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Biomedical subjects

H Komiya

Publications and source records attributed to H Komiya.

At least 37 records · Page 2Linked to original sources
PubMed1990

Use of a test diet in screening for neuroblastoma reduces false-positives attributable to food intake.

We attempted to reduce false-positives during screening for neuroblastoma using a qualitative urine test by introducing a test diet without foodstuffs known to cause false-positive results. In preliminary in-vivo experiments, intake of contra-indicated foods such as orange juice or banana was shown to result in high percentages of false-positive results several hours after food intake. False-positive results were obtained even after 24 hours among breast-fed infants whose mothers received orange juice. In a controlled field trial the false-positive rate was reduced to 2.84% among 540 infants taking the test diet compared with 5.05% among 9,844 control infants following conventional guidance on contra-indicated foods (p less than 0.05). For comparison, a questionnaire survey of nationwide screening in Japan in 1987 revealed that 66% of the screening centres employed qualitative urine tests, either a Spot or Dip method. False-positive rates, including those due to inappropriate urine collection, ranged from 0.4% to 33.7% (mean 7.1%). Rates ranged from 0.2% to 18.7% (mean 3.4%) in the remaining 34% of screening centres employing a quantitative method with high performance liquid chromatography.

Breast Feeding↗
PubMed1990

[Intravenous DSA as a screening method for cerebral aneurysms].

Intravenous DSA (IVDSA) was evaluated as a screening method for cerebral aneurysms. It was performed 390 times in 372 cases. Clinically useful images were obtained in 94.1% in all examinations. Nineteen aneurysms were visualized in cerebral angiography among 21 cases with SAH or 3rd nerve palsy, whereas in IVDSA 15 aneurysms were noted. Aneurysms not visualized in IVDSA were all 4 mm or less in size. Therefore, aneurysms, more than 4 mm in size, which have higher risks for rupture, were detectable in IVDSA. Based on these findings, IVDSA is considered to be clinically useful in screening for aneurysms. In all 372 cases, 33 aneurysms were suspected in IVDSA findings, whereas in cerebral angiography 21 of them turned to be aneurysms. Such 12 false positive cases were distributed mainly at anterior communicating and middle cerebral arteries. Improvement of image resolution, avoidance of vessel overlapping and proper selection of screened cases should be investigated for further development of this screening method.

Angiography, Digital Subtraction↗
PubMed1988

Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: protein-cofactor (bacteriochlorophyll, bacteriopheophytin, and carotenoid) interactions.

The three-dimensional structures of the cofactors and protein subunits of the reaction center (RC) from the carotenoidless mutant strain of Rhodobacter sphaeroides R-26 and the wild-type strain 2.4.1 have been determined by x-ray diffraction to resolutions of 2.8 A and 3.0 A with R values of 24% and 26%, respectively. The bacteriochlorophyll dimer (D), bacteriochlorophyll monomers (B), and bacteriopheophytin monomers (phi) form two branches, A and B, that are approximately related by a twofold symmetry axis. The cofactors are located in hydrophobic environments formed by the L and M subunits. Differences in the cofactor-protein interactions between the A and B cofactors, as well as between the corresponding cofactors of Rb, sphaeroides and Rhodopseudomonas viridis [Michel, H., Epp, O. & Deisenhofer, J. (1986) EMBO J. 3, 2445-2451], are delineated. The roles of several structural features in the preferential electron transfer along the A branch are discussed. Two bound detergent molecules of beta-octyl glucoside have been located near BA and BB. The environment of the carotenoid, C, that is present in RCs from Rb. sphaeroides 2.4.1 consists largely of aromatic residues of the M subunit. A role of BB in the triplet energy transfer from D to C and the reason for the preferential ease of removal of BB from the RC is proposed.

Bacteriochlorophylls↗
PubMed1988

Structure of the reaction center from Rhodobacter sphaeroides R-26: protein-cofactor (quinones and Fe2+) interactions.

The three-dimensional structure of the reaction center (RC) from Rhodobacter sphaeroides has been determined by x-ray diffraction to a resolution of 2.8 A with an R value of 24%. The interactions of the protein with the primary quinone, QA, secondary quinone, QB, and the nonheme iron are described and compared to those of RCs from Rhodopseudomonas viridis. Structural differences between the QA and QB environments that contribute to the function of the quinones (the electron transfer from QA- to QB and the charge recombination of QA-, QB- with the primary donor) are delineated. The protein residues that may be involved in the protonation of QB are identified. A pathway for the doubly reduced QB to dissociate from the RC is proposed. The interactions between QB and the residues that have been changed in herbicide-resistant mutants are described. The environment of the nonheme iron is compared to the environments of metal ions in other proteins.

Bacterial Proteins↗
PubMed1988

Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: symmetry relations and sequence comparisons between different species.

Photosynthetic reaction centers from purple bacteria exhibit an approximate twofold symmetry axis, which relates both the cofactors and the L and M subunits. For the reaction center from Rhodobacter sphaeroides, deviations from this twofold symmetry axis have been quantitated by superposing, by a 180 degrees rotation, the cofactors of the B branch onto the A branch and the M subunit onto the L subunit. An alignment of the sequences of the L and M subunits from four purple bacteria, one green bacterium, and the D1 and D2 subunits of a photosystem II-containing green alga is presented. The residues that are conserved in all six species are shown in relation to the structure of Rb. sphaeroides and their possible role in the function of the reaction center is discussed. A method is presented for characterizing the exposure of alpha-helices to the membrane based on the periodicity of conserved residues. This method may prove useful for modeling the three-dimensional structures of membrane proteins.

Amino Acid Sequence↗
PubMed1988

[Three cases of involuntary movements following pontine hemorrhage].

We reported three cases with involuntary movements following pontine hemorrhage. All cases had various symptoms indicating brain-stem lesions, but the consciousness and motor functions were not severely disturbed. CT scans showed a small hematoma localized in unilateral pontine tegmentum in all cases. Intention tremor developed six to ten months after the hemorrhage when the initial neurological symptoms were almost relieved. Electromyogram (EMG) showed a rhythmic 3-4 Hz alternating or synchronized tremor pattern which was induced by finger-nose test and arm stretching. In one case which had showed bilateral horizontal gaze palsy indicating bilateral PPRF involvement in the acute stage, spontaneous vertical nystagmus was observed when the tremor developed. Electronystagmogram (ENG) and its differential calculus showed a pendular nature of the eye movement. This abnormal eye movement did not disappear while the patient was asleep. This case also developed a palatal myoclonus in the chronic stage. Magnetic resonance images (MRI's) obtained one to three years after the hemorrhage revealed a lesion localized in hemipontine tegmentum. The responsible lesion of these involuntary movements was thought to be located in pontine tegmentum from the MRI findings. The functional Prognosis of small hemorrhage in unilateral pontine tegmentum is generally good, but care should be taken for the possibility of late development of various types of involuntary movement.

Cerebral Hemorrhage↗
PubMed1987

Structure of the reaction center from Rhodobacter sphaeroides R-26: the cofactors.

The three-dimensional structure of the cofactors of the reaction center of Rhodobacter sphaeroides R-26 has been determined by x-ray diffraction and refined at a resolution of 2.8 A with an R value of 26%. The main features of the structure are similar to the ones determined for Rhodopseudomonas viridis [Michel, H., Epp, O. & Deisenhofer, J. (1986) EMBO J. 5, 2445-2451]. The cofactors are arranged along two branches, which are approximately related to each other by a 2-fold symmetry axis. The structure is well suited to produce light-induced charge separation across the membrane. Most of the structural features predicted from physical and biochemical measurements are confirmed by the x-ray structure.

Bacterial Proteins↗
PubMed1987

Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits.

The three-dimensional structure of the protein subunits of the reaction center (RC) of Rhodobacter sphaeroides has been determined by x-ray diffraction at a resolution of 2.8 A with an R factor of 26%. The L and M subunits each contain five transmembrane helices and several helices that do not span the membrane. The L and M subunits are related to each other by a 2-fold rotational symmetry axis that is approximately the same as that determined for the cofactors. The H subunit has one transmembrane helix and a globular domain on the cytoplasmic side, which contains a helix that does not span the membrane and several beta-sheets. The structural homology with RCs from other purple bacteria is discussed. A structure of the complex formed between the water soluble cytochrome c2 and the RC from Rb. sphaeroides is proposed.

Bacterial Proteins↗
PubMed1987

Structure of the reaction center from Rhodobacter sphaeroides R-26: membrane-protein interactions.

The energetics of membrane-protein interactions are analyzed with the three-dimensional model of the photosynthetic reaction center (RC) from Rhodobacter sphaeroides. The position of the RC in the membrane and the thickness of the membrane were obtained by minimizing the hydrophobic energy with the energy function of Eisenberg and McLachlan. The 2-fold symmetry axis that relates the L and M subunits is, within the accuracy of 5 degrees, parallel to the normal of the membrane. The thickness of the membrane is estimated to be 40-45 A. Residues that are exposed to the membrane are relatively poorly conserved in the sequences of homologous RC proteins. The surface area of the RC is comparable to the surface areas of water-soluble proteins of similar molecular weight. The volumes of interior atoms in the RC are also similar to those of water-soluble proteins, indicating the same compact packing for both types of proteins. The electrostatic potential of the cofactors was calculated. The results show an asymmetry in the potential between the two possible pathways of electron transfer, with the A branch being preferred electrostatically.

Bacteria↗
PubMed1986

Differentiation of oocyte- and somatic-type 5S rRNAs in animals.

In some amphibians and bony fishes, oocyte- and somatic-type 5S rRNA genes are expressed differently in oocytes and somatic cells. In order to determine at what stage of animal evolution this differential expression system appeared and how it is regulated, the sequences of oocyte and somatic 5S rRNAs from three invertebrates (sea urchin, sea hare, and silkworm) and two vertebrates (lamprey and chick) were analyzed. It was found that the oocyte 5S rRNA from lamprey consists of two components, while its somatic 5S rRNA consists of only one. In other animals, such differential expression of 5S rRNA in oocytes and somatic cells was not seen. A phylogenetic tree of 63 animal 5S rRNAs was constructed by means of the parsimony method, and the evolution of oocyte and somatic-type 5S rRNAs was discussed.

Animals↗
PubMed1985

[Time-dependent measurement of differential digital plethysmogram in bicycle ergometer exercise].

Time-dependent measurements of differential digital plethysmogram during exercise were made on five male subjects. The results obtained were as follows; Differential digital plethysmogram (delta DPG) was obtained by using biophysical amplifier with the time constant of 0.03 seconds which minimized the fluctuation of the baseline in digital plethysmogram (DPG). A linear relationship was shown in P wave amplitude of both delta DPG and DPG. The decrease in delta DPG-P waves was observed in visual concentrations, mental learning and arithmetic, initial inspiratory phase with tachycardia, maximal inspiratory and/or expiratory breath holding, and head-up tilt at 60 degrees or over. The increase in delta DPG-P waves was obtained at the expiratory phase with bradycardia and in the effect of alcohol intake. During 15 minutes of bicycle ergometer exercise at 750 kpm/min, the P wave amplitude in delta DPG decreased to 77% of the control in the first one minute of exercise, and then gradually increased to 218% at the final stage of exercise (p less than 0.01). Heart rate measured simultaneously increased, as compared from the beginning of exercise. P wave amplitude and heart rate after exercise decreased progressively to the control level. It is suggested that the initial decrease in P wave amplitude of delta DPG couples with the dominant activity of the sympathetic vasoconstrictor, and the final increase in P waves is due to the compound factors of the increased cardiac output and arteriolar vasodilation.

Adult↗
PubMed1983

Nucleotide sequences of 5s rRNAs from sponge Halichondria japonica and tunicate Halocynthia roretzi and their phylogenetic positions.

The nucleotide sequences of 5S rRNAs from sponge Halichondria japonica and tunicate Halocynthia roretzi were determined by chemical and enzymatic gel methods. Their phylogenetic positions among metazoans were derived from the 5S rRNA sequences by a computer analysis based on the maximum parsimony principle. It was suggested that the sponge is closely related to several invertebrates and the tunicate has affinity to vertebrates rather than invertebrates.

Animals↗
PubMed1983

Terminal heterogeneity and corrections of the nucleotide sequence of 5S rRNA from an extreme thermophile, Thermus thermophilus HB8.

The nucleotide sequence of 5S rRNA from an extreme thermophile Thermusthermophilus HB8 has been re-examined and determined as [Formula: see text] The present study could resolve previously ambiguous residues and find two additional residues (G(8 3), C(9 7)), G at position 89 and two terminal heterogeneities which are exactly the same as reported with Thermusaquaticus 5S rRNA.Images

Base Sequence↗