[Production and cytotoxicity of peroxidized phospholipids].
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Animals↗
Biomedical subjects
T Miyazawa
Publications and source records attributed to T Miyazawa.
[Experimental evaluation of iotrolan as an arthrographic contrast medium--knee arthrography with iotrolan in rabbits].
Authors evaluated the efficacy and tolerability of iotrolan, a nonionic dimeric contrast medium used for myelography, as an arthrographic contrast medium in comparison with meglumine/sodium diatrizoate and iopamidol in rabbit. Iotrolan (Isovist, 300 mgI/ml) was injected in one knee joint and diatrizoate (Urografin, 292 mgI/ml) or iopamidol (Iopamiron, 300 mgI/ml) in the other at a dose of 1.5 ml/knee. Knee arthrograms were taken 2, 5, 10, 20, 30, 45 and 60 min after injection. Contrast density was determined by measuring the transmission density in the supra-patellar bursa with an image analysis system. The anterior displacement of the patellar from the femur was measured as an indicator of hydrarthrosis. Contrast duration in the supra-patellar bursa was longer with iotrolan than with diatrizoate and iopamidol. Hydrarthrosis was less pronounced with iotrolan than with diatrizoate and iopamidol. These results suggest that iotrolan has the advantage over existing contrast media for arthrography with respect to the efficacy and tolerability.
Animals↗
Nuclear-magnetic-resonance studies of human epidermal growth factor.
The 1H-NMR spectra of native human epidermal growth factor (EGF) and a derivative lacking the final five residues have been assigned by two-dimensional methods, enabling their structures to be compared. The same structural features are observed for each protein, although the final five residues of native human EGF interact with residues earlier in the sequence. Comparison of the resonance shifts of human, rat and mouse EGF and human transforming growth factor alpha (TGF alpha) enables shifts characteristic of the EGF conformation to be identified, providing standards by which the structures of related proteins may be assessed.
Amino Acid Sequence↗
Co-expression of N-ras p21 and C-erbB-2 (neu) oncogene products by common ALL antigen-positive aggressive diffuse lymphoma.
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Aged↗
Cerebral oxygen utilization analyzed by the use of oxygen-17 and its nuclear magnetic resonance.
In order to assess the usefulness of oxygen-17, a stable isotope of oxygen, oxygen-17, was administered to rats for studying cerebral oxygen utilization, and the produced metabolic water was detected by 17O-NMR spectroscopy in vitro and an 1H-NMR imaging system in vivo. In the vitro study, the increment in signal amplitude of oxygen-17 was observed in the brain extracted from rats that inhaled oxygen-17 gas. The in vivo study demonstrated that there were changes in the 1H-NMR image intensity of brain of rats that inhaled oxygen-17 gas. These facts indicate that oxygen-17 can serve as a tracer in the study of cerebral oxygen utilization.
Animals↗
Nonprotein amino acid furanomycin, unlike isoleucine in chemical structure, is charged to isoleucine tRNA by isoleucyl-tRNA synthetase and incorporated into protein.
Nonprotein amino acid furanomycin was found to bind with Escherichia coli isoleucyl-tRNA synthetase (IleRS) almost as tightly as the substrate L-isoleucine. The conformation of furanomycin bound to the enzyme was determined by NMR analyses including the transferred nuclear Overhauser effect method. The conformation of IleRS-bound furanomycin was similar to that of L-isoleucine, although the chemical structure of furanomycin is unlike that of L-isoleucine. By E. coli IleRS, E. coli tRNAIle was charged with furanomycin as efficiently as with L-isoleucine. Furthermore, furanomycyl-tRNAIle was bound to polypeptide chain elongation factor Tu as tightly as isoleucyl-tRNAIle. Furanomycin was found to be incorporated into beta-lactamase precursor by in vitro protein biosynthesis. A newly designed amino acid will probably be incorporated into proteins, provided that the new amino acid takes a similar conformation as a protein-constituting amino acid in the active site of an aminoacyl-tRNA synthetase.
Amino Acids↗
Conformational changes of aminoacyl-tRNA and uncharged tRNA upon complex formation with polypeptide chain elongation factor Tu.
The conformation change of Thermus thermophilus tRNA(1Ile) upon complex formation with T. thermophilus elongation factor Tu (EF-Tu) was studied by analysis of the circular dichroism (CD) bands at 315 nm (due to the 2-thioribothymidine residue in the T-loop) and at 295 nm (due to the core structure of tRNA). Formation of the ternary complex of isoleucyl-tRNA(1Ile) and EF-Tu.GTP increased the intensities of these CD bands, indicating stabilization of the association between the T-loop and the D-loop and also a significant conformation change of the core region. Upon complex formation of EF-Tu.GTP and uncharged tRNA, however, the conformation of the core region is not changed, while the association of the two loops is still stabilized. On the other hand, the binding with EF-Tu.GDP does not appreciably affect the conformation of isoleucyl-tRNA or uncharged tRNA. These indicate the importance of the gamma-phosphate group of GTP and the aminoacyl group in the formation of the active complex of aminoacyl-tRNA and EF-Tu.GTP.
Circular Dichroism↗
Transferred nuclear Overhauser effect analyses of membrane-bound enkephalin analogues by 1H nuclear magnetic resonance: correlation between activities and membrane-bound conformations.
Leu-enkephalin, [D-Ala2]Leu-enkephalin, and [D-Ala2]Leu-enkephalinamide (agonists) and [L-Ala2]Leu-enkephalin (inactive analogue) bind to lipid bilayer consisting of phosphatidylcholine and phosphatidylserine. The conformations that these compounds assume, once bound to perdeuterated phospholipid bilayer, have been shown to be unique, as shown by the transferred nuclear Overhauser effect (TRNOE) of 1H NMR spectroscopy. In addition, their location in the bilayer was analyzed by TRNOE in the presence of spin-labeled phospholipids. These analyses showed a clear relationship between the activity and the peptide-membrane interaction. The three active peptides, when bound to membranes, adopt the same conformation, characterized by a type II' beta-turn around Gly3-Phe4 and a gamma-turn around Gly2 (or D-Ala2). The inactive analogue, [L-Ala2]Leu-enkephalin, displayed a completely different TRNOE pattern corresponding to a different conformation in the membrane-bound state. The tyrosine residue of the active compounds is not inserted into the interior of membrane, but it is inserted into the bilayer for the L-Ala2 analogue. According to these results, [L-Ala2]Leu-enkephalin may be explained to be inactive because the mode of binding to the membranes is different from that of active compounds.
Enkephalin, Leucine↗
Complex formation of peptide antibiotic Ro09-0198 with lysophosphatidylethanolamine: 1H NMR analyses in dimethyl sulfoxide solution.
Ro09-0198 is a peptide antibiotic and immunopotentiator produced by Streptoverticillium griseoverticillatum which exhibits antitumor and antimicrobial activities. The chemical structure has been determined [Kessler et al. (1988) Helv. Chim. Acta 71, 1924-1929; Wakamiya et al. (1988) Tetrahedron Lett. 37, 4771-4772]. This peptide specifically interacts with (lyso)phosphatidylethanolamine, causing hemolysis and enhancing permeability in phosphatidylethanolamine-containing vesicles [Choung et al. (1988) Biochim. Biophys. Acta 940, 171-179, 180-187]. The highly specific nature of the interaction was studied by two dimensional proton NMR analyses. Proton resonances of the peptide were observed in dimethyl sulfoxide solution in the presence of 1-dodecanoyl-sn-glycerophosphoethanolamine. By comparison to the chemical shifts in the absence of lysophosphatidylethanolamine and by analysis of intermolecular cross-peaks in NOESY spectra, amino acid residues involved in the binding with the phospholipid were identified. The ammonium group of the phospholipid interacts with the carboxylate group of beta-hydroxyaspartic acid-15 but not with that of the carboxylate terminus. The secondary ammonium group of lysinoalanine-19/6 is probably bound to the phosphate group of the lipid. The peptide does not interact strongly with the fatty acid chain of the lipid. A folded structure of the central part [from Phe7 to Ala(S)14] of the peptide opens on binding with the phospholipid and accommodates the glycerophosphoethanolamine head group.
Amino Acid Sequence↗
Determination of lipid hydroperoxides in low density lipoprotein from human plasma using high performance liquid chromatography with chemiluminescence detection.
A high performance liquid chromatographic system with chemiluminescence detection (HPLC-CL) was used for determining phospholipid hydroperoxides in human plasma low density lipoprotein (LDL). This system involved separation of phospholipids from LDL-total lipids with normal phase silica gel HPLC and post-column detection of hydroperoxide-dependent chemiluminescence produced by luminol oxidation during the reaction of hydroperoxide with cytochrome c-haeme. By using HPLC-CL, we could detect phosphatidylcholine hydroperoxide (PCOOH) in human plasma LDL, and the LDL-PCOOH concentration was significantly higher in patients with atherosclerosis and hyperlipidemia than that of healthy volunteers. The LDL-PCOOH level was proportional to the plasma total cholesterol concentration.
Adolescent↗
Quantification of feline immunodeficiency virus in a newly established feline T-lymphoblastoid cell line (MYA-1 cells).
A quantitative method for analysis of feline immunodeficiency virus (FIV) was established by the indirect immunofluorescence (IF) test using MYA-1 cells infected with the serially diluted viruses. When we compared this method with the reverse transcriptase (RT) activity assay, the quantitative analysis by the indirect IF test was more sensitive than that by RT activity assay. The relationship between TCID50 measured by the indirect IF test and RT activity was linear. However, the RT activity assay was not suitable for measurement of low amounts of FIV in the supernatants of FIV-infected cultures.
Animals↗
Liver phosphatidylcholine hydroperoxidation provoked by ethionine-containing choline-deficient diet in mice.
It is shown that peroxidation of phosphatidylcholine (PC) is enhanced in liver of mice fed a hepatocarcinogenic choline-deficient diet containing 0.1% w/w ethionine. Mice were divided into 4 groups and fed for 4 weeks one of the following diets: choline-supplemented; choline-supplemented containing ethionine; choline-deficient; and choline-deficient containing ethionine. Phosphatidylcholine hydroperoxide (PCOOH) of liver lipids was measured by high performance liquid chromatography using a chemiluminescence detector. Mice fed a choline-deficient diet containing ethionine showed 6-fold higher PCOOH levels than the choline-supplemented control mice: the PCOOH/PC molar ratios of liver lipids were 32.3 X 10(-5) and 5.6 X 10(-5), respectively. In addition to this remarkable degree of lipid peroxidation in liver of mice fed the choline-deficient diet containing ethionine, we also observed a significant liver fatty infiltration, a decrease in plasma and liver alpha-tocopherol, and an increase in liver injury-indicative enzyme activities. Also, marker enzymes for hepatocarcinogenesis, glucose-6-phosphatase and gamma-glutamyl transpeptidase were affected. These data suggest that enhanced hydroperoxidation of phosphatidylcholine may participate in hepatocarcinogenesis provoked by choline deficiency in the presence of ethionine.
Animals↗
Phospholipid hydroperoxide accumulation in liver of rats intoxicated with carbon tetrachloride and its inhibition by dietary alpha-tocopherol.
The formation and accumulation of phospholipid hydroperoxides, especially of phosphatidylcholine hydroperoxide (PCOOH), a primary peroxidation product of phosphatidylcholine (PC), in livers of carbon tetrachloride-intoxicated rats was investigated. PCOOH in liver and blood plasma was measured by a chemiluminescence-high-performance liquid chromatography procedure originally developed by Miyazawa et al. (Anal. Lett. 20, 915, 1987; Free Radical Biol. Med. 7, 209, 1989). Male Sprague-Dawley rats (120 g body wt., 5 weeks of age) were used in the experiments. The amount of PCOOH in the liver of control rats (CCl4-untreated) was 160 +/- 20 pmol/100 mg protein (mean +/- SD) and the PCOOH/PC molar ratio was 1.1 +/- 0.1 X 10(-5). In CCl4 (0.1 ml/100 g body wt.)-dosed rats, the liver PCOOH was 289 +/- 65 pmol/100 mg protein (PCOOH/PC = 2.4 +/- 0.4 X 10(-5], 764 +/- 271 pmol/100 mg protein (PCOOH/PC = 5.2 +/- 1.7 X 10(-5], and 856 +/- 165 pmol/100 mg protien (PCOOH/PC = 6.0 +/- 0.8 X 10(-5] at 6 h, 24 h, and 1 week after the dose, respectively. Under such conditions, the liver phosphatidylethanolamine hydroperoxide (PEOOH) level was not altered and the concentration was less than 100 pmol/100 mg protein even after the dose. The increments of liver PCOOH were suppressed 56% by the oral supplementation of DL-alpha-tocopherol (5 mg/100 g body wt./day) for a week before CCl4 administration. A relatively larger amount of PEOOH was found after stimulation of PC hydroperoxidation in the liver of rats with a large amount of CCl4 (0.25 ml/100 g body wt.) rather than with the small amount of CCl4 (0.1 ml/100 g body wt.).(ABSTRACT TRUNCATED AT 250 WORDS)
Animals↗
Effect of water-soluble contrast medium on the lung in rats. Comparison of iotrolan, iopamidol, and diatrizoate.
Aspiration is a serious complication of oral contrast media (CM). The authors investigated the effects of iotrolan, iopamidol, and diatrizoate in rats' lungs. To quantify the lung damage induced by CM, pulmonary water and hemoglobin contents were determined. Arterial blood-gas exchange (pH, PCO2, and PO2) also was determined as an indicator of respiratory function. Iotrolan, iopamidol, or sodium/meglumine diatrizoate with a concentration of 300 mg I/mL was administered intrabronchially at a dose of 1 mL/kg. Physiologic saline was administered to the control group. Ten minutes after administration, arterial blood was collected and the lung was removed. Diatrizoate and iopamidol increased pulmonary water and hemoglobin contents and decreased blood PO2. The effect of iotrolan on these parameters was slight and no significant differences were observed between the iotrolan and saline groups. These results suggest that iotrolan is a preferable CM for gastrointestinal examination in the case of suspected aspiration.
Animals↗
[Tissue distribution of red blood cells treated with X-ray contrast media in rats].
Tissue distribution of red blood cells (RBC) that were treated with X-ray contrast media was investigated in rats. The contrast medium mixed with an equivolume of 51Cr-labelled RBC was administered to the internal carotid artery in a dose of 200 microliters/rat; and the radioactivity in the brain, lung and spleen were determined. The contrast medium mixed with an equivolume of blood was administered to the right atrium in a dose of 4 ml/kg, and the hemoglobin content in the lung and changes in pulmonary and circulatory functions were determined. In the ionic contrast medium (meglumine diatrizoate)-treated group, the radioactivity in the brain remained 30 to 50 times higher compared with the nonionic contrast medium (iopamidol)- and saline-treated group until 15 min after infusion. The radioactivity in the spleen increased and the radioactivity and hemoglobin content in the lung decreased time-dependently in the diatrizoate-treated group, whereas iopamidol- and saline-treated groups exhibited constantly low values during the experimental period. Changes in the airway pressure, pulmonary arterial pressure, systemic blood pressure and heart rate were similar after intra-atrial administration of diatrizoate mixed with blood and diatrizoate mixed with saline. These results suggest that the ionic contrast medium affects the RBC and causes a microcirculatory disturbance in the brain.
Animals↗
Continuous production of feline immunodeficiency virus in a feline T-lymphoblastoid cell line (MYA-1 cells).
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Animals↗
Existence of feline immunodeficiency virus infection in Japanese cat population since 1968.
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Animals↗
Recognition of tRNA identity determinants by aminoacyl-tRNA synthetases.
By analyzing aminoacylation activities of variants of isoleucine tRNAs and glutamic acid tRNA from Escherichia coli, it was found that the anticodons are the major determinants for "identities" of these tRNAs. It was also shown that the post-transcriptional modifications are essential to aminoacylation of these tRNAs. Interactions between the tRNAs and the aminoacyl-tRNA synthetases were analyzed by NMR spectroscopy.
Amino Acyl-tRNA Synthetases↗