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Biomedical subjects

A Kishimoto

Publications and source records attributed to A Kishimoto.

At least 91 records · Page 5Linked to original sources
PubMed1986

Multifocal ventricular ectopic complexes possibly related to diuretic induced hypokalemia in a woman with the long QT syndrome.

A 40-year-old housewife was observed with chief complaints of syncope and palpitation. The electrocardiogram indicated premature ventricular ectopic complexes of the torsade de pointes. Serum potassium level was low because of thiazide-induced hypokalemia for the treatment of transient hypertension. Even after the disappearance of threatening ventricular arrhythmias and normalization of serum potassium level, prolongation of QT interval was continuously persisted. Thiazide induced hypokalemia might have some roles on producing ventricular ectopic activity in prolonged QT syndrome as shown in our case.

Adult↗
PubMed1985

Rat brain and liver soluble phospholipase C: resolution of two forms with different requirements for calcium.

Two forms of phospholipase C, hydrolyzing specifically inositol phospholipids, are resoluted and partially purified from rat brain as well as liver cytosol by DEAE-cellulose followed by heparin-Sepharose, Sephacryl S-400, and aminohexyl-Sepharose column chromatographies. With phosphatidylinositol as substrate, at pH 7.4 one is most active at 10(-6) M Ca2+ (Type I) whereas the other requires 10(-3) M Ca2+ (Type II). At pH 5.5 both Type I and II are active at 10(-3) M Ca2+ but essentially inactive at lower concentrations of this divalent cation. Both Type I and II hydrolyze preferentially polyphosphoinositides particularly at lower concentrations of Ca2+.

Animals↗
PubMed1985

Studies on the phosphorylation of myelin basic protein by protein kinase C and adenosine 3':5'-monophosphate-dependent protein kinase.

The substrate specificity of protein kinase C was studied and compared with that of cyclic AMP-dependent protein kinase (protein kinase A) by using bovine brain myelin basic protein as a model substrate. This basic protein was phosphorylated at multiple sites by both of these protein kinases. In this analysis, the basic protein was thoroughly phosphorylated in vitro with [gamma-32P]ATP and each protein kinase, and then digested with trypsin. The resulting radioactive phosphopeptides were isolated by gel filtration followed by high performance liquid chromatography on a reverse-phase column. Subsequent amino acid analysis and/or sequential Edman degradation of the purified phosphopeptides, together with the known primary sequence of this protein, revealed that Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-161 at various reaction velocities. Contrary to protein kinase A, protein kinase C appears to react preferentially with seryl residues that are located at the amino-terminal side close to lysine or arginine. The seryl residues that are phosphorylated commonly by these two protein kinases have basic amino acids at both the amino- and carboxyl-terminal sides. These results provide some clues to understanding the rationale that these kinases may show different but sometimes similar functions depending on the structure of target phosphate acceptor proteins.

Amino Acid Sequence↗
PubMed1985

Activation of cellular protein kinase C and mode of inhibitory action of phospholipid-interacting compounds.

12-O-Tetradecanoylphorbol-13-acetate (TPA), that is intercalated into the cell membrane, binds a roughly stoichiometric amount of protein kinase C to produce a catalytically active complex with phospholipid. Local anesthetics and other phospholipid-interacting compounds such as chlorpromazine inhibit profoundly this complex formation in a manner competitive with phospholipid but not with TPA. A tiny change of the membrane phospholipid bilayer structure that is caused by TPA appears to facilitate this unique phospholipid-protein kinase C interaction.

Anesthetics, Local↗
PubMed1985

An experimental study on the physical properties of the cupula. Effect of cupular sectioning on the ampullary nerve action potential.

The frog posterior semicircular canal (PSC) was isolated and a part of the ampullary wall was cut to allow removal of the cupula from the crista. The cupula was replaced on the crista and the PSC ampullary action potential was recorded. The cupula was again removed and was sectioned in half, either in the plane vertical to the crista (vertical sectioning), or in the plane parallel to the crista (horizontal sectioning). The sectioned half of the cupula was then replaced on the crista. The action potentials after replacement of the vertical or horizontal segments of the cupula were compared to those achieved when the entire cupula was replaced. After vertical sectioning, the action potentials were significantly reduced; they were 50.3% of the completely replaced cupula when a small stimulus was used and 79.1% when a large stimulus was used. A reduced attachment surface between the cupular base and the crista is possibly responsible for the decreased action potential in the vertically sectioned specimen. After horizontal sectioning, the action potentials were 64.5% for the small stimulus and 108.2% for the large stimulus. These results indicate that elicited responses are related to the height of the cupula and the deflection angle. This further suggests that the movement of the cupula is represented by that of the elastic system.

Action Potentials↗
PubMed1985

[Clinical effects of SM-4300 in severe infectious patients].

A newly developed human immunoglobulin preparation for intravenous use, SM-4300, has been studied in Nagoyashi-Koseiin Geriatric Hospital on the effects of 14 cases of the various severe infections in the combined use with antibiotics. The following results were obtained: The patients had many kinds of underlying diseases. Cerebral vascular disease was the most frequent underlying disease, and found in 70% of 14 patients, followed by heart failure. Among them 8 cases were chosen for the clinical evaluation by doctors in charge. SM-4300 effected good in 1 case, fairly 3 and poorly 4. The efficacy rate was summarized as 12.5%. In all cases, there were no significant side effects regarding symptoms, hematological analysis, renal and live functions. Based on these results, SM-4300 may be safe and a drug worth to try in treatment of severe infections.

Aged↗
PubMed1984

Kinetics of a naltrexone sustained-release preparation.

A biodegradable sustained-release naltrexone bead preparation containing 70% naltrexone in a physical mixture with a copolymer of 90% lactic acid and 10% glycolic acid was evaluated in three male subjects. Each subject received a 10-mg iv dose of naltrexone HCl and a 63-mg dose by subcutaneous implantation of naltrexone beads. Kinetics of naltrexone estimated from the intravenous dose indicated a plasma clearance range of 3.1 to 3.4 l/min and a t 1/2 range of 1.7 to 3.7 hr. After bead implantation, average plasma naltrexone levels were maintained at 0.3 to 0.4 ng/ml and naltrexol levels were at 0.4 to 1.0 ng/ml for a period of approximately 1 mo, during which urine naltrexone and naltrexol levels were about 20 to 30 and 70 to 200 ng/ml. It was estimated that approximately 70% to 77% of the dose was absorbed after bead implantation. There were no serious adverse effects other than tissue irritation in two of the three subjects.

Absorption↗