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Biomedical subjects

N Yagi

Publications and source records attributed to N Yagi.

At least 145 records · Page 8Linked to original sources
PubMed1990

Specific binding of [3H]pyrilamine to histamine H1 receptors in guinea pig brain in vivo: determination of binding parameters by a kinetic four-compartment model.

The binding of [3H]pyrilamine, a selective ligand of histamine H1 receptors, to guinea pig brain in vivo was compared with its binding to a brain homogenate. The pharmacological properties (regional distribution, saturability, and stereoselectivity) of the [3H]pyrilamine binding in vivo were similar to those of the in vitro binding to brain homogenate. A dynamic four-compartment model was proposed for the analysis of the kinetics of [3H]pyrilamine binding in vivo. The receptor constants in vivo were determined by a computer-fitting method after correcting the radioactivity of arterial plasma and brain for the presence of radioactive metabolites. The in vivo association and dissociation were 213 and 42 times, respectively, slower than those of in vitro binding at 37 degrees C. A possible mechanism for slow association and dissociation in vivo is discussed.

Aminopyridines↗
PubMed1990

Studies on antiallergic agents. I. Synthesis and antiallergic activity of novel pyrazine derivatives.

Various pyrazine derivatives were synthesized and their antiallergic activity was examined. The inhibitory activity on allergic histamine release of the compounds bearing a 5-tetrazolyl group was more potent than that of the corresponding carboxyl derivatives. The introduction of -CONH- or -NHCO- between the pyrazine ring and the 5-tetrazolyl group as a spacer greatly enhanced the activity. N-(1H-Tetrazol-5-yl)-2-pyrazinecarboxamide (I-3) was estimated to exhibit nearly the same potency as disodium cromoglycate (DSCG). The structure-activity relationship among various derivatives modified by introducing some substituents onto the 3-, 5- or 6-position of the pyrazine ring of I-3 was investigated. The activity remained unchanged or was reduced when such substituents as methyl, chloro, methoxy, methylamino and dimethylamino were introduced at the 3- or 5-position. In contrast, 6-substitution with various alkylamino groups more or less increased the activity. Among them, the 6-dimethylamino (I-17c) and 6-(1-pyrrolidinyl) (I-34) derivative were proved to be most potent. The IC50 values (concentration which produces 50% inhibition of the allergic histamine release) of I-17c and I-34 were determined to be 4.7 x 10(-10) and 4.6 x 10(-10) M, respectively. These two compounds produced a potent inhibitory activity on passive cutaneous anaphylaxis (PCA) in rat, not only by the intravenous route (ED50 = 0.0096 mg/kg for both compounds) but also by the oral route (ED50 = 0.19 and 0.18 mg/kg, respectively). On the other hand, when the pyrazine ring of some representative compounds was replaced with a pyridine ring, the inhibitory activity on histamine release was significantly reduced.

Animals↗
PubMed1990

[Studies on quinolone antibacterials. I. Synthesis and antibacterial activity of 7-(2-aminoethoxy)-, 7-(2-aminoethylthio)-, and 7-(2-aminoethylamino)-1-cyclopropyl-6-fluoro-1,4-dihydro-4-oxo qui noline -3-carboxylic acids and their derivatives].

7-(2-Aminoethoxy)-, 7-(2-aminoethylthio)-, and 7-(2-aminoethylamino)-1-cyclopropyl-6-fluoro-1,4-dihydro-4-oxoq uin oline-3- carboxylic acids and their derivatives (11a--f, h, j, k, 12a--f, and 13a--f) were synthesized and their antibacterial activities were tested. Among them, compounds (13a, d) having a primary amino group at the terminal position of alkoxy and alkylthio groups were found to have excellent in vitro and in vivo antibacterial activity comparable to those of ciprofloxacin (5). Structure-activity relationship of these compounds was also stated.

Animals↗
PubMed1989

Structural changes in the thin filament during activation studied by X-ray diffraction of highly stretched skeletal muscle.

The actin layer-lines were recorded from a frog semitendinosus muscle stretched to a sarcomere length greater than 4.4 microM. On activation of the muscle, the equator, the second layer-line at 1/18 nm-1 and the 5.9 nm layer-line increased in integrated intensity. On the other hand, the integrated intensity of the first layer-line at 1/36 nm-1 decreased markedly on activation. This decrease was not fully attributable to shifts of tropomyosin strands and therefore suggested a structural change in the actin subunit. The decrease may account for the apparent lack of an intensity increase of this layer-line on activation at normal muscle lengths where attachment of myosin heads to actin increases the intensities of other layer-lines.

Actins↗
PubMed1989

Effect of 15(R)-15-methyl PGE2 (arbaprostil) on duodenal bicarbonate secretion in rat.

The present study was designed to observe the effect of 15(R)-15-methyl PGE2 (arbaprostil) on duodenal bicarbonate secretion in male Wistar rats anesthetized with urethane. A proximal duodenal loop (1.5cm) was made and perfused with saline (pH4.5) in an air tight circle system. The pH and Pco2 of the perfusing fluid were measured continuously and the quantity of bicarbonate was calculated according to the Henderson-Hasselbalch equation. Vehicle or arbaprostil was injected intravenously as a bolus injection. The total output of bicarbonate in 30 min was as follows; control: 0.449 +/- 0.093 microEq (mean +/- SE); 1,10 and 100 mu/kg of arbaprostil: 0.752 +/- 0.218, 2.75 +/- 0.430 and 5.958 +/- 0.578 microEq respectively. Arbaprostil (10 and 100 micrograms/kg) increased the total output of bicarbonate significantly (p less than 0.001). The rate of secretion was also increased by arbaprostil.

Animals↗
PubMed1989

Cross-bridge movement in rat cardiac muscle as a function of calcium concentration.

1. By applying the X-ray diffraction method to chemically skinned papillary muscles of the rat, the transfer of myosin heads from the thick to the thin filaments was studied as a function of Ca2+ concentration. 2. No significant transfer of the heads occurred when the Ca2+ concentration was below the threshold of contraction (pCa 6.2). 3. During the maximum isometric contraction at pCa 4.4, 80% of the myosin heads were transferred to the thin filament. 4. When the muscle was activated isometrically at low Ca2+ concentrations (pCa 6.2-5.8), where the average tension was less than 20% of the maximum, a disproportionately large number of myosin heads were transferred to the thin filament. 5. It was concluded that a significant fraction of the heads transferred at the low Ca2+ concentrations does not produce tension.

Animals↗
PubMed1988

An X-ray diffraction study of alpha-tropomyosin magnesium tactoid.

The structure of the needle-shaped aggregate of alpha-tropomyosin formed in the presence of Mg2+ ions (the Mg-tactoid) was studied by X-ray diffraction. Orientated specimens were prepared by magnetic orientation. The meridional reflections corresponding to a Bragg spacing of up to 2.6 nm were recorded and phased by the isomorphous replacement method using p-chloromercuribenzoate bound to the unique cysteine residue of the alpha-chain of tropomyosin. The axial electron density profile thus obtained was compared with the model proposed from electron microscopic investigations. With an adequate phase combination for the observed intensities, the agreement was satisfactory. Comparison with electron micrographs of negatively stained Mg-tactoids suggests that the C-terminus of the molecule has an extended conformation and penetrates into the N-N overlap region. The principal repeat length along the tactoid was 39.0 nm, which was about 5% shorter than the expected periodicity of the tropomyosin molecules with an end-to-end overlap of eight residues, suggesting supercoiling. The equatorial reflections consisted of the diffuse peaks at 1/8 nm-1 and 1/2.3 nm-1. The former indicates, for the first time, the presence of a large structural unit with low crystallinity. The spacing of the latter probably corresponds to the average centre-to-centre distance between neighbouring tropomyosin molecules.

Animals↗
PubMed1988

Changes in the 5.9 nm actin layer-line on activation of frog skeletal muscles.

The intensity changes of the actin layer-lines during activation of sartorius and overstretched semitendinosus muscles were measured by using a two-dimensional X-ray detector. In both muscles, the intensity of the 5.9 nm layer-line increased without a detectable shift in the peak position. The intensity of the second layer-line increased in both muscles by a similar amount. In semitendinosus muscle, a large intensity decrease of the first actin layer-line was observed. Model calculations suggest that these results are difficult to explain in terms of a simple steric blocking model of regulation involving only a movement of tropomyosin on the actin helix.

Actins↗
PubMed1987

Stapedial muscle electromyography in various diseases.

Stapedial muscle electromyograms (SEMGs), obtained by an averaging technique of electrocochleography, were studied in patients with various diseases. The latency of SEMG was prolonged in incomplete facial palsy (Bell's palsy and cerebellopontine angle tumor), with stapedial reflex (SR) of a small amplitude or without SR. In otitis media with effusion, in which SR could not be obtained, SEMGs were clearly observed and showed normal waveforms and latencies. In Meniere's disease and sensorineural hearing loss, SEMG waves had normal waveforms and latencies. These results indicate that the SEMG shows a normal waveform and latency when facial nerve function is intact, and that its latency is prolonged in incomplete paralysis of the facial nerve.

Adult↗
PubMed1987

A case of 'spontaneous otoacoustic emission'.

A 25-year-old man produced a continuous high-pitched pure tone (6.1 kHz, 37.2-dB sound pressure level) in his right ear. The tone was not audible to the patient. He had sensorineural deafness over 1 kHz with a dip of 45 dB at 6 kHz. The tone was considered to be emitted through the eardrum from the inner ear, ie, a "spontaneous otoacoustic emission".

Adult↗
PubMed1987

Eustachian tube patency detected by a photoelectric method.

A method was developed to observe tubal orifice movement by fiberscope and detect patency of the eustachian tube by a photoelectric device (phototubometry). A highly sensitive photodiode in the external ear canal detected tube opening as increased luminosity in the tympanic cavity from a light source placed at the pharyngeal portion of the eustachian tube. The phototubometric record was superimposed on a TV screen to compare the opening in the pharyngeal portion of the eustachian tube to the tube opening during swallowing. The phototubometric records of 21 normal subjects examined by phototubometry showed the close relationship with the opened tubal lumen at the tensor veli palatini muscle (TVP) attached portion. This method is useful for examining tubal patency and observing changes in the pharyngeal portion of the eustachian tube.

Deglutition↗
PubMed1986

Inhibitory effects of galanin on the isolated spinal cord of the newborn rat.

The effects of galanin, a 29-amino-acid peptide, on spinal reflexes were studied. In the isolated hemisected spinal cord of the newborn rat, galanin (0.1-5 microM) depressed the monosynaptic reflex that was induced by dorsal root stimulation and recorded from the corresponding ventral root. In the isolated spinal cord-tail preparation of the newborn rat, galanin (0.3-0.6 microM) depressed the nociceptive reflex that was induced by application of capsaicin to the tail and recorded from a lumbar ventral root. In both preparations the inhibitory effects of galanin were reversible and the full recovery of the reflexes was observed within 3-20 min after removal of the peptide. The mechanisms of action of galanin on the spinal reflexes and the physiological role of the peptide in the spinal cord are discussed.

Animals↗
PubMed1985

Lateral filamentary spacing in chemically skinned murine muscles during contraction.

A mouse toe muscle was chemically skinned with saponin and the 1,0 spacing of the hexagonal myofilament lattice at a sarcomere length of 2.5 micron was measured with the X-ray-diffraction method. In the relaxed state, the 1,0 spacing was 40.8 nm. When the muscle was maximally activated at pCa 4.4, the spacing decreased to 38.4 nm. During contractions at lower calcium concentrations, the spacing decreased less. In rigor, the spacing decreased to almost the same extent as during maximum contraction, although the rigor tension was only 8% of the maximum tension. When the spacing in relaxed muscle had been adjusted osmotically to about 38 nm, activation caused no further decrease in the spacing. The results support the view that the force responsible for the lattice shrinkage during contraction is produced by cross-bridges displaced from their optimum lateral positions.

Animals↗
PubMed1985

Movements of cross-bridges during and after slow length changes in active frog skeletal muscle.

The cross-bridge movements underlying the tension responses of active muscle to slow length changes were studied by a time-resolved X-ray diffraction method. During an isometric tetanus at 2 degrees C, the meridional reflexion at 1/14.3 nm-1 was 55% more intense than in the resting state, suggesting that the myosin heads maintain the 14.3 nm periodicity of the thick filament. When active muscle was stretched by 7% at a constant speed of 0.03-0.70 muscle lengths s-1, the intensity of the meridional reflexion decreased progressively as the tension increased continuously during the stretch. This suggests that the myosin heads spread out along the thick filament. During stress relaxation after a stretch, the intensity returned gradually toward the active isometric level, suggesting a rearrangement of the myosin heads. The meridional intensity changed in a similar manner when active muscle was released by 7% at the same speeds; it decreased progressively during the release and returned gradually to the isometric level after completion of the release. The intensity decrease during a release was smaller than that during a stretch, provided the speed was low (0.03-0.09 muscle lengths s-1). It was concluded that the tension responses to slow length changes are due to shifts of the myosin heads along the thick filament, and that the elastic element responsible for tension production is located in the myosin molecules.

Animals↗