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Biomedical subjects

S Boku

Publications and source records attributed to S Boku.

26 records · Page 2Linked to original sources

[The effect of enzymes on progesterone-receptor binding and chromatin binding of the complex in the estrogen-primed rabbit uterus (author's transl)].

The present study was designed to determine the characteristics of the progesterone receptor and chromatin binding site ("acceptor") of the progesterone-receptor complex in the rabbit uterus. The uterus was obtained from an estrogen-primed immature female rabbit. The binding of progesterone to the uterine receptor was examined in vitro. The progesterone-receptor binding was reduced only by proteases, and phosphorus moiety may not be related for progesterone-receptor binding. The effects of enzymes on the acceptor of the chromatin were investigated. The progesterone-receptor complex was bound to the dehistonized chromatin. The dehistonized chromatins, which were pretreated with enzymes at 4 degrees C or 37 degrees C for 30 minutes, were incubated with 3H-progesterone prelabeled uterine cytosol at 4 degrees C for 30 minutes, and the radioactivity in the chromatin pellet was counted. Proteases effectively decreased the receptor binding capacity to the dehistonized chromatin in the following order: pronase greater than trypsin greater than papain greater alpha-chymotrypsin. DNAse moderately and phospholipase A slightly decreased its binding capacity. The results may indicate that the acceptor site of the progesterone receptor is nonhistone protein over DNA of chromatin and may contain phosphorus moiety.

Animals↗

Preliminary studies on streoid-binding proteins in human testes of testicular feminization syndrome.

This study was designed to detect either 5alpha-dihydrotestosterone (DHT) or 17beta-estradiol (E2)-binding protein in the testes of a 1-year-old patient with testicular feminization syndrome (TFS) and in the testes of patients with prostatic cancer. Sucrose gradient analyses revealed E27S protein binding (but no such 7S protein binding of DHT) in the testes of the patient with TFS, but both E2 and DHT 7 S protein binding was observed in normal senile testes. The dissociation constants (Kd) were measured by charcoal adsorption. The Kd of E2 protein binding in both testes of different status was approximately 1.3 x 10(-9) M, and the Kd of DHT protein binding was 2.0 x 10(-9) M in the senile testes. A ligand specificty study indicated characteristics of both E2 and DHT receptors in the senile testes. It is speculated that a deficiency of androgen receptor and the presence of estrogen receptor in the testes of patients with TFS lead to insensitivity to androgen as a result of the androgen receptor deficiency and to sensitivity to estrogen as a result of the presence of the estrogen receptor.

Androgen-Insensitivity Syndrome↗

Progesterone receptor in human endometrium of leiomyoma uteri.

This study was designed to examine whether 8S protein as progesterone receptor exists in the human endometrium which has been primed with estrogen. The kinetic study showed that 8S-progesterone binding was specific with Kd of 2.0 X 10(-9) M. 5S-progesterone binding was inhibited competitively by cortisol. The study of ligand specificity also showed that progesterone and its related steroids had much stronger affinity for 8S component than for 5S component. Therefore, 5S protein may be CBG. Progesterone-8S protein binding was easily dissociated during the 5-20% sucrose gradient centrifugation, but such a protein from which progesterone had been dissociated could be sedimented at 8S region. Glycerol could stabilize progesterone-8S protein binding. These results indicate the existence of 8S protein as a progesterone receptor under the low salt medium in the estrogen primed human endometrium.

Endometrium↗

Zymogram analyses of various organs, glands and tissues from spontaneously hypertensive rats (SHR) and DOCA hypertensive rats.

Esterase and Acid phosphatase isozymes were examined in a number of organs, glands and tissues from Spontaneously Hypertensive Rats (SHR) and kidney and liver from DOCA hypertensive rats at various stages in comparison with those of normotensive rats (CR). In SHR, the abnormalities in the patterns of esterase isozyme were demonstrated in endocrine glands and respiratory tracts as well as in the kidney, liver and digestive tracts throughout the whole life span, and abnormalities in the patterns of acid phosphatase isozyme was also demonstrated in the liver after seven days of age. Moreover, in DOCA hypertensive Rats, minute alterations in esterase isozyme were demonstrated in the kidney and liver after seventh month of the duration of hypertension.

Acid Phosphatase↗