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)

We studied the binding of dihydrotestosterone-receptor complexes (DHT-R) from human genital skin fibroblasts to oligodeoxyribonucleotides and DNA. Following incubation of fibroblasts with 2 nM [3H]DHT (45 min, 37 degrees C), DHT-R were prepared as total fibroblast sonicates (sonication of cells in 0.5 M KCl), intact fibroblast cytosol (100000 X g supernatant) or intact fibroblast nuclear extract (sonication of nuclei in 0.5 M KCl). DHT-R were also prepared by incubation of fractionated fibroblast cytosol with 4 nM [3H]DHT (4 h, 0 degrees C). Optimal conditions were established for binding of DHT-R from total fibroblast sonicates to oligo-dT cellulose: 60 min, 0 degrees C, low salt (0.05-0.10 M KCl), linearity with DHT-R concentration, and nucleotide saturation. With total fibroblast sonicates the rank order of DHT-R binding was oligo-dT approximately equal to -dG greater than DNA greater than -dC greater than or equal to -dA approximately equal to -dI. Intact fibroblast cytosol displayed a similar preference of DHT-R binding to oligo-dT and -dG but the binding was quantitatively higher than for total fibroblast sonicates, the binding for fractionated fibroblast cytosolic DHT-R formed at 0 degrees C being quantitatively lower. However, binding of DHT-R from cytosol (0 degrees C) to DNA-cellulose was equal to that for DHT-R from cytosol (37 degrees C). Binding of DHT-R from intact fibroblast nuclear extracts was lower than for total fibroblast sonicates. Preparations from cells of patients with receptor-negative, complete androgen insensitivity lacked both DHT-R formation and specific oligonucleotide binding. Binding of oligonucleotides to DHT-R from cells of patients with receptor-positive, complete androgen insensitivity could not be distinguished from that of normal cells. These results suggest: (a) androgen receptor-steroid complexes recognize and bind to certain preferred deoxyribonucleotides; (b) various factors affect the quantitative binding of DHT-R from different cellular preparations to deoxyribonucleotides; and (c) neither qualitative nor quantitative abnormalities for DHT-R of complete androgen-insensitive patients were detectable from oligonucleotide or DNA binding.
Mol Cell Endocrinol 1983 Oct
PMID:Human androgen insensitivity mutation does not alter oligonucleotide recognition by the androgen receptor-DHT complex. 664 73

Human peripheral blood mononuclear cells were isolated on a large scale by leukapheresis of either individual donors or pooled cell concentrates supplied by a local blood bank. Optimal conditions with respect to cell density, lectin (soluble and insoluble Concanavalin A; phytohemagglutinin) concentration and culture time were established for monocyte chemotactic factor (LMCF) production. LMCF was assayed on highly purified human monocytes/macrophages which had been kept in culture up to 4 days for optimal expression of response to LMCF. Chemotaxis assays were performed in a novel type multichamber assembly and migrated cells were enumerated by enzyme-linked immunosorbent assay. Based on the described methodology it is possible to produce litre quantities of LMCF and assay large numbers of samples both of which are prerequisites for chemical and functional characterizations of LMCF.
Mol Immunol 1983 Mar
PMID:Characterization of human lymphocyte derived chemotactic factors for mononuclear phagocytes--I. Production and detection. 686 53

Translation by RNA 4 from plant brome mosaic virus coding for the virus coat protein in an E. coli cell-free system with pure factors of translation has been studied. It has been shown that the initiation of translation by this mRNA depends completely on the three E. coli initiation factors. Optimal ionic conditions for the formation of the initiatory 70S times fMet-tRNA times RNA 4 complex have been found. It has been shown that this complex is stable in conditions of zonal centrifugation. On the basis of reaction with puromycin it has been determined that the initiatory fMet-tRNA in this complex occupies the donor-tRNA-binding site of the ribosome. By the competence of the initiatory ribosomal complex for binding with Ser-tRNA (serine is the N-terminal amino acid in the virus coat protein) it can be concluded that the ribosomal and the E. coli initiation factors recognize the initiatory codon of the RNA r from brome mosaic virus. Peptide synthesis induced by RNA 4 has been obtained on E. coli ribosomes with five pure factors of translation: IF-1, IF-2A, IF-3, EF-Tu or (Tu--Ts) and EF-G. The dependence of elongation on the Mg2+ concentration in the medium at RNA 4 translation has been determined.
Mol Biol (Mosk)
PMID:[Translation of RNA 4 from plant brome mosaic virus in an Escherichia coli cell-free system with pure protein factors in translation]. 703 66

Epithelial cell-rich fractions of rat mammary gland were prepared using percoll gradients after collagenase dispersion. Their insulin-binding characteristics were similar to those of crude acini but superior to unfractionated isolated cells. Optimal binding was obtained after 60 min at 20 degrees C or 16 h at 4 degree C at pH 7.8 Binding at 37 degrees C was lower due probably to an enhanced rate of insulin degradation. 48 h after ovariectomy of 18-day pregnant rats insulin binding to acini doubled due to an increase in the number of insulin receptors. Progesterone but not bromocriptine (which prevented the rise in serum prolactin which occurred after ovariectomy) prevented this increase in insulin binding. These results illustrate that the change in serum progesterone rather than prolactin increases insulin binding to the mammary cell at parturition whilst insulin binding decreases in adipose tissue at the same time (Flint et al., Mol. Cell Endocrinol, 20, 101-111, 1981) enabling coordinated changes in the metabolism of these 2 tissues to take place during the perinatal period.
Mol Cell Endocrinol 1982 May
PMID:Insulin binding to rat mammary gland at various stages of cell isolation and purification. 704 14

Biosynthesis of ceruloplasmin was studied in wheat germ extract programmed with polysomal RNA from rat liver. Optimal potassium concentration for the total protein-synthesizing activity and for the synthesis of immunoreactive ceruloplasmin was 96 and 186 mM respectively. 7-methylguanosine 5'-monophosphate caused two-fold inhibition of the cell-free synthesis of ceruloplasmin. Immunoprecipitated ceruloplasmin that was synthesized at optimal potassium concentration was a homogeneous polypeptide of a molecular weight about 84 kD. The addition of membrane fractions from rat liver to the incubation mixture caused the conversion of the 84 kD polypeptide into 80 kD and 65 kD polypeptides that are similar to proceruloplasmins synthesized in rat liver during in vivo pulse labelling. The suggestion is made that 84 kD polypeptide is a primary product of the translation of ceruloplasmin mRNA (preproceruloplasmin).
Mol Cell Biochem 1981 Mar 27
PMID:Preproceruloplasmin is a primary product of cell-free translation of ceruloplasmin messenger RNA. 724 25

The properties of the informosomes released from isolated nuclei of wheat embryos were studied in an in vitro system. The release of the informosomes from isolated nuclei of wheat embryos labelled with [3H]uridine is stimulated by exogeneous ATP. Optimal conditions for informosomes release from nuclei were determined. The particles obtained have heterogeneous sedimentation coefficients in sucrose gradient ranging from 10 to 60S. The particles are sensitive to low concentrations of RNase. Buoyant density in CsCl is 1.40-1.43 g/cm3. RNA extracted from particles is characterized by heterogeneous distribution in sucrose gradient between 4 and 20S. The informosomes contain two main peptides with molecular mass 36 000 and 51 000 and a number of minor peptides.
Mol Biol (Mosk)
PMID:[Release of informosomes from isolated nuclei of wheat embryos in an in vitro system]. 733 79

Nuclear retinoic acid receptors (RARs) function as ligand-activated trans-acting transcription factors and mediate the effects of retinoids on gene expression, cell growth, and differentiation. Determination of the receptors' expression in premalignant and malignant lesions may provide prognostic value and direct the selection of receptor-specific retinoids in cancer prevention or treatment. We describe a sensitive and practical in situ hybridization method for the analysis of RARs in tissue sections of fixed and embedded surgical specimens. Digoxigenin-labeled antisense and sense RNA probes were prepared for nuclear RAR-alpha, RAR-beta, and RAR-gamma. The specificity of the probes for their respective receptor mRNAs was demonstrated by Northern blot hybridization to total RNA extracted from murine and human cells. Optimal conditions for in situ localization of the RAR mRNA were established using cultured tumor cells, and these conditions were then used for the detection of RAR mRNA in formalin-fixed, paraffin-embedded sections of surgical specimens from human tumors. The hybridization stain was detected in the cytoplasm (where it was expected to be localized) and not seen in the cell nucleus. This method provides a rapid detection procedure with good resolution that allows one to clearly distinguish strongly and weakly stained cells. A comparison of receptor expression in head and neck squamous carcinoma specimens and in adjacent normal tissues revealed a significant decrease in the level of RAR-beta mRNA in the tumor cells.
Diagn Mol Pathol 1994 Jun
PMID:Detection of nuclear retinoic acid receptor mRNA in histological tissue sections using nonradioactive in situ hybridization histochemistry. 752 Mar 32

The X-ray diffraction pattern of tendon collagen can contain a number of sharp Bragg peaks indicating three-dimensional crystallinity of the sample. Optimal diffraction images have been obtained with a high flux synchrotron X-ray source and a carefully maintained sample environment and staining techniques. The Bragg peaks are always superimposed on a diffuse background. This makes interpretation of data difficult and a number of conflicting models of collagen packing have been proposed. The removal of the diffuse scatter from the images allows the Bragg peaks to be seen on a relatively flat background. This was conducted by modelling the background points as a series of two-dimensional polynomial functions. The resultant set of observed Bragg reflections serves as an excellent basis to test the validity of two contradictory packing modes; (1) the triclinic model, Fraser et al., (2) the microfibril model, Kajava. From this it can easily be seen that the model proposed by Kajava is inappropriate, since there is limited agreement between predicted positions of reflections and the positions of observable reflections on film. The packing of collagen molecules on a triclinic lattice is favoured by this criterion.
J Mol Biol 1995 Apr 28
PMID:Type I collagen packing, conformation of the triclinic unit cell. 753 30

Two kinds of proteinases, type-I and type-II, were purified or partially purified from salted muscle of anchovy, Engraulis japonica. Mol. wts. of type-I and type-II proteinases were estimated to 25,000 and 37,000, respectively, on electrophoretic analysis. Both proteinases strongly hydrolyzed synthetic tri or tetrapeptide substrates specific to trypsin, alpha-thrombin, and an activated protein C, while they hardly hydrolyzed Arg-MCA and benzoyl Arg-MCA derivatives. The proteinases were inhibited by common trypsin inhibitors. Optimal pH for the proteinase activities were pH 6.8 (type-I) and pH 7.0 to 7.5 (type-II), and the proteinases showed the highest activities at 45 degrees C (type-I) and 50 degrees C (type-II). The N-terminal amino acid sequence of type-I proteinase, 1I-2V-3G-4G ... (29 residues were identified), was significantly similar to sequences of trypsins and tryptases. Based on these findings, both proteinases were presumed to be kinds of tryptases in E. japonica muscle.
 ...
PMID:Two kinds of neutral serine proteinases in salted muscle of anchovy, Engraulis japonica. 761 98

We describe eicosanoid biosynthesis by microsomal-enriched preparations of hemocytes from larvae of the tobacco hornworm Manduca sexta. Four major prostaglandins, PGA2, PGE2, PGD2, and PGF2 alpha, and a lipoxygenase product that co-chromatographed with 15-hydroxyeicosatetraenoic acid (HETE) were synthesized under most conditions. The HETE's fraction was the predominant product. Eicosanoid biosynthesis was sensitive to experimental conditions, including incubation time, temperature, and protein concentration. Optimal biosynthesis was observed with 1.5 mg of microsomal-enriched protein, incubated at 30 degrees C for 2 min. The hemocyte preparation is sensitive to low dosages of naproxin and esculetin. As in mammals, most lipoxygenase activity (87%) was localized in the cytosolic fraction of hemocytes. Unlike mammals, in which PGH synthase is associated with intracellular membranes, the hemocytic activity was detected in microsomal (59%), cytosolic (35%) and mitochondrial fractions (5%).
Insect Biochem Mol Biol 1995 Jun
PMID:Eicosanoid biosynthesis by hemocytes from the tobacco hornworm, Manduca sexta. 762 6


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