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Biomedical subjects

J Shimazaki

Publications and source records attributed to J Shimazaki.

At least 433 records · Page 24Linked to original sources
PubMed1982

Internal spermatic vein prostaglandins in varicocele patients.

Blood was collected from 20 patients with varicocele (15 in the infertile group and 5 in the incidental varicocele group) at the time of high ligation by insertion of a catheter into the internal spermatic vein toward the renal side. Simultaneously, blood was obtained from the antecubital vein. The levels of cortisol, prostaglandin (PG)(A + B), PGE, and PGF in these blood samples were measured. Although no differences in cortisol and PG(A + B) levels were observed between internal spermatic and peripheral vein bloods in varicocele patients examined, PGE and PGF levels were higher in internal spermatic venous bloods than in peripheral venous bloods. Differences in PGF levels between the samples of blood from the internal spermatic vein and from the peripheral vein in cases of the infertile group were larger than those of the incidental varicocele group. PGE and PGF in internal spermatic vein blood samples were correlated. The possibility that PGE and PGF, refluxed from the renal vein to the testes via the internal spermatic vein in varicocele patients, disturbs spermatogenesis is discussed.

Adult↗
PubMed1982

Low molecular weight component of androgen receptor in cytosols from benign hypertrophic human prostate treated with high KCl solution.

Cytosol of the benign hypertrophic human prostate was prepared in a low salt medium and then the concentration of salt was increased to 0.4 M with KCl (0.4 M KCl-cytosol). This preparation showed a high affinity binding to R 1881 and the binding was specific for androgens. These results suggest that the binding of the preparation to R 1881 was due mainly to the cytosolic androgen receptor. The R 1881 binding component in the 0.4 M KCl-cytosol was sedimented at 3S by sucrose density gradient centrifugation. The small sedimentation coefficient of the binder seems to be due to the high concentration of salt and not to degradation by proteolytic enzymes in the preparation. The molecular weight, Stokes radius and frictional ratio of this binding component were 32,000, 25.9 A and 1.24, respectively.

Cytosol↗
PubMed1981

Androphilic proteins in the human prostate.

Dihydrotestosterone-binding protein in cytosols from human prostates was different from the R1881- and R5020-binding proteins. The R1881- and R5020-binding proteins in the cytosol were very similar and most of the binding sites for R1881 were capable of binding R5020. However, nuclear extracts showed equal binding to dihydrotestosterone and R1881, but not to R5020, suggesting that there might not be a progestin receptor in the human prostate. Maximum binding sites to dihydrotestosterone, R1881, and R5020 in cytosols were very similar among "normal" and pathological prostates except that dihydrotestosterone binding was higher in "normal" prostates than in the pathological ones. Histochemically, R1881-binding was observed in the epithelial cells and in malignant cells, but not in the stroma.

Androgen-Binding Protein↗
PubMed1981

Binding of dihydrotestosterone, R 1881 and R 5020 in cytosols from normal, benign hypertrophic and cancerous human prostates.

The binding of dihydrotestosterone, R 1881 and R 5020 was examined in cytosols of normal, benign hypertrophic and cancerous tissues of the human prostates. Almost all samples obtained by open operation showed high affinity binding to these ligands. Dissociation constants of the binding to these ligands were approximately 10(-9) M irrespective of the pathological state of the prostates. Maximum binding sites for dihydrotestosterone seemed to be greater in normal tissues than in the pathological ones. However, maximum binding sites for R 1881 and R 5020 were not significantly different among the normal and pathological prostates examined in the present study. Moreover, some correlation was observed between the maximum binding sites for R 1881 and those for R 5020. The samples resected by TUR seemed to be inadequate for analyses of androgen binding.

Cytosol↗
PubMed1981

Progestin-binding protein in human benign prostatic hypertrophy.

Cytosols from human benign prostatic hypertrophy contained progestin-binding components which bound to R 5020, ORG 2058 and progesterone in high affinity fashion. Most of the protein bound to R 5020 was recovered in the precipitate with 0-30% saturation of ammonium sulfate. The R 5020-binding protein showed sedimentation coefficients of 3.6S and 8.4S, and was eluted in the void volume of a Sephadex G-200 column. This protein was clearly distinguished from the dihydrotestosterone-binding protein by its precipitability by ammonium sulfate, heat stability and susceptibility to delipidization. R 5020 and ORG 2058 binding were markedly inhibited by the addition of R 1881, therefore, most of the binding to progestin in cytosols from the benign prostatic hypertrophy seems to be also the sites for R 1881. Although nuclear extract by 0.4 M KCl showed R 1881 binding, the extract did not contain the R 5020-binding protein, and this suggested that the progestin-binding protein observed in the cytosols does not seem to be the steroid receptor.

Carrier Proteins↗