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Akira Miyake, Keiichi Tasaka, Shintaro Mori, Youichi Saito, and Toshihiro Aono

Abstract. The effect of prostaglandin D2 on the release of luteinizing hormone was studied in a superfusion system by superfusing human pituitary gland. Perfusion with 30 μg of prostaglandin D2 induced a significant increase of luteinizing hormone secretion. This is the first evidence of a direct effect of prostaglandin D2 on the secretion of luteinizing hormone from the human pituitary gland. This finding suggests the possible role of prostaglandin D2 in human reproductive function

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Haruyoshi Nakao, Masafumi Koga, Masayo Arao, Makoto Nakao, Bunzo Sato, Susumi Kishimoto, Yoichi Saitoh, Norio Arita, and Shintaro Mori

Abstract. We have performed an enzyme-immunoassay for estrogen receptor on 56 human pituitary adenomas and compared the results with a single point estradiol binding assay. There was a significant positive correlation between the two assays of cytoplasmic estrogen receptor (r = 0.960). Normal human pituitaries (N = 2) had an estrogen receptor concentration of 17 fmol/mg protein by enzyme-immunoassay. Of 14 prolactinomas, 6 (43%) contained estrogen receptor with a concentration of 33.5 ± 7.4 (mean ± sem) fmol/mg protein. Six of 11 (55%) macroprolactinomas were estrogen receptorpositive, whereas all 3 microprolactinomas were estrogen receptor-negative. Only one (13%) of 8 GH- and PRL-secreting adenomas, and 3 of 6 (50%) gonadotropin-secreting adenomas were estrogen receptor-positive; the latter had a concentration of 13.5 ± 1.6 fmol/mg protein. Estrogen receptor was not detected in 21 pure GH-secreting adenomas and 7 nonsecreting adenomas. These results demonstrate the precise frequency of estrogen receptor in various human pituitary adenomas, since enzyme-immunoassay as well as single point estradiol binding assay could detect estrogen receptor even in small specimens. Enzyme-immunoassay is suitable for evaluation of estrogen receptor status in human pituitary adenomas.

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Masafumi Koga, Haruyoshi Nakao, Masayo Arao, Bunzo Sato, Keizo Noma, Yasuhiko Morimoto, Susumu Kishimoto, Shintaro Mori, and Toru Uozumi

Abstract. Dopamine receptors on human pituitary adenoma membranes were characterized using [3H] spiperone as the radioligand. The specific [3H]spiperone binding sites on prolactin (PRL)-secreting adenoma membranes were recognized as a dopamine receptor, based upon the data showing high affinity binding, saturability, specificity, temperature dependence, and reversibility. All of 14 PRL-secreting adenomas had high affinity dopamine receptors, with a dissociation constant (Kd) of 0.85 ±0.11 nmol/l (mean ± sem) and a maximal binding capacity (Bmax) of 428 ± 48.6 fmol/mg protein. Among 14 growth hormone (GH)-secreting adenomas examined, 8 (57%) had dopamine receptors with a Kd of 1.90 ± 0.47 nmol/l and a Bmax of 131 ± 36.9 fmol/mg protein. Furthermore, 15 of 24 (58%) nonsecreting pituitary adenomas also had dopamine receptors with a Kd of 1.86 ± 0.37 nmol/l and a Bmax of 162 ± 26.0 fmol/mg protein. These results indicate that some GH-secreting adenomas as well as some nonsecreting pituitary adenomas contain dopamine receptors. But their affinity and number of binding sites are significantly lower (P < 0.05) and fewer (P < 0.001) respectively, than those in PRL-secreting adenomas.