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Biomedical subjects

S Nomiyama

Publications and source records attributed to S Nomiyama.

35 records · Page 2Linked to original sources

Conservative surgery for regional lymphadenectomy in the treatment of early gastric carcinoma.

The relationship between lymph node metastases and postoperative prognosis in 209 patients with early gastric cancer was studied. As to the postoperative prognosis in relation to the extent of lymph nodes dissection, no significant difference was observed among the age-corrected 5-year survival rates following three surgical procedures in patients with early gastric cancer. Age-corrected 5-year survival rates were 0.92 +/- 0.44 R1-resection, 0.95 +/- 0.44 in R2-resection, and 1.00 +/- 0.06 in R3-resection, respectively. In addition, in 71 patients including 33 with early gastric cancer and 38 patients with advanced but relative early gastric carcinoma, the relationship between the immunostatus and postoperative prognosis was investigated. Postoperative age-corrected 5-year survival rate (0.904 +/- 1.153) of the optimal responders with good immunostatus was significantly higher than that (0.582 +/- 1.153) of the suboptimal responders with impaired immunostatus (P less than 0.01). Thus, conservative surgery for regional lymphadenectomy may be an effective procedure for cure of early gastric carcinoma, particularly in cases of a carcinoma limited to the mucosal area of the stomach.

Adult↗

[Follow-up study of preoperative oral administration of an antineoplastic agent as an adjuvant chemotherapy in stomach cancer].

Based on the propensity of fat emulsion to be absorbed mainly into lymphatic capillaries and regional lymph nodes, preoperative oral administration of 5-FU emulsion was attempted as an adjuvant chemotherapy to surgery for gastric carcinoma. In our previous studies, it was demonstrated that the mean 5-FU level in the regional lymph nodes was higher in patients who received the 5-FU solution. Since 1974, we have administered 5-FU emulsion preoperatively to 167 patients with gastric cancer (500 mg X 10 days) and examined histologically the effect of this regimen on the metastatic foci in the lymph nodes. A positive change, such as marked necrosis or marked degeneration, was found in 58% of the metastatic lesions. Sixty-four patients with advanced cancer who received the preoperative 5-FU emulsion also received a curative resection between 1974 to 1977 in addition to postoperative chemotherapy (MMC 40 mg and 5-FU more than 5000 mg) (Group A). Their survival rate was compared with that of the curatively operated advanced cancer patients from 1959 to 1973 who received the same postoperative chemotherapy only (Group B, N = 59) and with that of patients, from 1959 to 1970, who received no chemotherapy (Group C, N = 222). The 5 year survival rate of Group A was 0.53 +/- 0.07, which was higher than that (0.49 +/- 0.07) of Group B and that (0.40 +/- 0.10) of Group C. Comparing the 5-year survival rates of the 3 groups from several points of view, such as a stage of cancer progress absence of serosal invasion, the 5-year survival rate of group A was higher than that of other groups. Although these differences between Group A and B were not statistically significant, but those between Group A and B were significant. From these results it is suggested that preoperative oral 5-FU emulsion might be effective as an adjunct to surgery for gastric cancer.

Administration, Oral↗

Comparative study of G- and D-cell population in the dog stomach.

Since somatostatin is a local hormone controlling gastric acid secretion and gastrin release, quantitative histopological distribution of the G-cells and D-cells in the canine whole stomach was investigated by the specific immunoperoxidase staining technique. The G-cells were identified only in the pyloric antrum and the estimated total number of G-cells was 15.5 X 10(6) cells. Most of the D-cells were also found in the pyloric antrum but a few were found scattered diffusely throughout body and fundus of the stomach. The estimated total number of D-cells was 11 X 10(6) cells in the pyloric antrum and 4 X 10(6) cells in the corpus and fundus. The G-/D-cell ratio in the antrum was 1.4:1. The number of G-cells as well as D-cells per unit mucosal surface area was significantly higher on the greater curvature and the proximal part of the antrum than on other areas of the antrum. Thus, the pattern of distribution in G-cells was similar to that of D-cells and there was a highly significant correlation between G- and D-cells per unit mucosal surface area. It would appear that under normal conditions, the number of G- and D-cells in the antrum are in good balance and may play an important role in the control mechanisms related to gastric secretion.

Animals↗

Indoleamine 2,3-dioxygenase. Purification and some properties.

Indoleamine 2,3-dioxygenase was purified from rabbit small intestine to apparent homogeneity as judged by polyacrylamide gel electrophoresis and analytical ultracentrifugation. The native enzyme was a monomeric protein of a molecular weight of 41,000 +/- 1,000 with an s020,w value of 3.45 S. It had a relative abundance of hydrophobic amino acids such as valine, leucine, and isoleucine, and contained approximately 5% carbohydrate by weight. The estimated content of sugar residues per mol of enzyme was: galactose, 1.2; mannose, 2.6; N-acetylglucosamine, 5.2; and sialic acid, 0.8. One mole of enzyme had 0.8 mol of protoheme IX as a prosthetic group. However, copper was not detected in a significant amount and the ratio of copper to heme was less than 0.03. EPR spectra of the nitric oxide complex of the ferrous enzyme indicated that a nitrogen atom, possibly in an imidazole group, might be coordinated as the fifth ligand of the heme coenzyme. The anisotropic g values were gx = 2.08, gy = 1.98, and gz = 2.01. A single enzyme protein catalyzed the oxygenative ring cleavage of D- and L-tryptophan, D- and L-5-hydroxytryptophan, tryptamine, and serotonin. In addition, the purified enzyme had a peroxidase activity with guaiacol and potassium iodide as hydrogen donors, but not a catalase activity.

Amino Acids↗