the early elongating spermatids of Stages IX and X. Immunohistochemical studies demonstrated that CRES protein was transiently expressed in both the testis and epididymis. Within the testis the protein was localized to the elongating spermatids, whereas within the epididymis CRES protein was exclusively synthesized by the proximal caput epithelium and then secreted into the lumen. Surprisingly, the secreted CRES protein had completely disappeared from the epididymal lumen by the distal caput epididymidis. Western blot analysis of testicular and epididymal proteins showed that the CRES antibody specifically recognized a predominant 19 kDa CRES protein and a less abundant 14 kDa form. These observations suggest that the CRES protein performs a specialized role during sperm development and maturation.
Mol Reprod Dev 1995 May
PMID:Transient appearance of CRES protein during spermatogenesis and caput epididymal sperm maturation. 761 4

In view of the inconclusive data concerning the role of androgen-binding protein (ABP) in male reproductive physiology, we thought it would be pertinent to make several transgenic mouse lines overexpressing the rat ABP gene to unravel its role in Sertoli cell and epididymal homeostasis. Heterozygote transgenic mouse lines carrying the 5.5 kb ABP rat genomic DNA were produced by pronuclear microinjection. Northern blot analysis showed overexpression of rat ABP (rABP) mRNA in the testis of transgenic mice compared to rat testis control. rABP was appropriately expressed in Sertoli cells as demonstrated by in situ hybridization analysis. Sertoli cell number is increased in the seminiferous tubules of mice overexpressing rABP compared to non-transgenic littermates and scattered Sertoli cells present vacuolated-like cytoplasms, PAS and osmium negative. Compared to the wild type, the transgenic mice exhibited reduced fertility and focal damage in seminiferous epithelium characterized by morphological features compatible with programmed cell death.
J Steroid Biochem Mol Biol 1995 Jun
PMID:Androgen binding protein is tissue-specifically expressed and biologically active in transgenic mice. 762 12


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