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Y Kakimoto

Publications and source records attributed to Y Kakimoto.

At least 37 records · Page 2Linked to original sources
PubMed1991

Characteristic distribution of alpha 2 wave in electroencephalograms of schizophrenic patients during discriminative tasks: support for the hypofrontality hypothesis of schizophrenia.

In a preliminary study, we noticed that alpha 2 activity in the frontal regions was suppressed less in schizophrenic patients than in other patients during the discriminative tasks. This was confirmed with 37 schizophrenic and 16 nonschizophrenic patients under the treatment of neuroleptics, 15 nonmedicated schizophrenic patients and 32 normal controls. The EEGs in eye-closed resting and during the auditory and visual discriminative tasks were recorded. Alpha 2 power values of the frontal, central, parietal, occipital and temporal regions in every subject group were processed by cluster analysis. During the discriminative tasks, the frontal regions were the most isolated cluster in schizophrenic patients and, in the normal and medicated nonschizophrenic groups, the frontal regions were incorporated in a different cluster. The same result was obtained by different statistical analyses of F-alpha 2 power ratio. The relative abundance of alpha 2 power value shifts from the occipital to the frontal regions during the discriminative tasks in schizophrenic patients. The weakened suppression of alpha 2 waves in the frontal regions by the discriminative tasks in schizophrenic patients supports the hypofrontal hypothesis of schizophrenia.

Adolescent↗
PubMed1990

Further studies on D-3-aminoisobutyrate-pyruvate aminotransferase.

D-3-Aminoisobutyrate-pyruvate aminotransferase (EC 2.6.1.40, D-BAIB aminotransferase) participates in the metabolism of thymine. Recently we purified this enzyme from rat liver. We have studied D-BAIB aminotransferase further to clarify its physiological function. Among our findings were the following. (1) The enzyme activity was widely distributed in the organs of guinea pigs and rats. The kidney, liver, and lung showed high specific activities. (2) Using the livers of six vertebrates, differences between species were studied. Activity was detected in all species, the human liver showing the lowest activity among them. (3) Developmental study using rat liver showed that the activity was low at birth, increased sharply thereafter for 10 days, and then subsequently declined to the adult level. (4) Intraperitoneal injection of BAIB and beta-alanine in rats was performed to determine whether they induce activity of this aminotransferase. Only BAIB increased the activity of the aminotransferase in the liver significantly. (5) Subcellular distribution study of this aminotransferase in rat liver revealed that it is a mitochondrial enzyme.

Aging↗
PubMed1990

High concentration of free trimethyllysine in red blood cells.

A high concentration of a basic unidentified amino compound was found in the blood of rats. It was isolated and identified as N epsilon,N epsilon,N epsilon-trimethyllysine by paper chromatography, thin-layer chromatography, high-performance liquid chromatography and amino acid analyzer. It was localized exclusively in red blood cells in the blood of rats. Free trimethyllysine was also determined in the liver, kidney, spleen, brain, muscle, heart and testis of rat. The concentration of free trimethyllysine in red blood cells was more than 10-times as high as that in the other tissues. This compound in red blood cells was found in different species of animals. The relationship between this free trimethyllysine and carnitine was discussed.

Amino Acids↗
PubMed1990

Purification and characterization of D-3-aminoisobutyrate-pyruvate aminotransferase from rat liver.

D-3-Aminoisobutyrate-pyruvate aminotransferase (EC 2.6.1.40) was purified 1900-fold from rat liver extract. The purified enzyme showed a molecular mass of 180 kDa by gel-permeation HPLC analysis using a TSK gel G3000SW column. Reductive polyacrylamide gel electrophoresis in sodium dodecyl sulfate resulted in identification of a single band of approx. 50 kDa, indicating that the native enzyme is probably a tetrametric protein. The specific activity of the purified enzyme was 1.14 mumol/min per mg protein. D-3-Aminoisobutyrate and beta-alanine were good amino donors. The Km value for L-3-aminoisobutyrate was 100-times larger than that for the D-isomer. The apparent Km values for D-3-aminoisobutyrate and beta-alanine were 35 and 282 microM, respectively. Pyruvate, glyoxylate, oxalacetate, 2-oxo-n-valerate, and 2-oxo-n-butyrate were good amino acceptors. The apparent Km values for pyruvate and glyoxylate were 32 and 44 microM, respectively.

Animals↗
PubMed1990

[Sleep-wake complaints in Parkinson's disease].

We analyzed the questionnaires concerning sleep-wake complaints in 1,575 Parkinsonian patients and 2,509 controls of 945 office workers and 1564 seniors living at home. The questionnaire included 20 contents. The Parkinsonian patients complained of sleep-wake disturbances more frequently than the controls in initiation disturbance, frequent awakenings in night, early morning awakening, day time sleepiness, usage of sleep pills, parasomnias, restless legs symptoms, nocturnal myoclonus, snoring, apnea episodes and dyspnea in night (chi-square method). The incidences of restless legs symptoms and nocturnal myoclonus increased significantly with worsening of physical symptoms in the Parkinsonian patients (p less than 0.01).

Aged↗
PubMed1989

Sphingolipid hydrolase activator proteins and their precursors.

Activator proteins for sphingolipid hydrolases (saposins) are small acidic, heat-stable glycoproteins that stimulate the hydrolysis of sphingolipids by lysosomal enzymes. The molecular mass of each stimulator is about 10 kDa, but glycosylated forms of higher mass exist too. The distribution and developmental changes in two saposins and their precursor proteins were studied with the aid of monospecific antibodies against saposin-B and saposin-C. They show a wide distribution in rat organs and forms intermediate between saposin and prosaposin (the precursor protein containing four different saposin units) could be seen. The amount of saposin and the degree of processing from prosaposin are quite different in different tissues. The saposins are the dominant forms in spleen, lung, liver, and kidney, while skeletal muscle, heart, and brain contain mainly precursor forms. In human blood, leukocytes contain mainly saposin, while plasma contains mainly precursor forms and platelets show many forms. Their subcellular distribution was studied using rat liver. The saposins of approximately 20 kDa are dominant in the light mitochondrial, mitochondrial, and microsomal fractions, following the distribution of the activity of a lysosomal marker enzyme. The nuclear fraction exhibits bands corresponding to non-glycosylated saposin. The soluble fraction contained much precursor forms. A developmental study of rat brain showed that the concentration of saposin precursors increased with age.

Animals↗
PubMed1989

Crew workload in JASDF C-1 transport flight: II. Change in urinary catecholamine excretion.

Serial changes in urinary catecholamine excretion were determined for 17 cockpit crews (6 captains, 6 copilots and 5 flight engineers) of JASDF C-1 aircraft during 10-hour (h) scheduled flights, in which captains and copilots performed almost the same flight tasks. The norepinephrine/epinephrine ratio (N/E) in copilots decreased significantly during the flight, whereas little decrease of the N/E was found in captains. Flight engineers showed an intermediate N/E value between captains and copilots. Hormonal responses appeared to correlate with differences in the amount of flying experience of crewmembers. Differences between captains and copilots were more significant when handling the aircraft. Results suggested that flight stresses perceived by crewmembers in the same cockpit were influenced by their flying experience and flight position which could be clearly assessed by determining relative excretions of epinephrine and norepinephrine.

Adult↗
PubMed1988

Crew workload in JASDF C-1 transport flights: I. Change in heart rate and salivary cortisol.

The physiological responses of heart rate and salivary cortisol for six paired captains and co-pilots during JASDF scheduled transport flights were compared to assess crew workload. The relative change of both responses showed similar patterns and were influenced significantly by whether pilots were controlling the aircraft. Moreover, differences in flying experience and responsibility of captains and co-pilots influenced the two physiological responses; heart rate and salivary cortisol measures increased more for both captains and co-pilots while they were in control of the aircraft than when they were not. Compared to captains, co-pilots showed much higher activation and variability in relative change of heart rate and salivary cortisol between periods of controlling and non-controlling the aircraft. On the other hand, captains showed relatively constant responses comparing aircraft controlling and non-controlling periods, especially in the cruise phase of flight. Salivary cortisol may be a useful, non-invasive method of assess crew workload.

Adult↗
PubMed1987

Distribution of alpha-(gamma-aminobutyryl)-hypusine.

The distribution of alpha-(gamma-aminobutyryl)-hypusine was examined in several organs of the rabbit and in the brain of the rat, rabbit, dog, ox, and monkey. The peptide occurred only in the brains, but appeared to be absent from dog brain. Concentrations were higher in the cerebral hemispheres than in other portions of the brain. No significant difference between white and gray matter was observed.

Animals↗
PubMed1987

Purification and properties of calmodulin-lysine N-methyltransferase from rat brain cytosol.

A S-adenosylmethionine:protein-lysine N-methyltransferase (EC 2.1.1.43) has been purified from rat brain cytosol 7,080-fold with a yield of 8%, using octopus calmodulin as a substrate. It contains a lysine residue that is not fully methylated. The enzyme was purified by ammonium sulfate fractionation, Sephacryl S-200 gel filtration, and phosphocellulose and octopus calmodulin-Sepharose affinity chromatographies. Among protein substrates, it was highly specific toward octupus calmodulin. The Km values for octopus calmodulin and S-adenosyl-L-methionine were found to be 2.2 X 10(-8) M and 0.8 X 10(-6) M, respectively. The molecular weight was estimated to be 57,000 by gel filtration and the pH optimum was between 7.5 and 8.5. The enzyme was stimulated in the presence of 10(-7) M Mn2+ and 10(-4) M Ca2+. HPLC of the acid hydrolysate of methyl-3H-labeled calmodulin showed the formation of epsilon-N-mono, epsilon-N-di, and epsilon-N-trimethyllysine. Reverse-phase HPLC of tryptic peptides of the methyl-3H-labeled calmodulin demonstrated that the labeled N-methyllysine lies in the 107-126 peptide. These findings suggest that this enzyme methylated a specific lysine residue of octopus calmodulin.

Animals↗
PubMed1986

In vitro carboxymethylation of myelin basic protein.

During a study to find natural substrate proteins of carboxymethylation, myelin basic protein was found to be a good substrate. The two protein carboxymethylases were purified partially using myelin basic protein as a substrate. These two enzymes may be identical with protein carboxymethylase I and II, which have been found to methylate gamma-globulin. The Km of myelin basic protein (25 microM) was very small compared with other substrates. The activities of the two carboxymethylases were high in the rat brain in comparison to the other rat organs. The activity increased during the period of myelination in the rat brain. These findings suggest that carboxymethylation of myelin basic protein may play an important role in myelination.

Animals↗
PubMed1986

Isolation and identification of alpha-(gamma-aminobutyryl)-hypusine.

A new dipeptide, alpha-(gamma-aminobutyryl)-hypusine, was identified in bovine brain. This compound was isolated from trichloroacetic acid-soluble fraction of bovine brain with five steps of ion-exchange chromatography. Its structure was postulated by routine chemical analyses and determined by synthesis. The amount of the compound isolated from 1.2 kg of bovine brain was 870 nmol.

Animals↗
PubMed1985

Accelerated protein turnover in the skeletal muscle of dystrophic mice.

The excretion of 3-methylhistidine increased in the urine of dystrophic mice C57BL/6J. The content of 3-methylhistidine residue decreased in the muscle proteins of dystrophic mice, but not in other organs. Methylated proteins in the skeletal muscle, actin and myosin, were partially purified from the dystrophic and control muscles. The amount of 3-methylhistidine residue in unit weight of the actin and myosin preparations was normal in dystrophic muscle. These three facts indicate that the turnover rates of actin and myosin are increased in the muscle of the dystrophic mice.

Actins↗
PubMed1984

A rapid and sensitive method for the determination of hypusine in proteins and its distribution and developmental changes.

A simple and sensitive method for determining hypusine in proteins was developed. A greater part of amino acids in the acid hydrolysate of proteins was separated from hypusine by treatment with an ion-exchange resin. The sample containing partially purified hypusine was then analyzed by high-performance liquid chromatography using the post-column derivatization method with o-phthalaldehyde. The recovery rate of hypusine through the overall procedure was more than 95%. Using this method, the distribution and developmental changes of hypusine in proteins were determined. The amino acid was found in proteins of all examined organs of rat. Its concentration was 5-40 nmol/g protein. The subcellular distribution in rat liver was also determined. About 60% of total amount of hypusine was present in the proteins of cytoplasmic and microsomal fractions and its relative concentration was high in the proteins of microsome and lysosome and low in mitochondria. In developing rat, the concentration of hypusine in the brain proteins was relatively high during the first 2 or 3 weeks of postnatal life and then decreased until adulthood. Its concentration in the liver proteins was highest at birth and then decreased continuously to the adult level.

Animals↗