Metabolism of α-naphthylthiourea by rat liver and rat lung microsomes

1980 ◽  
Vol 53 (1) ◽  
pp. 164-173 ◽  
Author(s):  
Philip W. Lee ◽  
Thomas Arnau ◽  
Robert A. Neal
Keyword(s):  
Rat Liver ◽  
Rat Lung

Increased expression of CTP:phosphocholine cytidylyltransferase in maturing type II cells

1994 ◽  
Vol 267 (1) ◽  
pp. L25-L32 ◽  
Author(s):  
M. Hogan ◽  
L. J. Zimmermann ◽  
J. Wang ◽  
M. Kuliszewski ◽  
J. Liu ◽  
...  
Keyword(s):  
Rat Liver ◽  
Type Ii Cells ◽  
Mrna Levels ◽  
Type Ii ◽  
Rat Lung ◽  
Protein Levels ◽  
Ctp:Phosphocholine Cytidylyltransferase ◽  
Fetal Rat ◽  
Fetal Rat Lung ◽  
Phosphatidylcholine Synthesis

We previously reported that phosphatidylcholine synthesis increased in fetal rat lung type II cells with advancing gestation. This increase was accompanied by an increase in CTP:phosphocholine cytidylyltransferase activity, which catalyses a rate regulatory step in de novo phosphatidylcholine synthesis by fetal type II cells. To determine whether this increase in cytidylyltransferase activity is due to an increase in cytidylyltransferase protein levels, the gene and protein expression of cytidylyltransferase was investigated in maturing type II cells. The cytidylyltransferase cDNA was cloned from fetal rat type II cells and showed 99% sequence homology with rat liver cDNA. The cDNA detected two mRNA transcripts (1.8 and 7.5 kb) in fetal rat lung. By reverse-transcriptase polymerase chain reaction (RT-PCR) analysis, cytidyltransferase mRNA content increased three-fold in fetal type II cells with advancing gestation, whereas cytidylyltransferase mRNA levels in fibroblasts remained constant. An antibody against rat liver cytidylyltransferase was used to assess cytidylyltransferase protein. Western blotting revealed that cytidylyltransferase protein content increased threefold in the microsomal fraction of type II cells with advancing gestation. The enzyme protein levels in the cytosolic fraction did not significantly change with development. Enzyme activity studies confirmed these latter observations. We conclude that the increase in surfactant phosphatidylcholine synthesis by type II cells at late fetal gestation is due in part to an increase in the amount of cytidylyltransferase protein.

scholarly journals Cytosolic glutathione transferases from rat liver. Primary structure of class alpha glutathione transferase 8-8 and characterization of low-abundance class Mu glutathione transferases

1989 ◽  
Vol 261 (2) ◽  
pp. 531-539 ◽  
Author(s):  
P Alin ◽  
H Jensson ◽  
E Cederlund ◽  
H Jörnvall ◽  
B Mannervik
Keyword(s):  
Rat Liver ◽  
Glutathione Transferase ◽  
Glutathione Transferases ◽  
Rat Lung ◽  
Cytosol Fraction ◽  
Methionine Residue ◽  
Isoelectric Points ◽  
Cytosolic Glutathione ◽  
Lung And Kidney

Six GSH transferases with neutral/acidic isoelectric points were purified from the cytosol fraction of rat liver. Four transferases are class Mu enzymes related to the previously characterized GSH transferases 3-3, 4-4 and 6-6, as judged by structural and enzymic properties. Two additional GSH transferases are distinguished by high specific activities with 4-hydroxyalk-2-enals, toxic products of lipid peroxidation. The most abundant of these two enzymes, GSH transferase 8-8, a class Alpha enzyme, has earlier been identified in rat lung and kidney. The amino acid sequence of subunit 8 was determined and showed a typical class Alpha GSH transferase structure including an N-acetylated N-terminal methionine residue.

scholarly journals Two immunologically distinct Yc-type subunits are present in rat lung glutathione S-transferases

1984 ◽  
Vol 224 (1) ◽  
pp. 335-338 ◽  
Author(s):  
S V Singh ◽  
Y C Awasthi
Keyword(s):  
Glutathione Peroxidase ◽  
Rat Liver ◽  
Peroxidase Activity ◽  
Gel Electrophoresis ◽  
Rat Lung ◽  
Glutathione Peroxidase Activity ◽  
Glutathione S Transferase ◽  
Two Dimensional Gel Electrophoresis ◽  
Glutathione S Transferases

Two types of 25 000-Mr subunits are present in rat lung glutathione S-transferase I (pI 8.8). These subunits, designated Yc and Yc', are immunologically and functionally distinct from each other. The homodimers YcYc (pI 10.4) and Yc'Yc' (pI 7.6) obtained by hybridization in vitro of the two subunits of glutathione S-transferase I (pI 8.8) were isolated and characterized. Results of these studies indicate that only the Yc subunits express glutathione peroxidase activity and cross-react with the antibodies raised against glutathione S-transferase B (YaYc) or rat liver. The Yc' subunits do not express glutathione peroxidase activity and do not cross-react with the antibodies raised against glutathione S-transferase B of rat liver. The amino acid compositions of these two subunits are also different. These two subunits can also be separated by the two-dimensional gel electrophoresis of glutathione S-transferase I (pI 8.8) of rat lung.

scholarly journals Rat lung glutathione S-transferases. Evidence for two distinct types of 22000-Mr subunits

1984 ◽  
Vol 221 (3) ◽  
pp. 609-615 ◽  
Author(s):  
S V Singh ◽  
C A Partridge ◽  
Y C Awasthi
Keyword(s):  
Rat Liver ◽  
The Other ◽  
Rat Lung ◽  
Glutathione S Transferase ◽  
Substrate Specificities ◽  
Liver Glutathione ◽  
Immunological Properties ◽  
Glutathione S Transferases

Two immunologically distinct types of 22000-Mr subunits are present in rat lung glutathione S-transferases. One of these subunits is probably similar to Ya subunits of rat liver glutathione S-transferases, whereas the other subunit Ya′ is immunologically distinct. Glutathione S-transferase II (pI7.2) of rat lung is a heterodimer (YaYa′) of these subunits, and glutathione S-transferase VI (pI4.8) of rat lung is a homodimer of Ya′ subunits. On hybridization in vitro of the subunits of glutathione S-transferase II of rat lung three active dimers having pI values 9.4, 7.2 and 4.8 are obtained. Immunological properties and substrate specificities indicate that the hybridized enzymes having pI7.2 and 4.8 correspond to glutathione S-transferases II and VI of rat lung respectively.

Initial Polymerization Sites Indicated During Mitochondrial Oxidation of Diaminobenzidine after Toluene Treatment

1977 ◽  
Vol 35 ◽  
pp. 408-409
Author(s):  
W. A. Shannon ◽  
M. A. Matlib
Keyword(s):  
Membrane Permeability ◽  
Cytochrome Oxidase ◽  
Rat Liver ◽  
Precise Definition ◽  
Cytochemical Localization ◽  
Oxidative Reaction ◽  
Mitochondrial Oxidation ◽  
Definition Of ◽  
Exogenous Substrates

Numerous studies have dealt with the cytochemical localization of cytochrome oxidase via cytochrome c. More recent studies have dealt with indicating initial foci of this reaction by altering incubation pH (1) or postosmication procedure (2,3). The following study is an attempt to locate such foci by altering membrane permeability. It is thought that such alterations within the limits of maintaining morphological integrity of the membranes will ease the entry of exogenous substrates resulting in a much quicker oxidation and subsequently a more precise definition of the oxidative reaction.The diaminobenzidine (DAB) method of Seligman et al. (4) was used. Minced pieces of rat liver were incubated for 1 hr following toluene treatment (5,6). Experimental variations consisted of incubating fixed or unfixed tissues treated with toluene and unfixed tissues treated with toluene and subsequently fixed.

Effects of 5-5'-Diphenyl-2-thiohydantoin (DPTH) and Thyroxine on the Ultrastructure and Chemical Composition of Rat Liver

1971 ◽  
Vol 29 ◽  
pp. 570-571
Author(s):  
E. A. Elfont ◽  
R. B. Tobin ◽  
D. G. Colton ◽  
M. A. Mehlman
Keyword(s):  
Chemical Composition ◽  
Rat Liver ◽  
Future Study ◽  
Mode Of Action ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Effective Inhibitor ◽  
Biochemical Effects ◽  
Glycerophosphate Dehydrogenase ◽  
Stimulation Of

Summary5,-5'-diphenyl-2-thiohydantoin (DPTH) is an effective inhibitor of thyroxine (T4) stimulation of α-glycerophosphate dehydrogenase in rat liver mitochondria. Because this finding indicated a possible tool for future study of the mode of action of thyroxine, the ultrastructural and biochemical effects of DPTH and/or thyroxine on rat liver mere investigated.Rats were fed either standard or DPTH (0.06%) diet for 30 days before T4 (250 ug/kg/day) was injected. Injection of T4 occurred daily for 10 days prior to sacrifice. After removal of the liver and kidneys, part of the tissue was frozen at -50°C for later biocheailcal analyses, while the rest was prefixed in buffered 3.5X glutaraldehyde (390 mOs) and post-fixed in buffered 1Z OsO4 (376 mOs). Tissues were embedded in Araldlte 502 and the sections examined in a Zeiss EM 9S.Hepatocytes from hyperthyroid rats (Fig. 2) demonstrated enlarged and more numerous mitochondria than those of controls (Fig. 1). Glycogen was almost totally absent from the cytoplasm of the T4-treated rats.

Effects of Steroids on Fetal Rat Liver

1969 ◽  
Vol 27 ◽  
pp. 350-351
Author(s):  
F. G. Zaki
Keyword(s):  
Liver Injury ◽  
Rat Liver ◽  
Fetal Liver ◽  
Dosage Level ◽  
Maternal Plasma ◽  
Methyl Prednisolone ◽  
Fetal Rat ◽  
Toxic Agents ◽  
Fetal Rat Liver ◽  
Neonatal Liver

Fetal and neonatal liver injury induced by agents circulating in maternal plasma, even though well recognized, its morphological manifestations are not yet established. As part of our studies of fetal and neonatal liver injury induced by maternal nutritional disorders, metabolic impairment and toxic agents, the effects of two anti-inflammatory steroids have been recently inves tigated.Triamcinolone and methyl prednisolone were injected each in a group of rats during pregnancy at a-dosage level of 2 mgm three times a week. Fetal liver was studied at 18 days of gestation. Litter size and weight markedly decreased than those of control rats. Stillbirths and resorption were of higher incidence in the triamcinolone group than in those given the prednisolone.

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