Enzyme induction in rat liver: The effects of Be2+in vivo

1981 ◽  
Vol 1 (3) ◽  
pp. 217-222 ◽  
Author(s):  
Margery G. Ord ◽  
Lloyd A. Stocken
Keyword(s):  
Protein Kinase ◽  
Rat Liver ◽  
Enzyme Induction ◽  
Orotic Acid ◽  
Tyrosine Aminotransferase ◽  
Cytoplasmic Protein ◽  
Ribonucleoprotein Particles ◽  
Liver Nuclei

Rats given an LD50 dose of Be2+ showed reduced activities of ornithine decarboxytase and tyrosine aminotransferase in liver in response to dexamethasone induction. Control fed animals showed ‘superinduction’. Be2+ also inhibited the uptake of [3H]orotic acid into rapidly labelled RNA of ribonucleoprotein particles extracted from liver nuclei in isomolar solutions at pH 8.0. Consistent with inhibition of cytoplasmic protein kinase reported previously (Kaser et at., 1980), the uptake of [32P]Pi into proteins in the ribonucleoprotein particles was also diminished.

scholarly journals ISOLATION OF TWO DISTINCT CLASSES OF POLYSOMES FROM A NUCLEAR FRACTION OF RAT LIVER

1968 ◽  
Vol 37 (1) ◽  
pp. 163-181 ◽  
Author(s):  
Paul D. Sadowski ◽  
Janet Alcock Howden
Keyword(s):  
Outer Membrane ◽  
Rat Liver ◽  
Orotic Acid ◽  
Specific Activity ◽  
Nuclear Fraction ◽  
Differential Centrifugation ◽  
Rat Liver Nuclei ◽  
Liver Nuclei ◽  
Triton X

Isolated rat liver nuclei were washed with Triton-X-100 in the presence of liver cell sap. This treatment liberated a fraction of polysomes which were isolated by differential centrifugation and were designated "outer membrane polysomes." The outer membrane polysomes synthesized protein in vivo. Shortly after injection of orotic acid-14C, the RNA of outer membrane polysomes had a higher specific activity than that of cytoplasmic polysomes. It was postulated that outer membrane polysomes may be an intermediate in the transfer of newly synthesized RNA from the nucleus to the cytoplasm. In other experiments, Triton-washed rat liver nuclei were lysed in the presence of deoxycholate and deoxyribonuclease. A ribonucleoprotein fraction was isolated from the lysate by differential centrifugation. This fraction contained "intranuclear ribosomes," which sedimented like partially degraded polysomes in sucrose gradients. This degradation could be partially prevented if intranuclear ribosomes were purified by sedimentation through heavy sucrose. The resulting pellets were termed "intranuclear polysomes" because they contained some undergraded polysomes. Intranuclear polysomes were highly radioactive after a brief pulse with orotic acid-14C, but did not appear to synthesize protein rapidly in vivo. Intranuclear polysomes may represent the initial stage of assembly of polyribosomes in the nucleus.

scholarly journals No correlation between binding of glucocorticosteroids to specific cytoplasmic proteins in vivo and enzyme induction in the rat liver

1983 ◽  
Vol 212 (2) ◽  
pp. 305-312 ◽  
Author(s):  
H Grote ◽  
J Voigt ◽  
C E Sekeris
Keyword(s):  
Rna Polymerase ◽  
Rat Liver ◽  
Enzyme Induction ◽  
Protein Complexes ◽  
Dose Dependence ◽  
Tyrosine Aminotransferase ◽  
Biologically Active ◽  
Cytoplasmic Proteins ◽  
Stimulation Of

Time- and dose-dependence of the formation of the different cytoplasmic hormone-protein complexes were studied in the rat liver after administration in vivo of [3H]cortisol or [3H]dexamethasone and compared with the stimulation of RNA polymerase B and induction of tyrosine aminotransferase and tryptophan oxygenase. No correlation could be found between formation in vivo of any of the five cytoplasmic hormone-protein complexes found and stimulation of RNA polymerase B activity or enzyme induction. After administration of [3H]cortisol, different metabolites of cortisol could be demonstrated in the isolated hormone-protein complexes. No time- or dose-dependence of the metabolite patterns could be observed after application of hormone doses that were in the range of the biologically active doses. After administration of [3H]dexamethasone, the same hormone-protein complexes were observed, which contained, however, the injected steroid instead of metabolites. These results seem to indicate that the cytoplasmic binding components present in the rat liver are enzymes involved in the metabolism of the glucocorticosteroids and that dexamethasone binds to these enzymes as a substrate analogue.

scholarly journals The effects of salicylate on the activity of rat liver tyrosine–2-oxoglutarate aminotransferase in vitro and in vivo

1972 ◽  
Vol 126 (2) ◽  
pp. 347-350 ◽  
Author(s):  
A. A.-B. Badawy
Keyword(s):  
Rat Liver ◽  
Pyridoxal Phosphate ◽  
Actinomycin D ◽  
Sodium Salicylate ◽  
Intraperitoneal Administration ◽  
Tyrosine Aminotransferase ◽  
Major Effect ◽  
Endogenous Activity

1. Salicylate, in concentrations of 0.25mm and above, enhances the basal activity of tyrosine–2-oxoglutarate aminotransferase in homogenates of rat liver incubated in the absence of added pyridoxal 5′-phosphate (endogenous activity). The effect is decreased by increasing the concentration of the cofactor. 2. The intraperitoneal administration of sodium salicylate enhances the activity of rat liver tyrosine aminotransferase; the major effect during the first hour being on the enzyme in the absence of added pyridoxal phosphate. Actinomycin D prevents the induction of the enzyme by cortisol and tryptophan. Induction by pyridoxine or salicylate is 50% inhibited by actinomycin D. The effects of the injections of various combinations of cortisol, pyridoxine and salicylate were also studied in the absence or presence of actinomycin D. 3. It is suggested that salicylate induces rat liver tyrosine aminotransferase by displacing its protein-bound cofactor and that a cofactor-type induction of the hepatic enzyme occurs in pyridoxine-treated rats.

scholarly journals Inactivation of tyrosine aminotransferase in neutral homogenates and rat liver slices

1972 ◽  
Vol 129 (5) ◽  
pp. 1131-1138 ◽  
Author(s):  
F. Auricchio ◽  
L. Mollica ◽  
A. Liguori
Keyword(s):  
Amino Acid ◽  
Rat Liver ◽  
Acid Concentration ◽  
Tyrosine Aminotransferase ◽  
Amino Acid Concentration ◽  
Acidic Ph ◽  
Ph Values ◽  
Neutral Ph ◽  
Liver Slices

Inactivation of tyrosine aminotransferase induced in vivo by triamcinolone was studied in a homogenate incubated at neutral pH values. The integrity and the presence of subcellular particles together with a compartment of acidic pH are necessary for inactivation of tyrosine aminotransferase. It is suggested that tyrosine aminotransferase is inactivated inside lysosomes. The system responsible for inactivation of tyrosine aminotransferase was partially purified and identified with lysosomal cathepsins B and B1. Inactivation of tyrosine aminotransferase in liver slices is controlled by the amino acid concentration and strongly stimulated by cysteine. 3,3′,5-Tri-iodo-l-thyronine reversibly and strongly decreases the rate of inactivation of tyrosine aminotransferase. The effect is not due to an increased rate of tyrosine aminotransferase synthesis.

scholarly journals cAMP-dependent protein kinase phosphorylates and activates nuclear Ca2+-ATPase

1998 ◽  
Vol 95 (16) ◽  
pp. 9178-9183 ◽  
Author(s):  
Patrick J. Rogue ◽  
Jean-Paul Humbert ◽  
Alphonse Meyer ◽  
Solange Freyermuth ◽  
Marie-Marthe Krady ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Nuclear Envelope ◽  
Rat Liver ◽  
Protein Band ◽  
Partial Purification ◽  
Dependent Protein Kinase ◽  
Rat Liver Nuclei ◽  
Camp Dependent Protein Kinase ◽  
Dependent Protein ◽  
Liver Nuclei

A Ca2+-pump ATPase, similar to that in the endoplasmic reticulum, has been located on the outer membrane of rat liver nuclei. The effect of cAMP-dependent protein kinase (PKA) on nuclear Ca2+-ATPase (NCA) was studied by using purified rat liver nuclei. Treatment of isolated nuclei with the catalytic unit of PKA resulted in the phosphorylation of a 105-kDa band that was recognized by antibodies specific for sarcoplasmic reticulum Ca2+-ATPase type 2b. Partial purification and immunoblotting confirmed that the 105-kDa protein band phosphorylated by PKA is NCA. The stoichiometry of phosphorylation was 0.76 mol of phosphate incorporated/mol of partially purified enzyme. Measurement of ATP-dependent 45Ca2+ uptake into purified nuclei showed that PKA phosphorylation enhanced the Ca2+-pumping activity of NCA. We show that PKA phosphorylation of Ca2+-ATPase enhances the transport of 10-kDa fluorescent-labeled dextrans across the nuclear envelope. The findings reported in this paper are consistent with the notion that the crosstalk between the cAMP/PKA- and Ca2+-dependent signaling pathways identified at the cytoplasmic level extends to the nucleus. Furthermore, these data support a function for crosstalk in the regulation of calcium-dependent transport across the nuclear envelope.

scholarly journals Determination of the amount of small messenger ribonucleic acid-containing particles free in liver cytoplasm

1975 ◽  
Vol 152 (1) ◽  
pp. 51-56 ◽  
Author(s):  
B M Mullock ◽  
R H Hinton
Keyword(s):  
Rat Liver ◽  
Ribonucleic Acid ◽  
Messenger Ribonucleic Acid ◽  
Ribonucleoprotein Particles

To assess the contribution made by mRNA-containing particles to the heterogeneity previously observed among rat liver 40S ribonucleoprotein particles, the amount of poly(A)-containing RNA in subribosomal particles was determined. RNA was labelled with orotate in vivo for 24h and then for 50min. Poly(A)-containing RNA was trapped on filters impregnated with poly(U). Very little poly(A)-containing RNA was found in conventionally prepared ribonucleoprotein particles after fractionation in sucrose. However, after preparation of ribonucleoprotein particles by sedimentation through 1 M-sucrose in the presence of 0.15M-KCl or by precipitation with Mg2+ as described by Leitin & Lerman [(1969) Biokhimiya 34, 839-849], amounts of poly(A)-containing RNA were similar to amounts of mRNA found by other workers in total ribonucleoprotein particles. Even in such preparations, less than 5% of the total rapidly labelled RNA in native subribosomal-particle fractions was mRNA. It seems that mRNA-containing particles make up only a very small part of the population of subribosomal particles in liver.

scholarly journals Studies on the pathogenesis of liver necrosis by α-amanitin. Effect of α-amanitin on ribonucleic acid synthesis and on ribonucleic acid polymerase in mouse liver nuclei

1967 ◽  
Vol 105 (2) ◽  
pp. 779-782 ◽  
Author(s):  
F. Stirpe ◽  
L. Fiume
Keyword(s):  
Rna Polymerase ◽  
Ammonium Sulphate ◽  
Ribonucleic Acid ◽  
Mouse Liver ◽  
Orotic Acid ◽  
Acid Synthesis ◽  
Liver Necrosis ◽  
Liver Nuclei

1. Injection of α-amanitin to mice causes a decreased incorporation of [6−14C]-orotic acid into liver RNA in vivo. 2. The activity of RNA polymerase activated by Mn2+ and ammonium sulphate is greatly impaired in liver nuclei isolated from mice poisoned with α-amanitin, and is inhibited by the addition of the same toxin in vitro. 3. The activity of the Mg2+-activated RNA polymerase is only slightly affected by α-amanitin either administered to mice or added in vitro.

Modulation of Rat Liver Protein Kinase C during in Vivo CC14-Induced Oxidative Stress

1993 ◽  
Vol 194 (2) ◽  
pp. 635-641 ◽  
Author(s):  
M.A. Pronzato ◽  
C. Domenicotti ◽  
E. Rosso ◽  
A. Bellocchio ◽  
M. Patrone ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Rat Liver ◽  
Liver Protein ◽  
Kinase C
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