[Jaundice caused by hepatic cell damage].
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Adult↗
Biomedical subjects
S Iida
Publications and source records attributed to S Iida.
[Surgical treatment of coronary artery fistulas].
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Adult↗
[Surgical management of atrial tachycardia].
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Adolescent↗
Aplysia myoglobins with an unusual amino acid sequence.
The complete amino acid sequence of the myoglobin from Aplysia juliana, a species distributed world-wide, has been determined and compared with the sequence of the myoglobin of Aplysia limacina, a Mediterranean species, and of Aplysia kurodai, a Japanese and Asian species. Unlike mammalian myoglobins, Aplysia myoglobins contain only a single histidine residue, lacking the distal one, the homology being 76% between A. juliana and A. limacina, 74% between A. juliana and A. kurodai, and 83% between A. limacina and A. kurodai. The hydropathy profiles of the Aplysia myoglobins are very similar, but completely different from that of sperm whale myoglobin, taken as the reference.
Amino Acid Sequence↗
Conformational change of sodium- and potassium-dependent adenosine triphosphatase. Conformational evidence for the Post-Albers mechanism in Na+- and K+-dependent hydrolysis of ATP.
The addition of ATP with K+ to pig kidney Na+,K+-ATPase (EC 3.6.1.3) modified with a sulfhydryl fluorescent reagent N-[p-(2-benzimidazolyl)phenyl]maleimide induced a transient decrease (t 1/2 = 0.01 s) in the fluorescence in the presence of Mg2+ with 0.64 M Na+, followed by a slow increase (t 1/2 = 0.08 s), to give a higher steady level than that observed without K+. The addition induced a transient increase (t 1/2 less than 0.02 s) in the amount of phosphoenzyme, followed by a slow decrease (t 1/2 = 0.08 s), but the addition without K+ induced a monophasic increase (t 1/2 = 0.02 s). The addition of ATP in the presence of 2 M Na+ with Ca2+ induced a monophasic decrease (t 1/2 = 0.1 s) in the fluorescence along with a much slower increase (t 1/2 = 1.2 s) in the amount of phosphoenzyme. No significant burst of acid-labile phosphate was observed. The data showed clearly the accumulation of the enzyme-ATP complex preceding the phosphoenzyme formation. Fluorescence intensity of these enzyme species and the amount of phosphoenzyme permitted the simulation using the reaction mechanism including enzyme-ATP complex, ADP-sensitive phosphoenzyme, K+-sensitive phosphoenzyme, and K+-bound enzyme. The simulation gave a good fit to the experimental data which showed that ATP is hydrolyzed in sequence through the above intermediates in the presence of both Na+ and K+.
Animals↗
Bacteriophage P1 carries two related sets of genes determining its host range in the invertible C segment of its genome.
The bacteriophage P1 genome carries an invertible C segment consisting of 3-kb unique sequences flanked by 0.6-kb inverted repeats. Host range mutations of P1 have been mapped in the C segment region. P1 derivatives carrying insertions and deletions in the left half of the C segment in one of two orientations termed C(+) do not affect the plaque-forming ability on Escherichia coli K12 and E coli C, whereas those having insertions in the right half of the C segment fail to form plaques on these hosts. An E. coli C mutant which allows the latter insertion mutants with the C segment in the C(-) configuration to form plaques has been isolated. Not only P1 C(-) but also P1 C(+) phages gave plaques on this E. coli C mutant. The results are consistent with the notion that the C segment of P1 carries two sets of genes for host specificity, and that C inversion alters the P1 host range through activation of one set of the genes. Furthermore, extended host range mutants can be isolated by point mutation in either set of the P1 genes. C inversion is a slow process, but it occurs on the phage genome upon its vegetative growth as well as on the prophage in the lysogenic state. The 3-kb invertible G segment of the phage Mu genome is known to be homologous with the central 3-kb part of the C segment of P1 and to carry also two sets of genes for Mu host specificity. While only Mu G(-) grows on E. coli C, both Mu G(+) and Mu G(-) phages form plaques on the E. coli C mutant sensitive to P1 C(-). In the discussion the gene organization of the P1 C segment is compared with that of the Mu G segment.
Coliphages↗
Ethanol metabolism in vivo by the microsomal ethanol-oxidizing system in deermice lacking alcohol dehydrogenase (ADH).
To assess the importance of non-ADH ethanol metabolism, ADH-negative and ADH-positive deermice were fed liquid diets containing ethanol or isocaloric carbohydrate for 2-4 weeks. Blood ethanol disappearance rate increased significantly after chronic ethanol feeding in both strains. Although at low ethanol concentrations (between 5 and 10 mM) there was no significant difference between ethanol-fed and pair-fed control animals, at high ethanol concentrations (between 40 and 70 mM) blood ethanol elimination rates were increased significantly after chronic ethanol feeding in both ADH-positive and ADH-negative animals. There was no significant effect of the catalase inhibitor 3-amino-1,2,4-triazole on the ethanol elimination/rates in both strains. Whereas catalase and ADH activities were not altered after chronic ethanol treatment, the activity of the microsomal ethanol-oxidizing system (MEOS) was enhanced three to four times in both strains, and microsomal cytochrome P-450 content was also increased significantly. When MEOS activity was expressed per cytochrome P-450 content, it was higher in ADH-negative than in ADH-positive animals, and it increased after ethanol administration. When microsomal proteins were separated by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, ethanol-fed animals had a distinct band which reflected the increase in microsomal cytochrome P-450 content and seemed to reflect a unique form of cytochrome P-450 induced by ethanol. Thus, despite the absence of the ADH pathway, a large amount of ethanol was metabolized by MEOS in ADH-negative deermice; this was associated with increased blood ethanol elimination rates, enhanced MEOS activity, and quantitative and qualitative changes of cytochrome P-450.
Alcohol Dehydrogenase↗
Characterization of three highly purified cytochromes P-450 from hepatic microsomes of adult male rats.
Three hepatic microsomal cytochromes P-450 (P-450f, P-450g, and P-450h) have been purified to electrophoretic homogeneity from both untreated and ethanol-treated adult male rats. By all criteria examined, the hemoproteins isolated from untreated rats are indistinguishable from the corresponding enzymes purified from rats administered ethanol. Highly purified cytochromes P-450f, P-450g and P-450h are characterized by minimum Mr of 51,000, 50,000, and 51,000, respectively, and unique coordinates in two-dimensional isoelectric focusing-sodium dodecyl sulfate-polyacrylamide gels. The CO-reduced spectral maxima of cytochromes P-450f and P-450g are at 447-448 nm, and the peak of cytochrome P-450h is at 451 nm. Cytochrome P-450h is a versatile catalyst exhibiting high activity toward benzphetamine, hexobarbital, and estradiol-17 beta and moderate activity toward benzo[alpha]pyrene and zoxazolamine. In contrast, cytochromes P-450f and P-450g have low metabolic activity for these substrates. The three hemoproteins catalyze the metabolism of testosterone with different regio- and stereospecificities and overall rates. Both cytochromes P-450f and P-450h catalyze the hydroxylation of testosterone at the 16 alpha-position; however, cytochrome P-450h also oxidizes the steroid at the 2 alpha- and 17 beta-position (androstenedione formation). Testosterone is oxidatively metabolized at the 6 beta-, 15 alpha- and an unknown position by cytochrome P-450g. Peptide maps, generated by proteolytic or chemical digestion of the hemoproteins, indicate that cytochromes P-450f, P-450g, and P-450h differ structurally from each other and five previously characterized rat hepatic microsomal cytochromes P-450 (P-450a, P-450b, P-450c, P-450d, and P-450e). Cytochromes P-450f, P-450g, and P-450h do not react with antibodies directed against these inducible hemoproteins by Ouchterlony immunodiffusion in the presence of detergent; however, in the absence of detergent, cytochrome P-450f cross-reacts weakly with anti-P-450b. Results of this study indicate that rat hepatic microsomal cytochromes P-450 are composed of at least four hemoproteins with CO-reduced absorbance maxima between 447-448 nm. Furthermore, a minimum of four microsomal cytochromes P-450 are now known to 16 alpha-hydroxylate testosterone.
Animals↗
Hepatic resection in 125 patients.
Hepatic resection was performed in 125 patients. Ninety-three of the 125 patients had malignant neoplasms; primary liver carcinoma in 61, metastatic liver carcinoma in 15, carcinoma of the bifurcation of the hepatic ducts in 16, and carcinoma of the gallbladder in one. Performance of hepatic resection was complicated by the presence of liver cirrhosis and jaundice in 42 and 19 patients, respectively. Nine of the 125 patients died within 30 days of the operations, with an operative mortality of 7.2%. Eight of the nine deaths were due to liver failure in the cirrhotic patients who underwent resection of more than two segments of the liver. None of the jaundiced patients died postoperatively. The three-year actuarial survival rates of the patients with hepatocellular carcinoma, metastatic liver carcinoma, and carcinoma of the bifurcation of the hepatic ducts were 31%, 56%, and 21% respectively.
Adolescent↗
Hemopoietic sites and development of eosinophil granulocytes in the loach, Misgurnus anguillicaudatus.
Unique eosinophils, each of which contained only one eosinophilic granule, have been found in the peripheral blood of the loach (Misgurnus anguillicaudatus). Several loach organs have been studied by light and electron microscopy to determine the hemopoietic site of this cell type. Eosinophils are produced mainly in the spleen and to a small extent in the kidney, but not in other organs. Presumed myeloblasts are identified as large lymphoid cells containing a number of small-dense granules (diameter, 0.12-0.16 micron) in the cytoplasm. These granules have been observed throughout eosinophilopoiesis but they are most abundant in the promyelocyte stage. The largest cells have been identified as myelocytes which contain a number of large granules (diameter, 0.7-1.4 micron) with electron-dense crystalline cores. These large granules are present from the myelocyte to metamyelocyte stage. Metamyelocytes differ from myelocytes in having more large granules. Mature eosinophils are morphologically similar to metamyelocytes but are characterized by the presence of only one very large electron-dense granule (diameter, 2.5-2.8 microns) with a crystalline core. The nature of these granules has been studied by enzyme digestion using pepsin and trypsin. The results indicate that the crystalline cores are almost pure protein.
Animals↗
Functional characterization of the prokaryotic mobile genetic element IS26.
IS26L and IS26R are the 820 bp long elements found as direct repeats at both ends of the kanamycin resistance transposon Tn2680. They can mediate cointegration in E. coli K12 which contains no IS26 in its chromosome. Cointegration occurs in rec+ or recA- strains with similar frequency. Upon cointegration mediated by either IS26R or IS26L, the element is duplicated and integrated into one of many different sites. Both IS26L and IS26R carry 14 bp perfect terminal inverted repeats and generate 8 bp direct repeats at their target sequences. Deletion formation mediated by IS26R was also observed. These functional and structural features of IS26 are characteristic of a prokaryotic mobile genetic element.
Base Sequence↗
IS30, a new insertion sequence of Escherichia coli K12.
Three independent spontaneous mutations of prophage P1 affecting the ability of the phage to reproduce vegetatively are due to the insertion of a mobile genetic element, called IS30. The same sequence is also carried in the R plasmid NR 1-Basel, but not in the parental plasmid NR 1. Southern hybridisation study indicates that the Escherichia coli K 12 chromosome carries several copies of IS30 as a normal resident. IS30 is 1.2 kb long and contains unique restriction cleavage sites for BglII, ClaI, HindIII, NciI and HincII, and it is cleaved twice by the enzymes HpaII and TaqI. The ends of IS30 are formed by 26 bp long inverted repeats with 3 bases mismatched. Upon transposition IS30 generates a duplication of only 2 bp of the target. The following observations suggest a pronounced specificity in target selection by IS30. In transposition to the phage P1 genome a single integration site was used three times independently, and in both orientations. A short region of sequence homology has been identified between the P1 and NR 1-Basel insertion sites. IS30 has mediated cointegration as well as deletion. The entire IS30 sequences were duplicated in the cointegrates between a pBR322 derivative containing IS30 and the genome of phage P1-15, and several loci on the P1-15 genome served as fusion sites, some of which were used more than once.
DNA Restriction Enzymes↗
NH2-terminal sequence analyses of four rat hepatic microsomal cytochromes P-450.
Cytochromes P-450f, P-450g, P-450h, and P-450i are four hepatic microsomal hemoproteins that have been purified from adult rats. Whereas cytochromes P-450g and P-450h appear to be male-specific hemoproteins, cytochrome P-450i is apparently a female-specific enzyme purified from untreated adult female rats. Cytochrome P-450f has been purified from adult male and female rats with equivalent recoveries. Amino-terminal sequence analyses of the first 15-20 amino acid residues of each of these cytochromes P-450 has been accomplished in the current investigation. Each protein possesses a hydrophobic leader sequence consisting of 65-87% hydrophobic amino acids, and only one charged amino acid (Asp) in the amino-terminal region. Although differences in the amino-terminal sequences of cytochromes P-450f, P-450g, P-450h, and P-450i are identified, these hemoproteins all begin with Met-Asp, and marked structural homology is observed among certain of these enzymes. Cytochromes P-450g and P-450h, two male-specific proteins, have 11-12/15 identical residues with cytochrome P-450i, a female-specific isozyme. Cytochromes P-450f and P-450h have 16/20 identical amino-terminal residues. Only limited sequence homology is observed between the amino-terminal sequences of cytochromes P-450f-i compared to rat liver cytochromes P-450a-e. The results demonstrate that cytochromes P-450f, P-450g, P-450h, and P-450i are isozymic to each other and five additional rat hepatic microsomal cytochrome P-450 isozymes (P-450a-e).
Amino Acid Sequence↗
Retinoic acid metabolism by a system reconstituted with cytochrome P-450.
Feeding rats with a diet containing a hundred times the normal amount of vitamin A resulted, within 2 to 3 weeks, in an increase in total hepatic microsomal cytochrome P-450 content. This was associated, in isolated microsomes, with an enhanced conversion of all-trans-retinoic acid to polar metabolites, including a two- to threefold increased production of 4-hydroxy- and 4-oxo-retinoic acid, whether expressed per microsomal protein or per cytochrome P-450. Unlike effects of other inducers (e.g., phenobarbital or methylcholanthrene), activities of benzphetamine, aminopyrine, and ethylmorphine demethylases or benzopyrene hydroxylase were not increased. Furthermore, the CO-reduced difference spectral peak was shifted towards 449 nm. On sodium dodecyl sulfate-gel electrophoresis, one band was increased with electrophoretic mobility identical to that of cytochrome P-450f, a recently isolated new form which has a CO-reduced difference spectral peak at 448 nm. In a system reconstituted with NADPH-cytochrome P-450 reductase, NADPH, and phospholipid, purified cytochromes P-450f and b were discovered to promote conversion of retinoic acid to polar metabolites, including 4-hydroxy-retinoic acid.
Animals↗
Ultrastructure of the effects of calcitonin on the development of mouse tooth germs in vitro.
Mandibular first molars, from 17-day-old embryos, were cultivated in control medium or medium containing 0.1, 0.01 or 0.001 unit/ml of calcitonin (CT) for periods up to 10 days. In untreated tooth germs, cells of the dental papilla differentiated into pre-odontoblasts up to 4 days and predentine was seen on day 6. Cells treated with 0.1 unit/ml of CT differentiated into pre-odontoblasts up to 4 days, but no predentine was formed even after 10 days in culture. With 0.01 unit/ml, cells differentiated into odontoblasts, and had already secreted predentine a few days earlier than the untreated group. With 0.001 unit/ml, the developing germs were similar to the control explants during the entire 10-day cultivation period. The proportional area of rough endoplasmic reticulum to cytoplasm of the odontoblasts was low at 0.1 unit/ml of CT and high at 0.01 unit/ml compared to the untreated explants.
Animals↗
The bacteriophage P1 site-specific recombinase cin: recombination events and DNA recognition sequences.
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Base Sequence↗
Partial characterization of ACTH-potentiating factors derived from porcine thymus.
We have demonstrated the presence of ACTH-potentiating factors in porcine thymus which contained neither biologically active nor radioimmunoassayable ACTH. The factors were acidic and heat stable in nature, and were present in heterogeneous forms having various molecular weight. Purification of the factors with small molecular weights was performed using reversed-phase high-performance liquid chromatography following gel filtration and cation-exchange chromatography. A purified factor exerted dose-dependent ACTH-potentiating activity. Loss of the ACTH-potentiating activity of purified factors by treatment with carboxypeptidase Y indicated their peptidic nature. ACTH-potentiating activity was readily observable after preincubating the adrenal cells with the thymic extract. The enhancement of ACTH-induced steroidogenesis by the factors was observed in the presence of bacitracin at a concentration to prevent ACTH degradation. Therefore, the existence of potentiating mechanisms other than inhibition of ACTH proteolysis was indicated.
Adrenal Cortex Hormones↗
Presence of adrenocorticotropin-potentiating factors in porcine thyroid glands.
An extract of porcine thyroid gland in 0.1 N acetic acid exerted dose-dependent potentiation of ACTH-induced corticosterone production in isolated rat adrenal cells. The extract by itself manifested no steroidogenic activity. Upon gel-filtration of the extract, potentiating activities were demonstrated in three main peaks with molecular weights of about 10,000, 5,000 and 2,000. These findings indicate the presence of heterogeneous forms of ACTH-potentiating factors in the thyroid. Significant enhancement of ACTH-induced steroidogenesis was readily apparent with three gel-filtration fractions at a lower concentration of ACTH (4.75 pM). At this concentration, dose-dependent potentiation was observed with these three fractions. Enhanced corticosterone production responses by cells preincubated with the thyroid extract were observed and the results indicated the existence of potentiating mechanisms other than inhibition of ACTH proteolysis. The lack of T4, T3 and thyroglobulin in this activity suggests that the activity resides in other constituents of the thyroid.
Adrenal Glands↗