Search PubMed⌕ Search

Biomedical subjects

M Tsuda

Publications and source records attributed to M Tsuda.

At least 469 records · Page 26Linked to original sources
PubMed1988

[Management of short bowel syndrome in infants--experience of adjunctive surgical therapy in three cases].

During the past nine years period, we managed 7 cases with short bowel syndrome resulting from massive intestinal resection in the neonatal period. Six children, aged 2 to 8 years are alive, and one died from cardiomyopathy caused by selenium deficiency at the age of one year. The carbohydrate-free milk was used for initial enteral nutrition, and the result was encouraging in 4 cases. In 3 cases in which residual small bowel varied between 6.5 to 18 cm, the enteral feeding was not incapable. These cases underwent adjunctive surgical therapy. Tailoring jejunoplasty was performed in the first case, and bowel lengthening in the second case. In both cases enteral nutrition was advanced postoperatively. The third patient who had rapid intestinal transit time underwent isoperistaltic colon interposition. Intestinal transit time was increased and enteral nutrition was advanced gradually.

Child↗
PubMed1988

Quantitation of beta-tubulin mRNA in mouse brain by RNA-RNA hybridization kinetics with single-stranded riboprobes.

A quantitative procedure involving RNA-RNA hybridization kinetics was developed for measurement of specific mRNA accumulated in particular tissues and cells. Two types of riboprobes for quantitating mouse beta-tubulin mRNA were prepared; one was a truncated RNA covering only the coding portion of beta-tubulin cDNA and the other was a non-truncated RNA covering the vector portion as well as the coding portion. These antisense RNAs were hybridized with the mouse brain RNA, yielding heat-stable hybrids. The truncated and non-truncated antisense RNA probes showed similar hybridization kinetics. Hybridization of the sense RNA, consisting of the beta-tubulin coding portion, with the antisense RNA probe gave standards for determining the proportion of beta-tubulin mRNA in total brain RNA. By this method, the amounts of beta-tubulin mRNA included in the brains of mice of 10 and 50 days old were quantitated.

Animals↗
PubMed1988

Effect of alpha-1-antichymotrypsin on activity of DNA primase isolated from human stomach adenocarcinoma cells.

This paper describes an investigation into the effect of alpha-1-antichymotrypsin (ACT) on DNA primase. DNA primase was partially purified from human stomach carcinoma cells. It was found that poly(dC)-dependent DNa primase activity was inhibited by ACT and the inhibition was proportional to the concentration of the inhibitor. The inhibitory effect of ACT remained even after ACT lost most of its chymotrypsin-inhibitory activity by heat treatment. Poly(dT)-dependent primase activity was enhanced by the presence of ACT. The enhancement was effective up to a concentration of 1mg/ml.

Adenocarcinoma↗
PubMed1988

Incorporation of alpha-1-antichymotrypsin into human stomach adenocarcinoma cell nuclei and inhibition of DNA primase activity.

Incorporation of alpha-1-antichymotrypsin (ACT) into human stomach adenocarcinoma cell nuclei and the effect of ACT on DNA primase from the same carcinoma cells were studied. ACT or [125I]-ACT were observed in carcinoma cell nuclei and high specific radioactivity was detected in washed nuclear fraction when 0.4 mg of ACT or [125I] ACT (8 x 10(7) cpm) was intravenously injected into carcinoma bearing nude mice 2 h before killing. The molecular weight of radioactivity presented in cell nuclei was same as the intact ACT on SDS-polyacrylamide gel electrophoresis. ACT inhibited DNA primase activity and this inhibiting activity was stable than its chymotrypsin inhibiting activity. The results presented here show ACT is incorporated into carcinoma cell nuclei without modification of its molecular weight and may inhibit DNA primase activity.

Adenocarcinoma↗
PubMed1988

Inhibition of DNA synthesis by alpha-1-antichymotrypsin.

The effect of alpha-1-antichymotrypsin (ACT), which is known as an efficient serum protease inhibitor and is detected in tumor cell nuclei, on DNA synthesis was studied. ACT inhibited the activity of DNA polymerase alpha purified from human stomach adenocarcinoma. Other human serum proteins including serum albumin, alpha-1-acidglycoprotein, alpha-1-antitrypsin, and immunoglobulin G, as well as other protease inhibitors, such as leupeptin, pepstatin, PMSF and chymostatin, did not affect the activity of DNA polymerase alpha. It was therefore concluded that the inhibitory action of ACT on DNA polymerase alpha was direct phenomenon unrelated to its protease inhibitory activity. Furthermore, the effect of ACT on DNA synthesis was also studied using lysolecithin-permeabilized cultured human stomach carcinoma cells. ACT added in the medium inhibited DNA synthesis and the degree of inhibition depended on incubation time. It was proportional to ACT concentration and the concentration of ACT required for 50% inhibition was 0.8 mg/ml.

Adenocarcinoma↗
PubMed1987

Properties of a Na+-coupled serine-threonine transport system in Escherichia coli.

Based on the following experimental results we conclude that the serine-threonine transport system in Escherichia coli is a Na+-coupled cotransport system. (1) Addition of serine to cell suspensions induced H+ efflux in the presence of Na+. (2) Addition of serine to cell suspensions induced Na+ uptake by cells. (3) Imposition of an artificial electrochemical potential of Na+ in starved cells induced serine uptake. Some of these phenomena were observed when threonine was added instead of serine or inhibited when cells were preincubated with threonine. The Na+/serine (threonine) cotransport system was considerably repressed when cells were grown on a mixture of amino acids. Serine transport in cells grown in the absence of amino acids mixture was stimulated by Na+. The half maximum concentration of Na+ was 21 microM. Sodium ion increased the Vmax of serine transport without affecting the Km.

Amino Acid Transport Systems↗
PubMed1987

Na+/adenosine co-transport in Vibrio parahaemolyticus.

Adenosine transport in Vibrio parahaemolyticus was studied. Na+ greatly stimulated adenosine uptake. Addition of adenosine to a cell suspension under anaerobic conditions elicited Na+ uptake, and the Na+ uptake was inhibited by monensin, an Na+ ionophore. Imposition of an electrochemical potential of Na+ or a membrane potential in energy-depleted cells elicited adenosine uptake. Therefore, adenosine transport in this organism was concluded to proceed by an Na+/adenosine co-transport mechanism. The Na+/adenosine co-transport system was induced when cells were grown in the presence of adenosine, and repressed by glucose. Although Na+ uptake elicited by adenosine was reduced by glucose, it was enhanced by methyl alpha-glucoside, which reduced the intracellular ATP level. Thus, the effects of glucose and the glucoside on the Na+/adenosine co-transport system did not seem to be due to inducer exclusion, but to be related to the intracellular ATP level.

Adenosine↗
PubMed1987

Resonance Raman spectroscopy of octopus rhodopsin and its photoproducts.

We report here the resonance Raman spectra of octopus rhodopsin and its photoproducts, bathorhodopsin and acid metarhodopsin. These studies were undertaken in order to make comparisons with the well-studied bovine pigments, so as to understand the similarities and the differences in pigment structure and photochemical processes between vertebrates and invertebrates. The flow method was used to obtain the Raman spectrum of rhodopsin at 13 degrees C. The bathorhodopsin spectrum was obtained by computer subtraction of the spectra containing different photostationary mixtures of rhodopsin, isorhodopsin, hypsorhodopsin, and bathorhodopsin, obtained at 12 K using the pump-probe technique and from measurements at 80 K. Like their bovine counterparts, the Schiff base vibrational mode appears at approximately 1660 cm-1 in octopus rhodopsin and the photoproducts, bathorhodopsin and acid metarhodopsin, suggesting a protonated Schiff base linkage between the chromophore and the protein. Differences between the Raman spectra of octopus rhodopsin and bathorhodopsin indicate that the formation of bathorhodopsin is associated with chromophore isomerization. This inference is substantiated by the chromophore chemical extraction data which show that, like the bovine system, octopus rhodopsin is an 11-cis pigment, while the photoproducts contain an all-trans pigment, in agreement with previous work. The octopus rhodopsin and bathorhodopsin spectra show marked differences from their bovine counterparts in other respects, however. The differences are most dramatic in the structure-sensitive fingerprint and the HOOP regions. Thus, it appears that although the two species differ in the specific nature of the chromophore-protein interactions, the general process of visual transduction is the same.

Animals↗
PubMed1987

Isolation and properties of a mutant of Escherichia coli possessing defective Na+/H+ antiporter.

A mutant of Escherichia coli with defective Na+/H+ antiporter was isolated. The rationale for its isolation was that cells possessing defective Na+/H+ antiporter, which is essential for establishment of a Na+ gradient, could not grow with a carbon source that was taken up with Na+. The mutant had no appreciable Na+/H+ antiporter activity, but its K+/H+ antiporter and Ca2+/H+ antiporter activities were normal. Judging from the reversion frequency, the defect seems to be due to a single mutation. The mutant could not grow at alkaline pH. Therefore, the Na+/H+ antiporter, but not the K+/H+ antiporter or the Ca2+/H+ antiporter, seems to be responsible for pH regulation in alkaline medium. This mutant will be useful for cloning the Na+/H+ antiporter gene and for detection of Na+-substrate cotransport systems.

Carrier Proteins↗
PubMed1987

A novel mechanism for utilization of extracellular AMP in Vibrio parahaemolyticus.

Vibrio parahaemolyticus could grow with AMP, ADP or ATP as the sole source of carbon. In the presence of Cl-, a membrane-bound Cl(-)-dependent 5'-nucleotidase seemed to hydrolyze the nucleotides extracellularly, and then the cells took up the resulting adenosine. In the absence of Cl-, although no significant dephosphorylation of the nucleotides occurred, the cells could still grow with AMP, but not with ADP or ATP. Moreover, in the presence of Cl-, Zn2+ inhibited the 5'-nucleotidase, and inhibited growth of the cells with ADP or ATP, but not with AMP, as the carbon source. V. parahaemolyticus was unable to grow with adenine or ribose 5-phosphate. These results suggested that the cells might have an AMP transport system. In fact, Na+ uptake was observed on addition of AMP to a cell suspension in the absence of Cl-, indicating Na+-AMP cotransport.

5'-Nucleotidase↗
PubMed1987

Effect of alpha-1-antichymotrypsin on DNA synthesis in permeabilized human cells.

The effect of Alpha-1-antichymotrypsin(ACT) on DNA synthesis was studied using lysolecithin-permeabilized cultured human stomach carcinoma cells. ACT added in medium inhibited DNA synthesis and the degree of inhibition is incubation time dependent. It is proportional to ACT concentration and the concentration of ACT required for 50% inhibition was 0.8 mg/ml.

Adenocarcinoma↗
PubMed1987

Genetic analysis of a transposon carrying toluene degrading genes on a TOL plasmid pWW0.

Toluene degrading (xyl) genes on a Pseudomonas TOL plasmid pWW0 are located within a 39-kb DNA portion. The 56-kb region including these xyl genes and its 17-kb derivative with a deletion of the internal 39-kb portion transposed to various sites on target replicons such as pACYC184 and R388 in Escherichia coli recA strains. Thus the 56- and 17-kb regions were designated Tn4651 and Tn4652, respectively. Genetic analysis of Tn4652 demonstrated that its transposition occurs by a two-step process, namely, cointegrate formation and its subsequent resolution. The presence in cis of DNA sequences of no more than 150 bp at both ends of Tn4652 was prerequisite for cointegrate formation, and this step was mediated by a trans-acting factor, transposase, which was encoded in a 3.0-kb segment at one end of the transposon. Cointegrate resolution took place site-specifically within a 200-bp fragment, which was situated 10 kb away from the transposase gene. Based on the stability of cointegrates formed by various mini-Tn4652 derivatives, it was shown that the cointegrate resolution requires two trans-acting factors encoded within 1.0- and 1.2-kb fragments that encompass the recombination site involved in the resolution.

Chromosome Deletion↗