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Biomedical subjects

Y Sawabe

Publications and source records attributed to Y Sawabe.

25 records · Page 2Linked to original sources
PubMed1992

[Lobular carcinoma of the male breast--a case report].

Lobular carcinoma of the male breast is very rare, because lobules do not exist in the male mammary gland. Seven cases of lobular carcinoma of the male breast have been reported in Europe and U.S.A., although no case in Japan. We encountered a very rare case of the lobular carcinoma of 74-year-old male breast. Histopathological examinations of both primary tumor and recurrent tumors of the skin led to the diagnosis of lobular carcinoma.

Aged↗
PubMed1991

A new method of hernioplasty for adult groin hernias centering on repair of the transversalis fascia.

A new method of hernioplasty for adult groin hernias centering on repair of the transversalis fascia was assessed by a questionnaire conducted every five years on adult patients who had received the above operation. The efficacy of this method was evaluated in terms of the postoperative quality of life and prevention of recurrence of groin hernias. Over the last 9 years, 834 adult patients with 921 groin hernias, including bilateral lesions, have undergone the above procedure and overall, favorable results were obtained, with only one case of recurrence (0.1 per cent) being reported. Contralateral herniation, which has been often reported following Bassini's or Hatakoshi's method, was found in only one of our patients although the number of patients who complained of pain in the operated region was comparatively high, being 51 cases or 11.4 per cent.

Adult↗
PubMed1985

Interaction of 3,4,3',4'-tetrachlorobiphenyl metabolites formed by cytochrome P-450 in vitro with rat erythrocytes.

Incubation of 14C-labeled 3,4,3',4'-tetrachlorobiphenyl (TCB) with a reconstituted monooxygenase system containing cytochrome P-450 isolated from 3-methylcholanthrene (MC)-treated rats caused an increase in incorporation of radioactivity to added rat erythrocytes and resulted in covalent binding of reactive metabolites to hemoglobin. Both increases in incorporation and covalent binding to the proteins were dependent on incubation time and required cytochrome P-450-linked monooxygenase activity. In the absence of erythrocytes, the reactive TCB metabolites bound to cytochrome P-450, NADPH-cytochrome P-450 reductase, and high-molecular weight aggregates, as determined by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis, whereas inclusion of the cells in the reaction mixture caused marked alkylation of hemoglobin and a decrease in binding to the electron transfer proteins. Several metabolites other than protein-bound metabolites were detected by thin-layer chromatography; some were found to be incorporated into the erythrocytes while others were not. These results suggest that several TCB metabolites formed by cytochrome P-450 can interact with rat erythrocytes in vitro, and that these interactions may be responsible for the persistence of TCB metabolites in blood observed in vivo.

Animals↗
PubMed1984

Comparative studies on distribution and covalent tissue binding of 2,4,2',4'- and 3,4,3',4'-tetrachlorobiphenyl isomers in the rat.

The 14C-labeled tetrachlorobiphenyl (TCB) isomers 2,4,2',4'-tetrachlorobiphenyl (2,4,2',4'-TCB) and 3,4,3',4'-tetrachlorobiphenyl (3,4,3'4'-TCB) were administered orally to rats, and distribution and covalent binding were measured in several organs. Marked differences in distribution and covalent binding of the two TCBs were observed. The accumulation and retention of 2,4,2',4'-TCB in adipose tissue were much higher than those of 3,4,3',4'-TCB, although the level of radioactivity in the blood was consistently higher in 3,4,3',4'-TCB treated rats. The radioactivity bound in covalent linkages with cellular macromolecules in several tissues was also measured. The data obtained indicated that covalent binding was higher in 3,4,3',4'-TCB treated rats than in those treated with 2,4,2',4'-TCB, particularly in liver and blood components. These results suggest that the two TCB isomers have different pharmacokinetic properties in rats, and the association of covalent binding with 3,4,3',4'-TCB-induced toxicities might be important. In addition, we found that repeated oral dosing with the two TCB isomers caused an increase in in vitro liver microsomal generation of reactive metabolites of TCBs, indicating that the microsomal enzyme system is likely to play an important role in the in vivo covalent binding of TCB.

Animals↗
PubMed1983

Activation of 3,4,3',4'-tetrachlorobiphenyl to protein-bound metabolites by rat liver microsomal cytochrome P-448-containing monooxygenase system.

The specificity of two major types of cytochrome P-450 of rat liver microsomes induced by phenobarbital (PB) and 3-methylcholanthrene (MC) toward activation of three 14C-labeled tetrachlorobiphenyl (TCB) isomers to protein-bound metabolites was examined by intact microsomal and reconstituted monooxygenase systems. The monooxygenase system containing PB-inducible form(s) of cytochrome P-450 was much more active than those inducible by MC in activating two TCB isomers, i.e., 2,4,2',5'-[14C]TCB, for the binding reaction. However, the binding of 3,4,3',4'-[14C]TCB was catalyzed most actively by the system containing a MC-inducible (P-448 type) cytochrome P-450 from rat liver microsomes. Thus two forms of cytochrome P-450 had different substrate specificities for the metabolism of TCB. In another series of experiments, the site of protein molecule bound to TCB metabolites was examined by the cytochrome P-448-containing reconstituted system with 3,4,3',4'-[14C]TCB as substrate. The following lines of evidence supported the hypothesis that the active metabolites of TCB bind covalently to cysteine residues of protein molecules a) TCB-binding activity was strongly inhibited by thiol compounds such as cysteine and glutathione and b) of the various kinds of proteins tested as target for TCB metabolites, only those which contained free sulfhydryl groups on the protein molecule were radiolabeled. Moreover, we found that during the metabolism of 3,4,3',4'-TCB, the heme content of the reconstituted system was lowered, probably reflecting the alkylation of the sulfhydryl groups in the active sites of cytochrome P-448.

Animals↗