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Biomedical subjects

S Endo

Publications and source records attributed to S Endo.

At least 577 records · Page 32Linked to original sources
PubMed1988

[Studies on absorption and excretion of rokitamycin dry syrup in healthy volunteers].

The absorption and excretion of rokitamycin (RKM) in dry syrup form for children were studied following oral administration to fasted healthy volunteers with high gastric acidity as a suitable model to estimate bioavailability of RKM in children. In a comparative study on tablet and dry syrup forms, peak plasma concentrations of RKM and areas under plasma concentration-time curve (AUC) values were calculated using the trapezoidal rule. RKM dry syrup gave about 84 and 86% of these values for RKM tablet. Urinary recovery of RKM in 8 hours with the administration of dry syrup was also about 80% of the value obtained with tablet. Judging from these results, the bioavailability of RKM administered as dry syrup, was fairly close to that obtained with RKM tablet. The AUC values were dose dependent when examined with dose levels of 300, 500 and 800 mg administered as RKM dry syrup. The AUC value and urinary recovery of RKM administered as dry syrup were 3-4 times higher than these values for midecamycin acetate administered also as dry syrup.

Absorption↗
PubMed1988

[Acute epidural hematoma of the posterior fossa caused by forehead impact].

A rare case of acute epidural hematoma of the posterior fossa caused by forehead impact is reported. This 36-year-old man fell from a truck and hit his face. He was conscious and was brought to our center 30 minutes after the injury. On admission, a contused wound of the right forehead was noticed. He was restless and had severe pain in the neck and upper extremities. Skull X-ray showed a linear fracture of the frontal bone and computed tomography (CT) scan was normal. He continued to be restless and sudden respiratory arrest and pupillary dilation occurred 10 hours after the admission. A CT scan revealed a lenticular high density area in the left posterior fossa which extended to the supratentorial region. The 4th ventricle was compressed and displaced to the right and also the quadrigeminal and ambient cisterns were not visualized at all. Immediate surgery disclosed a 30 g epidural hematoma of the left posterior fossa and the supratentorium and the clot was completely evacuated. The source of bleeding could not be identified. Opening of the dura revealed contusion in the occipital lobe. He died on the 17th postoperative day. The possible mechanism in the production of the posterior fossa hematoma in this case is discussed.

Adult↗
PubMed1988

[A case of isolated cerebral angiitis with sequential angiographic changes].

The pathogenesis of migraine has not been completely understood. However, it is generally accepted that the prodromal symptoms encountered in classic migraine usually result from vasoconstriction of intracranial vessels, while the headache itself results from dilation of other cranial vessels, often branches of the external carotid artery. Despite of increasing refinement in angiographic technique, many authors demonstrate the difficulty of interpreting abnormal radiographic findings in patients of migraine. We experienced recently a rare case who complained of migraine with neurological disorder manifesting for dynamic changes of cerebral arteries on sequential angiography. This 39-year-old man was admitted to our hospital with complaint of classic migraine accompanied with transient hemiparesis of the left side. Curious dynamic changes were noted sequentially on the repeated angiograms sequentially during his hospitalization. The carotid angiogram on admission showed narrowing at the right M1 portion. The second angiogram obtained at the fourth hospital day showed reduction of the narrowing, and occlusion of the right angular artery. The patient was treated with Ergotamine. The third angiogram taken after admission for the period of 1 month showed increased stenosis at the right M1 portion. Isolated angiitis of central nervous system was suspected because of such sequential dynamic angiographic changes, and steroid therapy was started. However he began to suffer from hemiparesis of left side one week after the treatment. Therefore, EC-IC bypass was performed, and his symptoms were improved gradually. Migraine is one of the common neurologic disorders countered in clinical practice. This report suggests that careful observation is needed in patients of migraine.

Adult↗
PubMed1987

Comparative structural study of the N-linked oligosaccharides of human normal and pathological immunoglobulin G.

The structures of oligosaccharides of normal and pathological immunoglobulin G (IgG) are reported. Asparagine-linked neutral oligosaccharides were released by N-oligosaccharide glycopeptidase (almond) digestion. The reducing ends of the oligosaccharide chains thus obtained were aminated with a fluorescent reagent, 2-aminopyridine, and the mixture of pyridylamino derivatives of the oligosaccharides was separated by reverse-phase high-performance liquid chromatography. It was possible to separate 15 out of the 16 kinds of oligosaccharides that have been suggested to exist in normal human IgG. High-resolution proton nuclear magnetic resonance spectroscopy was used along with chemical methods to determine the structures of the separated oligosaccharides. It has been shown that in normal IgG a biantennary complex-type oligosaccharide with a fucose residue (formula; see text) is predominant and four kinds of oligosaccharides, which are biantennary with bisecting N-acetylglucosamine and without fucose residues, exist only in a very small quantity. The results obtained for normal IgG were compared with those obtained for three myeloma IgG proteins. It has been found that the most abundant species that exist in the pathological proteins analyzed in the present work lack one or two galactose residues at the nonreducing terminal. We show that the fractions of fucose-containing oligosaccharides are markedly decreased in the heavy-chain disease protein Per. It is of particular interest that in this paraprotein the major component is a biantennary complex-type oligosaccharide that lacks a fucose residue and an oligosaccharide with the structure (Formula: see text) exists as one of the most abundant components.

Asparagine↗
PubMed1987

On the pathogenesis of chronic alcoholic pancreatitis from the viewpoint of experimental results in rats.

To elucidate the pathogenesis of chronic alcoholic pancreatitis, light-microscopic and electron microscopic observations of pancreases from Wistar strain rats given 20% ethanol ad lib, instead of water, were performed. Results were as follows: (1) In 3 (11%) rats, focal lobular unit acinar cell damage was observed under light-microscopy. In these cases, the intercalated ducts and centroacinar cells showed proliferation independently of protein plugs in ducts. (2) After ethanol intake, several degenerative changes in the acinar cells and ductular cells were observed under electron microscopy. The earliest and most consistent change was the irregular formation of microvilli and interdigitation between the parenchymal cells, accompanied by widening of the intercellular space, especially between the acinar and centroacinar cells. After three months of ethanol intake, an increase in the lysosomes and mitochondrial alteration occurred in acinar cells, and after six months of ethanol ingestion, there was tortuous ductular proliferation accompanied by the degeneration of the ductular cells. In addition to these parenchymal changes, the capillary endothelium and nervous tissue of the pancreas showed occasional degenerative changes after three to six months of ethanol intake. These results suggest that repeated degeneration and regeneration of the ductular cells results in deformation of ductular structures, with subsequent stenosis, and represents the primary event in the development of chronic alcoholic pancreatitis in rats.

Alcoholism↗
PubMed1987

Structural analysis of N-linked oligosaccharides by a combination of glycopeptidase, exoglycosidases, and high-performance liquid chromatography.

A simple, sensitive, and rapid method for the analysis of structures of N-linked carbohydrates is reported. The method involves four steps: preparation of carbohydrate chains from glycopeptides by N-oligosaccharide glycopeptidase digestion; derivatization of the reducing ends of carbohydrate chains with a fluorescent reagent, 2-aminopyridine, by using sodium cyanoborohydride; separation of oligosaccharide derivatives by reverse-phase high-performance liquid chromatography; and structural analysis of oligosaccharides by sequential exoglycosidase digestion. The elution positions of 50 standard oligosaccharide derivatives were determined by HPLC. The structure of an unknown oligosaccharide can be characterized by comparison of its elution position with those of the standard compounds. The method was applied to elucidate the structures of oligosaccharides in the myeloma IgG protein, Yot.

Amidohydrolases↗
PubMed1987

Structures of the sugar chains of a major glycoprotein present in the egg jelly coat of a starfish, Asterias amurensis.

Sugar chains of a major glycoprotein, obtained from the egg jelly coat of a starfish (Asterias amurensis), were released quantitatively as oligosaccharides by hydrazinolysis. After N-acetylation, they were converted to radioactive oligosaccharides by reduction with NaB3H4. Analysis by paper electrophoresis revealed that all of them were neutral oligosaccharides. Upon Bio-Gel P-4 column chromatography, the radioactive oligosaccharide mixture was separated into four components. Structural study of each component by sequential glycosidase digestion in combination with 1H-NMR spectroscopy revealed that the glycoprotein contains the following oligosaccharides, in which R represents either proton, Glc alpha 1----, Glc alpha 1----3Glc alpha 1----, or Glc alpha 1----2Glc alpha 1----3Glc alpha 1----. (Formula: see text)

Acetylation↗
PubMed1987

A high molecular weight actin binding protein: its localization in the cortex of the sea urchin egg.

From the Triton-treated cortex fraction of sea urchin eggs, a high molecular weight actin binding protein (260K protein) was solubilized by a high salt solution and purified. A cosedimentation assay revealed that the 260K protein binds to actin filaments in a concentration-dependent manner. The low-shear viscosity of actin solutions largely increased in a concentration-dependent manner after addition of 260K protein. Electron microscopy showed that this protein induces the formation of large curled bundles of actin filaments. Different from fascin-induced actin bundles, no clear striations were observed within the actin bundles formed by the 260K protein. Antibodies against the 260K protein were raised in a rabbit and affinity purified. Immunoblotting analysis of Triton-solubilized cortex and various subcellular fractions showed that first only a single band reacted with the antibody and second that the 260K protein exclusively localized in the cortex fraction. Indirect immunofluorescence microscopy localized the protein in the cortex and the region of the cleavage furrow. After double staining, the fluorescence images for actin filaments and the 260K protein well correlate with each other.

Animals↗
PubMed1987

[Effect of metabolites on the human plasma concentration as total activity after oral administration of rokitamycin. Comparison of three different bioassay methods].

Three different bioassay methods for rokitamycin (TMS-19-Q) were compared to each other in vitro and in vivo. Method I was a paper disc method using Micrococcus luteus ATCC 9341 as the test organism in nutrient agar (pH 8.0), method II was a paper disc method using Streptococcus pyogenes Cook in brain heart infusion agar (pH 7.4) and method III was an agar well method using M. luteus ATCC 9341 in the agar medium provided in the Minimum Requirements for Antibiotic Products of Japan (pH 6.5). Ratios of relative potency of TMS-19-Q and its metabolites calculated from standard curves in human plasma using these bioassay methods, were 1.00:1.13:3.34:0.96 (TMS-19-Q:10"-OH-TMS-19-Q:LM A7:LM V) in method I, 1.00:1.58:0.40 (TMS-19-Q:LM A7:LM V) in method II and 1.00:0.51:0.86:0.114 (TMS-19-Q:10"-OH-TMS-19-Q:LM A7:LM V) in method III. The relative potency obtained from method I, generally used for macrolide antibiotics, greatly contradicted MIC values of TMS-19-Q and its metabolites against clinically isolated 190 strains of Staphylococcus aureus. On the other hand, the relative potency obtained from method III reflected closely MIC values of TMS-19-Q and its metabolites. Therefore, method III should be the most suitable bioassay method to measure the plasma concentration of TMS-19-Q. Plasma concentrations measured by these 3 different methods were compared to each other in vivo, after oral administration of TMS-19-Q at a dose of 1,200 mg to each of fasted healthy volunteers. Values obtained from method I were about 4.3 times higher than those method III.(ABSTRACT TRUNCATED AT 250 WORDS)

Administration, Oral↗
PubMed1987

[Studies on the metabolic fate of isepamicin sulfate (HAPA-B). I. Absorption, distribution, metabolism and excretion in rats].

Absorption, distribution, metabolism and excretion of isepamicin sulfate (HAPA-B), a new aminoglycoside antibiotic, after a single administration were studied in rats. After intramuscular administration of HAPA-B at a dose level between 6.25 and 100 mg/kg, the drug was rapidly absorbed to reach the peak in 0.10 to 0.21 hour (Tmax). The maximum drug concentration in the plasma (Cmax) and the size of the area under the plasma concentration-time curve (AUC) depended on dose levels. The HAPA-B disappeared rapidly from the plasma after intramuscular and intravenous administrations with biological half-lives (T1/2) from 0.41 to 0.47 hour with intramuscular administration and from 0.23 to 0.35 hour with intravenous administration. Peak time after intramuscular, intraperitoneal and subcutaneous administration of HAPA-B at a dose of 25 mg/kg were 0.18, 0.24 and 0.37 hour, respectively. Maximum drug concentrations in plasma were 64.15, 53.71 and 40.39 micrograms/ml and biological half-lives of the drug were 0.47, 0.73 and 0.87 hour, respectively. The HAPA-B was distributed rapidly into tissues, especially at a high level into kidney after intramuscular or intravenous administration of 25 mg/kg. Concentrations in lung and heart were next to that in kidney, but were not higher than plasma concentrations. The drug was excreted mainly into the urine after intramuscular and intravenous administration within 24 hours and approximately 79 to 90% of the administered amount was excreted. Meanwhile, the excretion of HAPA-B into the bile was 0.1% or less during the first 24 hours after intramuscular and intravenous administration. Bioautograms of thin layer chromatographs of 0 approximately 6 hours urine samples after intramuscular administration showed single bands with the identical Rf value to the standard HAPA-B. No difference between male and female was observed in the fate of the administered HAPA-B through intramuscularly. The shape of the plasma concentration curve and the urinary excretion after intramuscular administration of HAPA-B at the dose of 25 mg/kg was similar to those of amikacin (AMK) and gentamicin. Tissue concentrations after intramuscular and intravenous administration of HAPA-B were also similar to AMK.

Aminoglycosides↗
PubMed1987

[Studies on the metabolic fate of isepamicin sulfate (HAPA-B). II. Accumulation of HAPA-B after multiple administration in rats].

The accumulation of isepamicin sulfate (HAPA-B) in tissues and plasma was studied upon multiple intramuscular and intravenous administrations of 25 mg/kg of HAPA-B daily for 8 or 15 days to male rats. Shapes of plasma concentration curves in multiple intramuscular and intravenous administrations were very similar to that in a single administration. Drug concentrations in kidney at 24 hours after 8- and 15-multiple administrations through both routes were 3 to 4 and 4 to 5 times as high as that after a single administration. The concentration in kidney increased by multiple administrations for 8 days, but did not increase so highly there after till the 15-multiple administrations. On the other hand, the elimination of HAPA-B from kidney after multiple administrations was similar to that after a single administration. The accumulation of HAPA-B upon multiple administration was also observed in lung, heart, spleen and liver, but peak concentrations of the drug in these tissues were lower than that in kidney.

Aminoglycosides↗