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Biomedical subjects

S Oda

Publications and source records attributed to S Oda.

At least 487 records · Page 27Linked to original sources
PubMed1982

[Pre-operative chemotherapy of stomach cancer combined with local administration of OK-432--evaluation of macroscopic results].

We have developed OMF treatment which is consisting of endoscopical injection of OK-432 into the perilesional area of cancer, intraarterial or intravenous injection of mitomycin C by one shot and oral administration of 5-FU, and applied it to the patients with preoperative gastric cancer to whom remarkable macroscopic effects were obtained. We determined its efficacy by establishing a response criteria. Although there were no excellent results, the clinical results were rated as good in 5 lesions (50%) and as fair in 5 lesions (50%) out of 10 lesions in 9 cases. In none of the cases, the treatment was ineffective.

Aged↗
PubMed1980

Effects of actin and calcium ion on chymotryptic digestion of skeletal myosin and their implications to the function of light chains.

Experiments have been carried out to assess the involvement of the myosin light chains [obtained by treatment of myosin with 5,5'-dithiobis(2-nitrobenzoic acid) (Nbs2)] in the control of cross-bridge movement and actomyosin interactions. Chymotryptic digestions of myosin, actomyosin, and myofibrils do not detect any Ca2+-induced change in the subfragment 2 region of myosin. Actin, like Ca2+, protects the in situ Nbs2 light chains from proteolysis and causes a partial switch in the digestion product of myosin from subfragment 1 to heavy meromyosin. This effect is independent of the state of aggregation of myosin, and it persists in acto heavy meromyosin and in actinomyosin in 0.6 M NaCl. Digestions and sedimentation studies indicate that there is no direct acto light chain interaction. Proteolysis of myosin shows a gradual transition from production of heavy meromyosin to subfragment 1 with lowering of the salt level. In the presence of Ca2+ heavy meromyosin is generated both in digestions of polymeric and of monomeric myosin. These results are explained in terms of localized changes within the Nbs2 light chains and subfragment 1. Subunit interactions in the myosin head lead to a Ca2+-induced reduction in the affinity of heavy meromyosin for actin in the presence of MgATP. The resulting Ca2+ inhibition of the actin-activated ATPase of myosin can be detected at high salt concentrations(75 mM KCl).

Actins↗
PubMed1980

Polydactyly Nagoya, Pdn: A new mutant gene in the mouse.

A new hereditary polydactyly (gene symbol Pdn) was found in the course of breeding JCL : ICR mice. The genetic analysis indicated that the polydactyly was an autosomal dominant trait. The homozygotes died within two days after birth. The homozygous fetuses or newborn had 1-3 extra-digits both in te fore- and hindlimbs on the preaxial side. They occasionally showed exencephaly, cleft palate, open eyelid, short tibia and fibula or deformed sternum. The heterozygotes had one extra-digit preaxial side. They occasionally showed exencephaly, heterozygotes had one extra-digit preaxially in the hindlimb and an enlarged first digit on the forelimb which often showed bifurcated distal phalanx. A tab on the postaxial side of the forelimb was found in all homozygotes and in some heterozygotes.

Animals↗
PubMed1980

Evaluation of femoral neck fracture healing in man by serial 99mTc-diphosphonate scintimetry.

99mTc-diphosphonate uptake was measured in thirty-four patients with intracapsular fractures of femoral neck and in sixteen patients with trochanteric fractures during their healing process. A peak value in count ratio was recorded in all patients 4 to 6 weeks after fractures. Fifty patients were classified into a normal healing group and a delayed or non-union group. Namely, 99mTc-diphosphonate uptake was significantly higher in the delayed or non-union group than in the normal healing union group 10 weeks after injury. The application of 99mTc-diphosphonate scintimetry seems to make it possible to differentiate objectively the normal healing union from the delayed or non-union.

Adult↗