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Biomedical subjects

T Shibata

Publications and source records attributed to T Shibata.

At least 1,063 records · Page 59Linked to original sources
PubMed1982

[Proximal ligation of the vertebral artery for treatment of vertebral aneurysms].

Vertebral aneurysms are not necessarily rare. In general neck clipping of vertebral aneurysms is the surest method for treatment of aneurysms, but as for vertebral aneurysms, it is often difficult to clip the neck without danger, because they cross over lower cranial nerves and are often fusiform. The indication of proximal ligation of the vertebral artery for treatment of vertebral aneurysms has not yet established. This procedure in 28 cases in the literature and our 3 cases treated successfully was discussed and following results were obtained. 1) Proximal ligation of the vertebral artery was useful for prevention of a rupture of vertebral aneurysms. 2) Intracranial ligation of the vertebral artery was better than the ligation in the cervical region. 3) It was necessary for the diameter of the contralateral vertebral artery to be, at least, approximately same. 4) In order the diameter of the vertebral artery to enlarge to 1.2 times as wide as that of a preoperative state, and the blood flow in the basilar artery to be enough, it was necessary for the contralateral vertebral artery not to be sclerotic.

Adult↗
PubMed1981

Escherichia coli recA protein protects single-stranded DNA or gapped duplex DNA from degradation by RecBC DNase.

RecA- mutants of Escherichia coli extensively degrade their DNA following UV irradiation. Most of this degradation is due to the recBC DNase, which suggests that the recA gene is involved in the control of recBC DNase in vivo. We have shown that purified recA protein inhibits the endonuclease and exonuclease activities of recBC DNase on single-stranded DNA. The extent of inhibition is dependent on the relative concentration of recA protein, recBC DNase, and the DNA substrate; inhibition is greatest when the concentrations of DNA and recBC DNase are low and the concentrations of recA protein is high. At fixed concentrations of recA protein and recBC DNase, inhibition is eliminated at high concentrations of DNA. In the presence of adenosine 5'-O-(3-thiotriphosphate), an ATP analog which stabilizes the binding of recA protein to both single- and double-stranded DNA, recA protein is a more potent inhibitor of the nuclease activities on single-stranded DNA and is a weak inhibitor of the exonuclease activity on double-stranded DNA. Inhibition of the latter is enhanced by oligodeoxynucleotides, which stimulate the binding of recA protein to double-stranded DNA. In the presence of adenosine 5'-O-(3-thiotriphosphate), recA protein also inhibits the action of exonuclease I on single-stranded DNA and of lambda exonuclease on double-stranded DNA. These observations are most consistent with the idea that recA protein protects DNA from recBC DNase by binding to DNA. RecA protein also blocks the endonucleolytic cleavage of gapped circular DNA by recBC DNase. Since both recA protein and recBC DNase have the ability under certain conditions to unwind duplex DNA and to displace strands, we looked for evidence that their combined action would enlarge gaps but found no extensive enlargement. D-loops, a putative intermediate in genetic recombination, are effectively protected against the action of recBC DNase by the E. coli single strand binding protein and by recA protein in the presence of adenosine 5'-O-(3-thiotriphosphate).

Bacterial Proteins↗
PubMed1981

Homologous pairing in genetic recombination. Purification and characterization of Escherichia coli recA protein.

RecA protein, which is essential for genetic recombination in Escherichia coli, was extensively purified from a strain of E. coli which contained the recA gene cloned in a plasmid (Sancar, A., and Rupp, W. D. (1979) Proc. Natl. Acad. Sci. U. S. A. 76, 3144-3148). Using the DNA-dependent ATPase activity of recA protein as an assay, we obtained about 60 mg of purified recA protein from 100 g of cells. Ten micrograms or 1 microgram of the purified protein exhibited only one detectable band with Mr approximately = 40,000 upon sodium dodecyl sulfate-acrylamide gel electrophoresis. More than 99% of the ATPase activity of purified recA protein was dependent on single-stranded DNA. Purified recA protein had no detectable DNase, topoisomerase, or ligase activities. The enzyme was stable for a least a year when stored at 0-4 degrees C. The half-life of the ATPase activity of 25 microM recA protein was 37 min at 51 degrees C. Purified recA protein binds to single-stranded and double-stranded DNA, unwinds duplex DNA by a mechanism that is stimulated by single-stranded DNA or oligonucleotides, and pairs homologous single strands with duplex DNA.

Adenosine Triphosphatases↗
PubMed1981

Homologous pairing in genetic recombination. The pairing reaction catalyzed by Escherichia coli recA protein.

Purified recA protein, which is essential for genetic recombination of Escherichia coli, catalyzed ATP-dependent homologous pairing of double-stranded DNA and single-stranded fragments to form D-loops. When the double-stranded DNA was nicked circular DNA (form II) or linear DNA (form III), the reaction proceeded nearly linearly during 30 min of incubation at 37 degrees C. When the double-stranded DNA was superhelical (form I), anomalous kinetics was observed. This anomaly was suppressed by the addition of spermidine without affecting the final yield of D-loops. The formation of D-loops required stoichiometric amounts of recA protein, which were proportional to the concentration of single-stranded DNA but which were not affected by the concentration of double-stranded DNA. With form II or III DNA as the recipient for the formation of D-loops, the rate of the reaction was greatest when there was one monomer of recA protein/2-3 nucleotide residues of single-stranded DNA; larger amounts of single-stranded DNA inhibited the reaction. The formation of D-loops was half inhibited by 30 mM NaCl and by 0.6 mM ADP, one of the products of the reaction. The thermal stability of D-loops made by recA protein was the same as that of D-loops made by annealing. In addition to pairing linear single strands with duplex DNA, recA protein made joint molecules from single-stranded circular DNA and homologous form II or III DNA. According to these and previous observations (Cunningham, R. P., DasGupta, C., Shibata, T., and Radding, C. M. (1980) Cell 20, 223-235), rcA protein will stably pair two molecules of DNA if one of them is single-stranded or partially single-stranded and if either molecule has a free end.

Bacterial Proteins↗
PubMed1981

Chromosomal loci of genes controlling site-specific restriction endonucleases of Bacillus subtilis.

We constructed transformation of B. subtilis 168 which acquired genes for site-specific restriction endonucleases. These endonucleases originated from various strains of B. subtilis and were classified into five groups based on the specificity of the sequences recognized by the enzymes. We examined the loci of genes for site-specific restriction endonucleases belonging to different groups: hsrE determined Endo. R. Bsu1231 (I), hsrB Endo.R.Bsu1247(I), hsrR Endo.R.BsuR and hsrC Endo.R.Bsu-1247(II). One gene, hsrE, was located between sacA and purA by transduction crosses with phage PBS1, and another gene, hsrB, between hsrE and purA. Genes hsrR and hsrC had been suggested to be allelic or closely linked by previous studies with transformation. We located hsrR and hsrC between purB and tre. Our previous observation and this study show that B. subtilis 168 has at least three independent loci on the chromosome for four genes for site-specific restriction endonucleases in addition to the locus for the original restriction activity (Bsu168-specific restriction) of strain 168.

Bacillus subtilis↗
PubMed1981

Homologous pairing and topological linkage of DNA molecules by combined action of E. coli RecA protein and topoisomerase I.

E. coli RecA protein and topoisomerase I, acting on superhelical DNA and circular single strands in the presence of ATP and Mg2+, topologically link single-stranded molecules to one another, and single-stranded molecules to duplex DNA. When superhelical DNA is relaxed by prior incubation with topoisomerase, it is a poor substrate for catenation. Extensive homology stimulates the catenation of circular single-stranded DNA and superhelical DNA, whereas little reaction occurs between these forms of the closely related DNAs of phages phi X174 and G4, indicating that, in conjunction with topoisomerase I, RecA protein can discriminate perfect or nearly perfect homology from a high degree of relatedness. Circular single-stranded G4 DNA reacts with superhelical DNA of chimeric phage, M13G ori 1, to form catenanes, at least half of which survive heating at 80 degrees C following restriction cleavage in the M13 region, but few of which survive following restriction cleavage in the G4 region. Electron microscopic examination of catenated molecules cleaved in the M13 region reveals that in most cases the single-stranded G4 DNA is joined to the linear duplex M13(G4) DNA in the homologous G4 region. The junction frequently has the appearance of a D loop, with an extent equivalent to 100 or more bp. We conclude that a significant fraction of catenanes were hemicatenanes, in which the single-stranded circle was topologically linked, probably by multiple turns, to its complementary strand in the duplex DNA. These observations support the previous conclusion that RecA protein can pair a single strand with its complementary strand in duplex DNA in a side-by-side fashion without a free end in any of the three strands.

Adenosine Triphosphate↗
PubMed1981

Excitation-contraction coupling in mammalian cardiac muscle during Ba2+-induced contracture.

The membrane potential and tension were recorded during contracture of mammalian ventricular muscles bathed in Tyrode solution with Ba2+ in the place of Ca2+. Strength of contracture increased with increasing Ba2+ concentration from 0.1 to 4 mM and reached a plateau above 4 mM. The membrane potential was depolarized to about -35 mV with 0.1 mM Ba2+ and to -20 mV with 5 mM Ba2+. When 0.5 mM Mn2+ was added to Ba2+-Tyrode solution, in which the muscle had been in a state of steady contracture, the muscle immediately started to relax to the resting level. In contrast, addition of 2 micrograms/ml epinephrine to Ba2+-Tyrode solution increased the strength of the contracture. Neither epinephrine nor Mn2+ caused any noticeable changes of the depolarized membrane potential. The results suggest that Ba2+ not only activates the contractile system but also depolarizes the membrane potential independently of activating the contractile system. These two remarkable actions of Ba2+ seem to be responsible for the long-lasting contracture.

Action Potentials↗