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)

The hormonal regulation of thyroglobulin synthesis has been studied using two independent clones of the OVNIS 6H cell line. Insulin, hydrocortisone and TSH were able to stimulate thyroglobulin synthesis, whereas transferrin, somatostatin and glycyl-histidyl-lysine were without effect. Insulin stimulated thyroglobulin synthesis without affecting cAMP production. Hydrocortisone, when combined with insulin was a stimulator too; this stimulation was not accompanied by an increase in cAMP. TSH alone was unable to stimulate either cAMP or thyroglobulin synthesis. The stimulatory effect of TSH on thyroglobulin synthesis took place only when combined with insulin or insulin plus hydrocortisone, and was mediated by cAMP. Consequently, insulin and hydrocortisone stimulated thyroglobulin synthesis by cAMP-independent mechanisms, whereas TSH acted via the cAMP system. Forskolin mimicked TSH effects on cAMP and thyroglobulin synthesis. Calf serum inhibited cAMP and thyroglobulin production. Optimal cAMP and thyroglobulin synthesis as well as TSH responsiveness were obtained in serum-free medium supplemented with 5 micrograms/ml insulin, 100 nM hydrocortisone and 1 mU/ml TSH.
Mol Cell Endocrinol 1987 Jul
PMID:cAMP dependent and independent regulation of thyroglobulin synthesis by two clones of the OVNIS 6H thyroid cell line. 304 Apr 95

The expression of Tc resistance gene derived from plasmid pBR322 has been studied in Bacillus subtilis cells where this alien gene is not usually expressed. Fragments of Bacillus subtilis chromosome were inserted into the Tc resistance gene promoter region of the hybrid plasmid pGG20 and the expression of this gene was registered. Plasmid pGG20 confers a constitutive mode of Tc resistance in Escherichia coli cells. In contrast, the inducibility of Tc resistance gene expression in Bacillus subtilis cells has been reported. Optimal concentration for the highest inducibility of Tc resistance by the antibiotic has been determined.
Mol Gen Mikrobiol Virusol 1986 May
PMID:[Characteristics of expression of the tetracycline resistance gene from the plasmid pBR322 in Bacillus subtilis cells]. 309 84

Factors affecting the efficiency of transfection of Ps. aeruginosa PAO1 cells by the temperate SM bacteriophage DNA have been determined. The efficiency of transfection by DNA preparations isolated from the wild type bacteriophage SMc+ or its thermoinducible mutant SM cts6 is practically the same. The frequency of transfection is (7-9) X 10(4) of infectious centers per mkg of transfecting DNA. Variability in the frequencies of transfection has been registered depending of the infection conditions or on the transfer of the Ps. aeruginosa PAO1 recipient strain population into the competence phase. The efficiency of transfection is increased by the addition of Ca2+ or Mg2+ ions affecting the adsorption and absorbtion of phage DNA by the recipient cells. Optimal concentrations of the bivalent metal ions are 0.15M CaCl2 and 0.2M MgCl2. The results obtained have been used for optimizing the conditions of Ps. aeruginosa PAO1 transfection by SM bacteriophage DNA.
Mol Gen Mikrobiol Virusol 1987 Jan
PMID:[Transfecting activity of Pseudomonas aeruginosa bacteriophage SM]. 310 74

The purpose of these studies was to ascertain the extent to which endogenous inhibin regulates follicle-stimulating hormone (FSH) secretion at different intervals during development in the male and female rat. This was determined by examining the changes in plasma FSH that resulted from immunoneutralizing endogenous inhibin in male and female rats at different ages during development and into adulthood. Passive immunoneutralization of endogenous inhibin was achieved using specific, high titer ovine antiserum, generated against the alpha-subunit of the recently described inhibin molecule. Optimal antiserum volumes and time after injection required to observe maximal changes in FSH secretion were determined in initial experiments. No clear effect of immunoneutralizing endogenous inhibin could be demonstrated on FSH secretion in female rats until 20 days of age, after the completion of the endogenous rise in FSH which occurs between days 5 and 20. Thereafter, injection of the anti-alpha-inhibin serum (anti-alpha IN) produced a progressively marked increase in plasma FSH as the age of the females increased. In male rats, injection of the anti-alpha IN serum caused an increase in FSH secretion as early as 5 days of age, although the response was more delayed at this age than at later times. The ability of the anti-alpha IN serum to increase plasma FSH was observed through 20 days of age. At 30 days of age, during the peak of the endogenous rise in plasma FSH, injection of the anti-alpha IN serum failed to further increase the already elevated levels of plasma FSH. As the endogenously high levels of FSH gradually decreased, the ability of anti-alpha IN serum to increase FSH secretion returned (40 days of age) but was diminished by 50 days of age and was completely lost by 60 days of age. The results of the present study indicate that inhibin plays an increasingly important role as a regulator of FSH secretion in the female from at least 20 days of age into adulthood. In the male, however, the role of inhibin in regulating FSH secretion, which is clearly present during early postnatal development, is apparently lost at the time of puberty.
Mol Cell Endocrinol 1988 Aug
PMID:Passive immunoneutralization of endogenous inhibin: sex-related differences in the role of inhibin during development. 314 31

ADP ribosylation of membranes by pertussis toxin (PT) and cholera toxin (CT) was studied as a function of addition of ATP, various guanine nucleotides, Mg2+, and inorganic phosphate (Pi). ADP ribosylation of a 40 kilodalton (kDa) band by PT is markedly enhanced by ATP and GTP and is strongly inhibited by Pi or Mg2+. GTP analogs (GTP gamma S and GMP-adenyl-5'-yl imidodiphosphate) were less effective. In contrast, ADP ribosylation of two substrates for CT (of 42 and 50 kDa) is stimulated by Pi, Mg2+, and GTP or GTP analogs such as GTP gamma S, but is unaffected by ATP. These stimulatory conditions correlate well with GTP-mediated activation of stimulated nucleotide-binding regulatory component of adenyl cyclase. Optimal conditions for ADP ribosylation by PT do not correlate simply with conditions thought to lead to stabilization of an inactive form of inhibitory nucleotide-binding regulatory component of adenyl cyclase (Gi) or Gi-like protein; rather, the data suggest the involvement of both a stimulatory nucleotide site on PT (positively affected by either ATP or GTP) and a stabilizing site on the PT substrate (affected by GDP, GDP beta S, or GTP). Treatment of membranes with Lubrol PX increased ADP ribosylation by PT by as much as 25- to 30-fold, but inhibited the action of CT. Using defined conditions for ADP ribosylation by PT and CT, distinct labeling patterns were observed in thyroid, brain, corpus luteum, liver, heart, and erythrocytes membranes. All membranes were more intensely labeled by PT rather than CT.
Mol Endocrinol 1987 Jul
PMID:Adenosine diphosphate ribosylation of G proteins by pertussis and cholera toxin in isolated membranes. Different requirements for and effects of guanine nucleotides and Mg2+. 315 63

Rat liver microsomal fraction was treated with several non-ionic, anionic or zwitterionic detergents in order to investigate which is most suitable for subsequent purification of the iodothyronine deiodinase. Criteria for effective solubilization were (a) no or little inhibitory effect of the detergent on deiodinase activity, (b) non-sedimentable activity by centrifugation at 105,000 X g, and (c) a low molecular weight of the soluble complex as determined by Sephacryl S-300 gel filtration in the presence of detergent. Optimal solubilization was obtained by treatment of the microsomes with cholate and subsequent precipitation of dispersed protein with 30% ammonium sulfate, resulting in the removal of adhering phospholipids. Enzyme was resolubilized best with the non-ionic detergents Brij 56 or Emulgen 911 in the presence of 0.5 M NaCl. This deiodinase preparation had an isoelectric point at pH 9.3 and was further purified by subsequent chromatography on DEAE-Sephacel and CM-Sepharose. Only the Emulgen 911-dispersed enzyme was retained by the CM-Sepharose column. Further purification was investigated by chromatofocusing. This resulted in a rapid inactivation of the Emulgen 911 preparation whereas the Brij 56-soluble enzyme was ultimately purified 400 times after DEAE-Sephacel and chromatofocusing.
Mol Cell Endocrinol 1988 Feb
PMID:Partial purification of the microsomal rat liver iodothyronine deiodinase. I. Solubilization and ion-exchange chromatography. 335 2

Synthetic nonsteroidal antiestrogens are bound intracellularly by two high affinity saturable bindings sites, the estrogen receptor and the microsomal antiestrogen-binding site (AEBS). In order to further define the structural requirements for ligand binding to AEBS from rat liver and the MCF 7 human breast cancer cell line, the relative binding affinities of an extensive series of structurally related ligands were investigated using competitive binding assay techniques. The groups of compounds studied were: analogues of the triphenylethylene antiestrogens, Cl 628 and tamoxifen; analogues of cyclofenil; bibenzyl and stilbene derivatives; analogues of the cytochrome P-450 inhibitor SKF-525A; phenothiazine derivatives; and a series of structurally related compounds with a variety of pharmacological activities. High affinity binding to AEBS required the presence of both a hydrophilic basic aminoether side chain and a hydrophobic aromatic ring structure (di- or tricyclic for maximal affinity). Structural modifications to either influenced binding affinity. Aromatic substitution either raised (CF3) or lowered (OH, OCH3) affinity, apparently by electronic effects transmitted through the benzene nucleus. Side chain structure was the major determinant of binding affinity, but its influence was complex and dependent upon terminal amino group structure, side chain branching and substitution, and tissue source of AEBS. Optimal binding affinity was shown by side chains bearing basic heterocyclic amino terminal groups. Other cellular sites that are known to bind antiestrogens with relatively high affinity include calmodulin, cytochrome P-450, and histamine, dopamine, and muscarinic receptors. Binding studies using a variety of pharmacologically active and radiolabeled ligands selective for these sites, including those for dopamine D1 and D2 receptors ([3H]fluphenazine, [3H]flupenthixol, [3H]spiperone, and [3H]SCH 23390) and histamine H1 receptors ([3H]pyrilamine), demonstrated that several of these compounds interact with AEBS with high affinity. However, the ligand specificity and other binding properties of the AEBS as determined by competitive binding studies and Scatchard analysis show this site to be a molecular entity truly distinct from these other cellular binding sites.
Mol Pharmacol 1987 May
PMID:Studies on the ligand specificity and potential identity of microsomal antiestrogen-binding sites. 355 93

We have developed a system using explanted embryonic chicken lens epithelia to express foreign recombinant genes containing crystallin DNA regulatory sequences introduced by calcium phosphate transfection. Optimal results were obtained with lens epithelia from 14-day embryos transfected 1 day after explantation and assayed 3 days later. When DNA sequences (-364 to +45) of the murine alpha A-crystallin gene were inserted in the pSVO-CAT expression vector of Gorman et al. [Gorman, C. M., Moffat, L. F. & Howard, B. H. (1982) Mol. Cell. Biol. 2, 1044-1051] in the same orientation as in the crystallin gene, they promoted chloramphenicol acetyltransferase (CAT; EC 2.3.1.28) activity in the transfected epithelia. Sequences 87 to 364 base pairs upstream from the murine gene cap site were required for CAT gene expression. These crystallin gene regulatory sequences did not promote CAT expression in primary cultures of embryonic chicken fibroblasts or other nonlens cells. By contrast, the long terminal repeat of Rous sarcoma virus and the early promoter of simian virus 40 promoted CAT activity in lens and nonlens cells. Our experiments thus demonstrate that the explanted embryonic chicken lens epithelium is an advantageous recipient for identifying lens-cell-specific regulatory sequences of crystallin genes and implicate a DNA region upstream of the "TATA box" for regulation of the murine alpha A-crystallin gene. These experiments also suggest that explanted epithelia from other tissues may be useful for studying the expression of foreign genes.
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PMID:Lens-specific expression of the chloramphenicol acetyltransferase gene promoted by 5' flanking sequences of the murine alpha A-crystallin gene in explanted chicken lens epithelia. 385 84

We have demonstrated that in certain conditions 50S subunits can transfer peptide moiety from peptidyl-tRNA to puromycin in the absence of alcohol. Monovalent cations NH4+ and K+ support this reaction, while Na+ and Li+ are ineffective. Optimal concentration for NH4+ is 1.8 M. Mg2+ ion concentrations above 12 mM are needed as well as an elevated temperature (30 degrees C). Using the alcohol-free puromycin reaction of 50S subunits we show that alcohol activates the peptidyl transferase center, but does not participate in the puromycin reaction. Neither does it change the protein composition of subunits.
Mol Biol (Mosk)
PMID:[Stimulation of peptidyltransferase activity of 50S subunits by alcohols]. 389 29

GTP cyclohydrolase (EC 3.5.4.16), the first enzyme in the pteridine pathway leading to the de novo formation of folic acid, has been identified and isolated from the human malaria parasite, Plasmodium falciparum. The enzyme was purified 200-fold by high performance size-exclusion chromatography on a TSK-G-3000 SW protein column. The molecular weight was estimated at 300 000. Optimal enzyme activity was observed at pH 8.0 and 42 degrees C. The Km for GTP was 54.6 microM. Products of the enzyme reaction were identified as the carbon-8 of GTP and D-erythro-dihydroneopterin triphosphate. ATP was a competitive inhibitor (Ki = 600 microM) of the enzyme. Activity of the enzyme was Mg2+-independent, whereas Mn2+, Cu2+ and Hg2+ (5 mM) were inhibitory. GTP cyclohydrolase activity was also identified in a murine parasite, Plasmodium berghei, and a simian parasite, Plasmodium knowlesi. Activity of the enzyme in P. knowlesi, an intrinsically synchronous quotidian parasite, was found to be dependent on the stage of parasite development.
Mol Biochem Parasitol 1985 Dec
PMID:Guanosine triphosphate cyclohydrolase in Plasmodium falciparum and other Plasmodium species. 390 34


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