Biomedical subjects

T Nishiki

Publications and source records attributed to T Nishiki.

At least 37 records · Page 2Linked to original sources

PubMed1994

[Zonisamide monotherapy against absence attacks: report of two cases].

We report two cases of absence seizures, in which zonisamide monotherapy was effective. In one case the attacks recurred 6 months after the beginning of zonisamide therapy but ceased again with an increase of the dosage. The EEG prior to treatment showed 3 Hz generalized spike-wave patterns and 3 Hz high voltage slow wave burst in the right occipital area in one case, and 3.5-4 Hz generalized spike-wave patterns and focal spike-wave complexes in the left frontal to central areas in the other. One of the generalized spike-wave patterns were preceded by right occipital delta wave burst in one case, and bilateral occipital sharp-wave complex in the other. It is suggested that zonisamide monotherapy may be effective against absence seizures with focal paroxysmal discharges.

Child↗

PubMed1993

Solubilization and characterization of the acceptor for Clostridium botulinum type B neurotoxin from rat brain synaptic membranes.

The acceptor for Clostridium botulinum type B neurotoxin was solubilized from rat brain synaptic membrane with nonionic detergent, nonanoyl-N-methylglucamide (MEGA-9). The solubilized acceptor was assayed for the binding activity by precipitating the acceptor with acetone in the presence of phosphatidylcholine. 125Ilabeled neurotoxin specifically bound to the lipid vesicles having incorporated the acceptor together with gangliosides. The lipid vesicles having incorporated either the acceptor or gangliosides alone showed extremely low binding activity. The treatment of the solubilized acceptor with lysyl endopeptidase and glycopeptidase F but not with sialidase resulted in decreased toxin binding, indicating that the putative acceptor is a glycoprotein accompanying an N-linked carbohydrate moiety. The observations suggest also that a protein acceptor/ganglioside complex may be required to form the functional toxin receptor.

Animals↗

PubMed1993

Treatment of an infant with congenital sodium diarrhea by oral rehydration.

We have been following a male case of congenital sodium diarrhea (CNaD), who had a distended abdomen, passed watery stools with high sodium concentration, and showed metabolic acidosis in the first week of life. He also showed hyponatremia, low urine sodium, high serum aldosterone and high renin activity. Other possible causes of secretory diarrhea were ruled out. The initial effective treatment was oral supplements of water and electrolytes lost in the fecal fluid: with this he gained weight, and hyponatremia and metabolic acidosis were corrected. Loperamide hydrochloride was administered to increase intestinal absorption of sodium, as the serum prostaglandin was high. Watery diarrhea then improved, but as he passed acholic stools, we stopped and postponed the treatment for a while; the stools then became watery again. Although diarrhea has persisted, he has not shown any abnormalities in growth or psychomotor development for the first two years of life.

Alkalosis↗

PubMed1990

ADP-ribosylation of the rho/rac proteins induces growth inhibition, neurite outgrowth and acetylcholine esterase in cultured PC-12 cells.

Botulinum ADP-ribosyltransferase C3 (C3 exoenzyme) was purified to homogeneity and added to cultured rat pheochromocytoma PC-12 cells. Incubation with this exoenzyme caused inhibition of cell growth and induced neurites as well as acetylcholine esterase in these cells. These changes were dependent on the amount of the enzyme added to the culture, which correlated with the in situ ADP-ribosylation of the rho/rac proteins in the cells. Preincubation with a specific anti-C3 exoenzyme monoclonal antibody inhibited both the ADP-ribosyltransferase activity and the neurite-inducing activity of the enzyme preparation. These results suggest that C3 exoenzyme affected the cellular function of the rho/rac proteins by ADP-ribosylation to induce these changes in the cells.

Acetylcholinesterase↗

PubMed1990

Immunochemical identification of the ADP-ribosyltransferase in botulinum C1 neurotoxin as C3 exoenzyme-like molecule.

Botulinum C1 neurotoxin and C3 exoenzyme were purified to apparent homogeneity from the culture filtrate of Clostridium botulinum type C strain 003-9. Both preparations catalyzed ADP-ribosylation of the same substrate, the Mr 22,000 rho gene product (Gb). When the light and heavy chains of C1 toxin were separated, ADP-ribosyltransferase activity in the toxin was quantitatively recovered in the light chain fraction. Anti-C1 toxin antiserum precipitated the ADP-ribosyltransferase activity and the neurotoxicity of C1 toxin in parallel, whereas it had no effect on C3 exoenzyme. On the other hand, anti-C3 exoenzyme antiserum precipitated the ADP-ribosyltransferase activities of both C3 exoenzyme and C1 toxin. This antibody, however, did not precipitate the neurotoxicity of C1 toxin. The ADP-ribosyltransferase in C1 toxin was quantitatively adsorbed onto the anti-C3 antibody column and separated from the majority of C1 toxin protein. The enzyme was then eluted with acidic urea and Western blotting analysis of this eluate revealed the appearance of a protein band positively stained with anti-C3 antibody at a position similar to that of C3 exoenzyme. Quantitative determination by enzyme-linked immunosorbent assay showed that the C3-like immunoreactivity is present in the C1 toxin molecules at the molecular ratio of 1 to 1,000. These results suggest that the ADP-ribosyltransferase activity in C1 toxin is expressed by a C3-like molecule which is present in a small amount in the toxin preparation and appears to bind to the toxin component(s). The above results also indicate that the ADP-ribosyltransferase in C1 toxin is not related to its neurotoxin action.

Antibodies, Bacterial↗

PubMed1990