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N Furuta

Publications and source records attributed to N Furuta.

At least 73 records · Page 4Linked to original sources
PubMed1980

The waveform of the group mean SEP of normal human subjects.

The following conclusions were deduced from 200 SEPs recorded from 100 male and 100 female controls, of average age 22.34 +/- 1.70 years. (1) It was confirmed that the waveforms of a group mean SEP and of a group SD converge to a waveform which is not a flat horizontal line. (2) The waveform of the group mean SEP for the 200 normal subjects consisted of 12 components and was tetraphasic within 500 msec latency. The waveform of the group SD for the 200 normal subjects was also shown. (3) Some coincidences were established in early components within 50 msec latency, between the group mean SEP obtained in the present study and the group schematic SEPs reported by others, but large discrepancies were noted in later components. (4) With scaled SEPs, which were converted from unscaled SEPs by amplitude scaling in order to eliminate individual variation in absolute amplitude, similar results were obtained to those with unscaled SEPs. These results indicate the possibility of data reduction by amplitude scaling.

Adult↗
PubMed1980

The group mean SEP of normal human subjects.

The following conclusions were deduced from the SEPs of 100 normal human subjects, whose mean age was 21.80+/-1.62. It was confirmed that the waveform of a Group Mean SEP and of a Group SD each converges to a waveform different from a flat horizontal line. The waveform of the Group Mean SEP consisted of 12 components, and was roughly tetraphasic within 500 msec in latency. Large discrepancies were found in the later components between the Group Mean SEP and the Group Schematic SEPs reported by others, although some coincidences were shown in the early components within 100 msec in latency. The results derived from the Scaled SEPs, which were converted from the (unscaled) SEPs, indicated the possibility of a reduction of the data by the Amplitude Scaling.

Adult↗
PubMed1979

Chromatin transcription by progesterone-receptor complex in rabbit uterus.

This study was designed to investigate the chromatin transcription in vitro by progesterone-receptor complex in the estrogen-primed rabbit uterus. RNA synthesis by the uterine chromatin was stimulated when progesterone-uterine cytosol complex was bound to the chromatin and the stimulation was dependent upon the dose of the bound progesterone-cytosol 8S complex and upon the incubation time of the complex in the presence of the chromatin. Either norethindrone- or dydrogesterone-uterine cytosol complex also stimulated the uterine chromatin transcription but the extent was less than that of progesterone complex. These results indicate that progesterone as well as synthetic progestogens can directly regulate chromatin transcription via progesterone receptor in the rabbit uterine cells.

Animals↗
PubMed1978

[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↗
PubMed1978

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↗
PubMed1977

Contribution of functional groups of 19-nor-progestogens to binding to progesterone and estradiol-17beta receptors in rabbit uterus.

The structural elements of 19-norprogestogens which may be essential for binding to progesterone and estradiol-17beta(E2) receptors were investigated in the rabbit uterine cytosol. The kinetic study showed that 19-nor-progestogens are competitive inhibitors of progesterone-receptor (8S) binding and E2-receptor binding. The affinities of steroids for the progesterone receptor were as follows: norethindrone (Ki of 2.3 X 10(-9)M) greater than 5alpha-dihydronorethindrone greater than norethindrone acetate greater than lynestrenol greater than 17alpha-ethynyl-estra-4-ene-3beta, 17beta-diol greater than ethynodiol diacetate (Ki of 1.3 X 10(-7) M). The affinities of steroids for the E2 receptor were as follows: ethynodiol diacetate (Ki of 1.3 X 10(-7)M) greater than 17alpha-ethynyl-estra-4-ene-3beta, 17beta-diol greater than norethindrone acetate greater than norethindrone greater than 5alpha-dihydronorethindrone greater than lynestrenol (Ki of 8.4 X 10(-7)M). The results indicate that 3-ketone and 17beta-hydroxyl groups, and the plane of ring A/B of 19-norprogestogen are important for binding to the progesterone receptor. The affinities of 19-nor-progestogens for the E2 receptor were very weak. Their affinities for the E2 receptor increased with addition of acetate or hydroxyl groups at the 3beta and 17beta positions, and were decreased by the elimination of a 3 oxygen function or the reduction of ring A.

Animals↗