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Biomedical subjects

T Funada

Publications and source records attributed to T Funada.

15 recordsLinked to original sources
PubMed2004

[Pulmonary metastasis of uterine leiomyosarcoma 8 years after hysterectomy; report of a case].

A 57-year-old woman, who had undergone hysterectomy for uterine leiomyosarcoma 8 years ago, was admitted to our hospital for pulmonary tumors on chest X-ray. Two tumors were recognized on each side at left and right lung field by computed tomography (CT). Two-staged tumor resection was performed by left thoracotomy and by video-assisted thoracoscopic surgery (VATS) in the right. The histologic findings showed that those tumors were metastases of uterine leiomyosarcoma. This case suggests that the long term follow-up is necessary in the case of uterine leiomyosarcoma after operation.

Female↗
PubMed2000

Synthesis of the fatty sterol bound protein for a new sterol antibody.

For the purpose of applying the particular antibodies as a new diagnostic procedure for atherosclerosis and related diseases, we successfully achieved the synthesis of the fatty sterol with a linker, then linked the target protein to this sterol. Synthesis was started from pregnenolone and achieved by the Grignard reaction with pentenyl magnesium bromide, regioselective photoaddition of thiolacetic acid toward the 25-double bond, esterification of 3-OH with linoleic anhydride, in situ conjunction of the cross-linker (MBS) to the thiol group after selective deprotection from its acetyl ester, and finally by the reaction with protein such as KLH or albumin through this linker.

Adjuvants, Immunologic↗
PubMed2000

Effects of chemical modification of carboxyl groups in the hemolytic lectin CEL-III on its hemolytic and carbohydrate-binding activities.

Effects of chemical modification of carboxyl groups in the hemolytic lectin CEL-III on its activities were investigated. When carboxyl groups were modified with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) and glycine methyl ester, hemolytic activity of CEL-III decreased as the EDC concentration increased, accompanied by reduction of oligomerization ability and hemagglutinating activity. However, binding ability of CEL-III for immobilized lactose was retained fairly well after modification, suggesting that one of two carbohydrate-binding sites might be responsible for such inactivation of CEL-III.

Animals↗
PubMed1998

Chemical modification of the hemolytic lectin CEL-III by succinic anhydride: involvement of amino groups in the oligomerization process.

CEL-III is a Ca(2+)-dependent lectin from a marine invertebrate, Cucumaria echinata, which shows strong hemolytic activity toward human and rabbit erythrocytes. After binding to carbohydrate receptors, CEL-III oligomerizes in the erythrocyte membrane to form ion-permeable pores, leading to the colloid osmotic rupture of the cells. Since hemolysis was greatly increased in the alkaline pH, especially above pH 9, involvement of amino groups of CEL-III in its hemolytic activity was evaluated using chemical modification by succinic anhydride. After modification of 7 amino groups per protein molecule, the hemolytic activity of CEL-III was reduced to 23% of the native protein, but hemagglutinating and carbohydrate-binding activities were only slightly affected even after modification of 14 amino groups. A circular dichroism spectrum of modified CEL-III showed almost no change in the secondary structure from that of the native protein, indicating that the decrease of hemolytic activity was not caused by partial unfolding of the protein. Immunoblotting analysis of the erythrocyte membrane treated with modified CEL-III showed a decrease in the formation of CEL-III oligomer in the membrane in parallel with the decrease in hemolytic activity. These results suggest that amino groups of CEL-III are involved in its oligomerization in the cell membrane, and their modification leads to inactivation of the protein without much influence on the carbohydrate-binding activity.

Amino Acids↗
PubMed1991

Changes in fatty acid composition in rat blood and organs after infusion of docosahexaenoic acid ethyl ester.

An infusible emulsion of docosahexaenoic acid ethyl ester (DHA-EE) was prepared. One hundred milliliters of the emulsion contained 10 g DHA-EE (90% pure). Three milliliters of the emulsion was infused into tail veins of 22 Wistar rats weighing approximately 300 g. They were killed 1, 6, and 24 h and 3 and 7 d after the infusion, and fatty acid composition of various organs and plasma was analyzed along with that of control rats. DHA concentrations reached their peaks within 24 h after DHA infusion in plasma lipid fractions and in the phospholipid fraction of liver and lung. DHA did not increase at all in cardiac phospholipid fraction. However, DHA concentrations increased markedly (from 0.7% to 11%) in the free fatty acid fraction of heart 1 h after the infusion. DHA emulsion might be useful for patients in whom a rapid increment in DHA in tissues is beneficial.

Animals↗
PubMed1981

[The computerized display of epicardial mapping (author's transl)].

UNLABELLED: The epicardial mapping is necessary for the surgical treatment of drug-resistant cardiac arrhythmia. The procedure for the epicardial mapping consists of three stages: 1) recording of heart potentials, 2) extraction of excitation transmission time, and 3) display of epicardial mapping. In this paper, our new microcomputer-based system was discussed. It was achieved by this system to simplify the method for the extraction and to make the colorgraphic display of epicardial mapping. Two methods for extraction were used in this study to compare with manual operation: 1) D method; extracting the time, when the differentiated wave takes maximal potential, and 2) Wi method; extracting the time of (Formula: see text). RESULTS: 1) similar epicardial excitation maps were obtained by these computerized methods, and 2) the most approximate values of the transmission time was obtained by Wi (i=2) method.

Computers↗
PubMedDate not supplied

Effects of dietary arginine supplementation on protein turnover and tissue protein synthesis in scald-burn rats.

We assessed the effects of dietary arginine supplementation on protein turnover and organ protein synthesis in burned rats. Male Wistar rats weighing about 200 g underwent catheter jejunostomy and received scald burns covering 30% of the whole-body surface area. Animals were divided into a control group (n = 9) and an arginine group (n = 9) and continuously received total enteral nutrition for 7 d (250 kcal.kg-1.d-1, 1.72 gN.kg-1.d-1). Changes in body weight, plasma total protein, plasma albumin, urinary excretion of polyamines, nitrogen balance, whole-body protein kinetics, and tissue protein synthesis rates were determined. Whole-body protein kinetics and tissue fractional protein synthetic rates (Ks, percent/d) were estimated using a 24-h constant enteral infusion of 15N glycine on the last day. The changes in body weight were not different between the control and arginine groups. The urinary excretion of polyamines was higher in the arginine group than in the control group (P < 0.01). Burned rats enterally fed arginine-supplemented diet yielded significantly greater cumulative and daily nitrogen balance on days 3 and 5 than those fed a control diet (cumulative, P < 0.05; day 3, P < 0.01; day 5, P < 0.01). Whole-body protein turnover rate was significantly elevated in the arginine group as compared to that in the control group (P < 0.05). The Ks of rectus abdominis muscles were significantly increased in the arginine group in comparison to the control group (P < 0.01). We have shown that dietary arginine supplementation improved protein anabolism and attenuated muscle protein catabolism after thermal injury.

Animals↗