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Biomedical subjects

M Noda

Publications and source records attributed to M Noda.

At least 559 records · Page 31Linked to original sources
PubMed1988

[Esophageal cancer developing 13 years after radiotherapy of lung cancer].

This paper reports on an autopsied case manifesting an esophageal cancer that had developed 13 years after radiotherapy for lung cancer. The patient was a 61-year-old man. He was found to have a squamous cell carcinoma of the right lower bronchus with a swelling of the mediastinal and left supraclavicular lymph nodes in July of 1973. He received 60 Gy of irradiation in the right lung, the mediastinum, and the left supraclavicular region. Later, after doing well until August of 1986, a squamous cell carcinoma of the esophagus was found at the upper intrathoracic site. Thus, he also received additional radiotherapy but died of pneumonia after this local recurrence 7 months later. At autopsy, no local recurrence of the primary lung cancer was found. The site of esophageal cancer was far from that of the primary lung cancer though it was included in the previous treatment ports. This suggests the possibility that the primary esophageal cancer had been induced by therapeutic irradiation. So far as we know, this is the first report of esophageal cancer that may have developed after irradiation for lung cancer.

Aged↗
PubMed1987

Screening of volatile compounds present in human blood using retention indices in gas chromatography.

The retention index in gas chromatography was introduced to screen volatile compounds in blood. Sixty-one organic compounds with high volatility were determined using a gas chromatograph with a flame ionization detector and a packed column system with 10% OV-17. Porapak P was used as a supplementary column for determining alcohol. Detection limits were determined for several substances. This method was used to analyse blood samples obtained at autopsy from patients suspected of solvent abuse. This approach proved to be superior to conventional gas chromatography in that mixed unknown volatiles in the blood could be identified simply and rapidly.

Adult↗
PubMed1987

Alteration by v-Ki-ras in NaF, cholera toxin and forskolin-induced adenylate cyclase activation in NIH/3T3 fibroblast cells.

It has been suggested that ras proteins are involved in the transmembrane signaling mechanism and they share structural features with GTP-binding proteins. To identify the role of ras oncogene and it's products in the coupling mechanisms of GTP-binding proteins to adenylate cyclase, we examined effect of NaF, cholera toxin and forskolin in normal and v-Ki-ras transformed NIH/3T3 fibroblast cells. In transformants, adenylate cyclase activity was markedly enhanced by NaF and cholera toxin, in contrast to normal cells. It is suggested that ras oncogene proteins plays enhancing role in coupling of GTP-binding proteins to adenylate cyclase.

Adenylyl Cyclases↗
PubMed1987

Histamine increases the Ca current in guinea-pig ventricular myocytes.

Histamine prolonged the action potential duration and shifted the plateau in an upward direction in guinea-pig ventricular myocytes. Whole cell voltage clamp experiments revealed that histamine increases the amplitude of the inward Ca current with a slight increase in the outward current. Cimetidine but not mepyramine inhibited the effects of histamine. We suggest that histamine increases the Ca current via the mediation of the H2-receptors.

Action Potentials↗
PubMed1987

A new diet-exercise therapy in our obese-child clinic.

Because a large percentage of childhood obesity may persist into adulthood and cause a hotbed of so-called seijin-byoh (adult diseases), its treatment should also be considered from the viewpoint of seijin-byoh prophylaxis. Most obese children, however, are awkward in their movements, in spite of binge eating or bulimia, and unable to carry out any severe exercise-diet therapy. For such subjects, we have designed a new practicable procedure, and obtained excellent results for the last five years. The main principle of our procedure is that the control of caloric intake is relaxed as much as possible after due consideration of a child's growth in height: no restriction for mild, 10-15% of the requirement for moderate, and 20-25% for severe obese children, respectively. The ratio of protein/energy is established at a higher level than usual, while that of fat/energy at a lower level. For exercise, walking is the most easy and important exercise and the proper speeds for individuals are converted from the same amount of movement determined at the 1st increase point of serum lactate values, where the proportion of movement-energy originating from body fat reaches the highest percentage at about 75%. Our new procedure is supported also by the fact that the reduction in body weight combines with the improvement in measurement values of fatty metabolites without any change in values of proteins.

Adolescent↗
PubMed1987

cDNA cloning of alkaline phosphatase from rat osteosarcoma (ROS 17/2.8) cells.

Two cDNA clones of rat alkaline phosphatase (AP) were isolated from a rat osteosarcoma lambda gt 11 cDNA library (ROS 17/2.8) utilizing a human bone-liver-kidney (BLK) type AP cDNA. These clones contain overlapping DNA sequences of 597 and 520 bp, respectively, corresponding to the 3' noncoding region of AP mRNA. The sequence homology with the human BLK AP cDNA is 61%. In Northern blot analysis the rat cDNA hybridizes to a single band of 2.5 kb mRNA from ROS 17/2.8 and rat liver, under highly stringent conditions. Steady state levels of AP mRNAs measured in several rat osteosarcoma cell lines (ROS 17/2.8, ROS 2/3, ROS 25/1, UMR 106) correlate with the level of AP enzymatic activity in these cells. Dexamethasone, which stimulates AP enzymatic activity in ROS 17/2.8 cells, increases the relative abundance of AP mRNA in a dose-dependent manner. This probe can be used to study AP expression in rat tissues and cells.

Alkaline Phosphatase↗
PubMed1987

Type beta transforming growth factor (TGF beta) regulation of alkaline phosphatase expression and other phenotype-related mRNAs in osteoblastic rat osteosarcoma cells.

TGF beta 1 from porcine platelets increased alkaline phosphatase (AP) activity in the rat osteoblastic cell line ROS 17/2.8 about three-fold. This effect was dose-dependent with an ED50 of about approximately 0.2 ng/ml and was larger during logarithmic growth than at confluence. TGF beta 1 inhibited cell growth by about 30% with similar dose dependence. Thirty min exposure to TGF beta 1 was sufficient to increase AP activity 3 days later by about two-fold but did not affect cell growth, suggesting dissociation between effects on proliferation and differentiation. The rise in AP activity started 6 h after TGF beta 1 addition and was blocked by cycloheximide and actinomycin D. TGF beta 1 also increased AP mRNA by two- to three-fold and this effect was not blocked by cycloheximide. The half-life of AP mRNA, estimated following the addition of 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole was about ten h in both control and TGF beta 1-treated cells. The mRNAs for type I procollagen and osteonectin were also increased by TGF beta 1 but fibronectin mRNA was decreased. TGF beta 2 effects on AP and cell growth were similar to those of TGF beta 1, except for lack of activity following transient exposure. At saturating concentrations, TGF beta 2 (2 ng/ml) or dexamethasone (10(-7) M), which has similar effects on these cells, did not further augment the effects of TGF beta 1 (at 2 ng/ml). Above findings suggest that TGF beta promotes osteoblastic differentiation in rat osteosarcoma cells at least in part by acting at the pretranslational level.

Alkaline Phosphatase↗
PubMed1987

Effect of electric currents on DNA synthesis in rat osteosarcoma cells: dependence on conditions that influence cell growth.

Effects of sinusoidal 60-Hz electric currents on DNA synthesis in rat osteosarcoma cell (ROS 17/2.8) in culture were investigated using agar electrodes. This exposure system eliminates electrochemical effects at electrode surfaces, minimizes the contribution of magnetic fields and produces no detectable temperature changes (less than +/- 0.1 degrees C) at current densities of up to 1,500 microA r.m.s. (root mean square)/cm2. Thirty-four hours exposure to electric current at intensities of 300-400 microA r.m.s./cm2 enhanced DNA synthesis by 20% relative to controls. The effect depended on serum concentration, cell seeding density, and the age of the cell population at the time of seeding: effects were seen at 0.2% fetal bovine serum, in cells seeded 4 days after previous passage, at 20,000 cells/cm2. These findings indicate that sinusoidal electric currents can midly enhance DNA synthesis in these cells under growth-limiting conditions.

Animals↗
PubMed1987

Patch clamp characterization of sodium channels expressed from rat brain cDNA.

Sodium currents, INa, were recorded from Xenopus laevis oocytes which had been injected with mRNA synthesized by in vitro transcription of the rat brain sodium channel II cDNA (Noda et al. 1986 a, b). Patch pipettes were used to apply depolarizing voltage steps and to record macroscopic sodium currents of between 50 and 750 pA from cell-attached patches of the oocyte membrane. With a combination of whole-cell and patch clamp recording, the properties of the implanted sodium channels could be studied in detail. They were analyzed according to the model of Hodgkin and Huxley (1952 a) assuming three activation gates. The activation of the sodium currents is characterized by an equilibrium potential of -29 mV and an apparent gating charge of 8.7 e0. At -64 mV half of the sodium currents were inactivated. From single-channel current recordings, an elementary sodium channel conductance of 19 pS and an average open time of 0.43 ms were obtained at -32 mV membrane potential and 16 degrees C. The single-channel and activation properties of rat brain sodium channel II are therefore comparable to those found in peripheral nerve and skeletal muscle, but inactivation occurs at less negative potentials. This could be a specific property of the brain sodium channels and may underlie the maintained inward sodium currents reported in brain neurones (French and Gage 1985).

Animals↗
PubMed1987

Hemagglutination with transmissible gastroenteritis virus.

Transmissible gastroenteritis virus grown in primary swine kidney cell cultures agglutinated erythrocytes from chicken, guinea pig and cattle but not erythrocytes from mouse and goose. The optimal incubation temperature was at 4 degrees C. The hemagglutination (HA) reaction was inhibited by specific antiserum. Some factors involved in the HA and HA-inhibition (HI) were investigated and standard HA and HI tests were established. HI antibody titers of individual pig sera showed a significant positive correlation with their neutralizing antibody titers.

Animals↗
PubMed1987

Purification and some properties of Shiga-like toxin from Escherichia coli O157:H7 that is immunologically identical to Shiga toxin.

A cytotoxin to Vero cells (Shiga-like toxin), which was neutralized by antibody against purified Shiga toxin produced by Shigella dysenteriae 1, was purified from Escherichia coli O157:H7, isolated from a patient with hemorrhagic colitis. The purification procedure consisted of ammonium sulfate fractionation, DEAE-cellulose column chromatography, chromatofocusing column chromatography and high performance liquid chromatography. About 200 micrograms of purified Shiga-like toxin was obtained from cell extracts of 14 liters of culture with a yield of about 15%. The purified Shiga-like toxin showed identical physicochemical, biological and immunological properties to those of Shiga toxin. Purified Shiga-like toxin and Shiga toxin also had the same mobilities on polyacrylamide disc gel electrophoresis and polyacrylamide gel isoelectrofocusing. On sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis, purified Shiga-like toxin migrated as two bands corresponding to the A and B subunits, and these migrated to the same positions as A and B subunits of Shiga toxin. The amino acid composition of the purified Shiga-like toxin was also similar to that of Shiga toxin. The purified Shiga-like toxin showed various biological activities: lethal toxicity to mice when injected intraperitoneally, the LD50 being 30 ng per mouse; cytotoxicity to Vero cells, killing about 50% of the cells at 6 pg; and fluid accumulation in rabbit ileal loops at concentrations of more than 1.25 micrograms/loop. These values are comparable with those obtained with Shiga toxin. In an Ouchterlony double gel diffusion test, the lines formed by the purified Shiga-like toxin and Shiga toxin fused, indicating that the two toxins were immunologically identical.

Amino Acids↗
PubMed1987

Enhancement of choleragen ADP-ribosyltransferase activities by guanyl nucleotides and a 19-kDa membrane protein.

Choleragen activates adenylate cyclase by catalyzing, in the presence of NAD, the ADP-ribosylation of Gs alpha, the stimulatory guanyl nucleotide-binding protein of the cyclase system. Kahn and Gilman [Kahn, R. A. & Gilman, A. G. (1986) J. Biol. Chem. 261, 7906-7911] identified another guanyl nucleotide-binding protein termed ADP-ribosylation factor (ARF) that stimulated this reaction. It was proposed that the toxin substrate is an ARF-Gs alpha complex and that ARF may have a physiological role in regulation of Gs alpha activity. We have found that purified ARF from bovine brain enhances not only the ADP-ribosylation of Gs alpha but also Gs alpha-independent choleragen-catalyzed reactions. These are (i) ADP-ribosylation of agmatine, a low molecular weight guanidino compound; (ii) ADP-ribosylation of several proteins unrelated to Gs alpha; and (iii) auto-ADP-ribosylation of the toxin A1 peptide. These reactions, as well as the ADP-ribosylation of ARF itself, were stimulated by GTP or stable GTP analogues such as guanyl-5'-yl imido-beta gamma-diphosphate and guanosine 5'-O-[gamma-thio]triphosphate; GDP and guanosine 5'-O-[beta-thio]diphosphate were inactive. These observations are consistent with the conclusion that ARF interacts directly with the A subunit of choleragen in a GTP-dependent fashion thereby enhancing catalytic activity manifest as transfer of ADP-ribose to Gs alpha and other proteins, to the toxin A1 peptide, or to agmatine. It is tempting to speculate that ARF may be involved in regulating one or another of the ADP-ribosyltransferases found in animal cells.

ADP Ribose Transferases↗