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Biomedical subjects

S Sawada

Publications and source records attributed to S Sawada.

At least 469 records · Page 26Linked to original sources

[Transcatheter arterial embolization therapy of recurrent pelvic cancer].

Embolization of the internal iliac artery with Gelfoam partiles was performed in 14 patients with recurrent pelvic cancer between February 1984 and February 1985. The sites of treatment were the uterus, urinary bladder, sacral mass, vulva and obstrator muscle. Full-dose radiotherapy had been performed as the primary treatment in 10 cases. According to Karnofsky's criteria, the therapeutic effect of embolization was rated as 1-A or better in 71.4% of the patients. Regarding complications of embolization therapy, two cases of vesicovaginal fistula were noted. All these results suggest that embolization is a useful method for the treatment of recurrent pelvic cancer, especially after radiotherapy.

Adenocarcinoma↗

Oxidation of reduced cucumber ascorbate oxidase.

Reoxidation process of reduced cucumber ascorbate oxidase (1.10.3.3) with dioxygen was investigated in detail through absorption, circular dichroic (CD) and electron paramagnetic resonance (EPR) spectra. One of the three type I coppers and the type II copper were reoxidized more rapidly than other type I coppers. The principal active site of ascorbate oxidase was considered to be comprised of one type I, one type II and a pair of type III coppers similarly to the active sites in laccase and ceruloplasmin. Remaining two type I and a pair of type III coppers were also disclosed to contribute to the oxidation of L-ascorbate.

Ascorbate Oxidase↗

1H NMR studies of substrate hydrogen exchange reactions catalyzed by L-methionine gamma-lyase.

Hydrogen exchange reactions of various L-amino acids catalyzed by L-methionine gamma-lyase (EC 4.4.1.11) have been studied. The enzyme catalyzes the rapid exchange of the alpha- and beta-hydrogens of L-methionine and S-methyl-L-cysteine with deuterium from the solvent. The rate of alpha-hydrogen exchange was about 40 times faster than that of the enzymatic elimination reaction of the sulfur-containing amino acids. The enzyme also catalyzes the exchange reaction of alpha- and beta-hydrogens of the following straight-chain L-amino acids which are not susceptible to elimination: norleucine, norvaline, alpha-aminobutyrate, and alanine. The exchange rates of the alpha-hydrogen and the total beta-hydrogens of L-alanine and L-alpha-aminobutyrate with deuterium followed first-order kinetics. For L-norvaline, L-norleucine, S-methyl-L-cysteine, and L-methionine, the rate of alpha-hydrogen exchange followed first-order kinetics, but the rate of total beta-hydrogen exchange decreased due to a primary isotope effect at the alpha-position. One beta-hydrogen of S-methyl-L-cysteine was exchanged faster than the other, although both the beta-hydrogens were exchanged completely with deuterium ultimately. L-Phenylalanine and L-tryptophan slowly underwent alpha-hydrogen exchange. The pro-R hydrogen of glycine was deuterated stereospecifically. None of the following amino acids were susceptible to the enzymatic hydrogen exchange: D isomers of the above amino acids, branched chain L-amino acids, acidic L-amino acids, and basic L-amino acids.(ABSTRACT TRUNCATED AT 250 WORDS)

Carbon-Sulfur Lyases↗

Impaired B cell proliferation by Staphylococcus aureus Cowan 1 in patients with systemic lupus erythematosus.

We examined the proliferative response to Staphylococcus aureus Cowan 1 (SAC) by enriched peripheral blood B cells from patients with systemic lupus erythematosus (SLE). Responses of B cells from patients with active and inactive SLE were significantly lower than those of B cells from normal individuals. Hyporesponsiveness to SAC was not observed in healthy family members of SLE patients. This hyporesponsiveness did not correlate with prednisolone therapy and could not be attributed to serum factors; it did correlate with the presence of suppressor monocytes. However, we could not exclude the possibility of enhanced sensitivity of SLE B lymphocytes to suppressive signals delivered by the monocytes.

B-Lymphocytes↗

Blocking action of pentobarbital on receptors for excitatory amino acids in the guinea pig hippocampus.

The actions of pentobarbital sodium (Pent) on receptors for glutamate (Glu) and related compounds were studied in thin sections of the guinea pig hippocampus. Depolarizations induced by Glu and quisqualate (Quis) in CA3 neurons were reduced in amplitude during iontophoretic administration of Pent. This action of Pent was not accompanied by any noticeable changes in membrane potential or neuron input resistance. Depolarizations induced by N-methyl-D-aspartate were less sensitive to Pent. The fast kainate (KA) response was as susceptible as the Glu response, whereas the slow KA response was unaffected by Pent in three quarters of the neurons examined. Pent suppressed the Glu response at lower concentrations than required to potentiate responses to gamma-amino butyric acid. Excitatory postsynaptic potentials (EPSPs) elicited by stimulation of mossy fibers were suppressed by Pent. The EPSPs were a little more resistant to Pent than were the Glu responses. These results indicate that Pent blocks receptors for excitatory amino acids in the hippocampus. Of the three different populations of the receptors, Quis receptors are the most sensitive to Pent and KA receptors are the least sensitive. The suppression of the EPSPs is in accordance with the notion that Glu is the transmitter released from mossy fibers.

Amino Acids↗

Inhibitors of high-affinity uptake augment depolarizations of hippocampal neurons induced by glutamate, kainate and related compounds.

Actions of dihydrokainate (DHKA) and 3-hydroxy-DL-aspartate (HAsp), inhibitors of high-affinity uptake for L-glutamate (Glu), were studied in vitro in thin hippocampal slices of the guinea pig. The amplitude of the depolarizations induced by Glu and by L-aspartate (Asp) in CA3 neurons are markedly augmented by DHKA and HAsp. Depolarizations induced by D-homocysteate (DH) were unaffected by the inhibitors. In about half of the neurons, depolarizations induced by L-homocysteate (LH) and by quisqualate (Quis) were slightly augmented by the inhibitors. Fast responses to kainate (KA) were augmented by the inhibitors to a similar extent as were Glu responses whereas slow KA responses were insensitive to HAsp. HAsp was without effect on excitatory postsynaptic potentials elicited by stimulation of granular layer. These findings are in general agreement with the biochemical data on amino acid uptake processes and are also consistent with the slow time-courses of depolarizations induced by DH, LH and Quis. Augmentation of fast KA responses provides strong evidence for the hypothesis that an KA pulse causes a liberation of Glu and/or Asp from the tissue and the liberated amino acid(s) induces the fast KA response in neurons nearby.

Animals↗

Clinical evaluation of computed tomography images in esophageal cancer after submucosal injection of iodized oil.

A submucosal injection of iodized oil (Lipiodol) was administered to patients with esophageal cancer and computed tomography scanning was performed. Infiltration to the surrounding organs, especially the aorta, vertebra, trachea, bronchi, heart, and lymph nodes was examined and the results compared with those from plain computed tomography. Compared with plain computed tomography findings, invasion to the submucosa, adventitia, and surrounding organs was much more clearly demonstrated. This method accurately delineated the oral side of mucosal lesions, which could be useful in establishing a plan for radiotherapy.

Aged↗

Characterization of a human monoclonal antibody to lipopolysaccharides of Pseudomonas aeruginosa serotype 5: a possible candidate as an immunotherapeutic agent for infections with P. aeruginosa.

A human monoclonal antibody, P3D9 (IgG2, lambda type), that bound to Pseudomonas aeruginosa Homma serotype 5 cells with high specificity was produced by cell fusion between a human tonsillar lymphocyte and a mouse plasmacytoma cell, P3-X63-Ag8-U1 (P3U1). The yield of P3D9 secreted into the culture supernatant from the mouse-human hybridoma was 2-10 micrograms/ml, and this hybridoma cell line has been stably producing this antibody for six months. Antibody P3D9 alone did not cause agglutination of serotype 5 cells, but the cells were agglutinated after addition of goat antibody to human IgG. Antibody P3D9 was proven to have protective activity against infection with P. aeruginosa, and the 50% protective dose estimated for experimental peritoneal infection with P. aeruginosa was 2.4 micrograms per mouse.

Agglutination Tests↗

A new common polysaccharide antigen of strains of Pseudomonas aeruginosa detected with a monoclonal antibody.

A monoclonal antibody, E87, that binds to various serotype strains of Pseudomonas aeruginosa was produced by a hybridoma cell line prepared by fusion of mouse plasmacytoma P3-X63-Ag8-U1 with spleen cells of mice immunized with P. aeruginosa strain IFO3080 (serotype M). E87 bound to approximately 80% of the tested strains of various serotypes of P. aeruginosa. The antigen recognized with E87 was found in the lipopolysaccharide and was eluted in void volume fractions of Sephadex G50 column chromatography after acetic acid treatment. This antigen was eluted in the fraction containing substances of lower molecular weight than the O side chain by Sephacryl S-300 column chromatography, and this fraction was found to be the peak fraction of hexose. This antigen was not separated from the O side chain by Sephacryl S-300 column chromatography of untreated lipopolysaccharide. Colorimetric analyses and thin-layer chromatography showed that this antigen consisted mainly of rhamnose and ribose (molar ratio, 10:1).

Acetates↗

HPLC-studies on nonmercapt-mercapt conversion of human serum albumin.

Human mercaptalbumin (HMA) and nonmercaptalbumin (HNA) could be separated by high-performance liquid chromatography (HPLC) at neutral pH. Using HPLC, the present authors found the nonmercapt-mercapt conversion (HNA----HMA) during hemodialysis and the mercapt-nonmercapt conversion (HMA----HNA) after hemodialysis in chronic renal failure, indicating HMA as the covalent carrier protein for sulfur-containing amino acids.

Chromatography, High Pressure Liquid↗