Pub Date : 1992-06-01DOI: 10.1507/endocrj1954.39.315
K Shizume, Y Shishiba, K Kuma, S Noguchi, J Tajiri, K Ito, J Y Noh
Periodic paralysis has been known to be associated with thyrotoxicosis in Japan. The incidence was 8.6% among male and 0.4% among female thyrotoxic patients according to a survey performed in the three major thyroid clinics in Japan in 1957. To determine the changes in the incidence during the intervening 34 years, the same type of survey was carried out again in 1991 at the same three major thyroid clinics previously involved. The incidence of paralysis in 1991 was 4.3% among male and 0.04% among female thyrotoxic patients, indicating more than a 40% decrease in the incidence. The possible cause of the decrease is related to the changes in food consumption, namely, to the fact that less carbohydrate and more potassium were taken in 1991 than in 1957.
{"title":"Comparison of the incidence of association of periodic paralysis and hyperthyroidism in Japan in 1957 and 1991.","authors":"K Shizume, Y Shishiba, K Kuma, S Noguchi, J Tajiri, K Ito, J Y Noh","doi":"10.1507/endocrj1954.39.315","DOIUrl":"https://doi.org/10.1507/endocrj1954.39.315","url":null,"abstract":"<p><p>Periodic paralysis has been known to be associated with thyrotoxicosis in Japan. The incidence was 8.6% among male and 0.4% among female thyrotoxic patients according to a survey performed in the three major thyroid clinics in Japan in 1957. To determine the changes in the incidence during the intervening 34 years, the same type of survey was carried out again in 1991 at the same three major thyroid clinics previously involved. The incidence of paralysis in 1991 was 4.3% among male and 0.04% among female thyrotoxic patients, indicating more than a 40% decrease in the incidence. The possible cause of the decrease is related to the changes in food consumption, namely, to the fact that less carbohydrate and more potassium were taken in 1991 than in 1957.</p>","PeriodicalId":11534,"journal":{"name":"Endocrinologia japonica","volume":"39 3","pages":"315-8"},"PeriodicalIF":0.0,"publicationDate":"1992-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1507/endocrj1954.39.315","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12597242","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1992-06-01DOI: 10.1507/endocrj1954.39.269
N Baskal, G Erdogan, A N Kamel, S S Dagci, S Akyar, C Ekinci
A case of immunoblastic lymphoma, involving only the thyroid and the adrenal glands, is presented. The patient had clinical symptoms and findings of Addison's disease, and computed tomography (CT) demonstrated bilateral adrenal tumoral enlargement. He also had euthyroid diffuse multinodular goiter. The diagnosis of the patient was based on the cytological examination of the aspiration materials from both endocrine glands. The patient received "m-BNCOD" chemotherapy regimen and replacement therapy for Addison's disease. At the end of three courses, a partial response was obtained.
{"title":"Localized non-Hodgkin's lymphoma of the adrenal and thyroid glands.","authors":"N Baskal, G Erdogan, A N Kamel, S S Dagci, S Akyar, C Ekinci","doi":"10.1507/endocrj1954.39.269","DOIUrl":"https://doi.org/10.1507/endocrj1954.39.269","url":null,"abstract":"<p><p>A case of immunoblastic lymphoma, involving only the thyroid and the adrenal glands, is presented. The patient had clinical symptoms and findings of Addison's disease, and computed tomography (CT) demonstrated bilateral adrenal tumoral enlargement. He also had euthyroid diffuse multinodular goiter. The diagnosis of the patient was based on the cytological examination of the aspiration materials from both endocrine glands. The patient received \"m-BNCOD\" chemotherapy regimen and replacement therapy for Addison's disease. At the end of three courses, a partial response was obtained.</p>","PeriodicalId":11534,"journal":{"name":"Endocrinologia japonica","volume":"39 3","pages":"269-76"},"PeriodicalIF":0.0,"publicationDate":"1992-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1507/endocrj1954.39.269","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12556616","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1992-06-01DOI: 10.1507/endocrj1954.39.325
T Tamagawa, A Iguchi, K Uemura, H Miura, K Nonogaki, T Ishiguro, N Sakamoto
The role of protein phosphatases in the regulation of insulin release from rat pancreatic islets was studied with protein phosphatase inhibitors, okadaic acid and calyculin A. Okadaic acid inhibited glucose- and glyceraldehyde-induced insulin release dose-dependently and also inhibited the potentiation of glucose-induced release either by adding forskolin, an activator of adenylate cyclase or by increasing K+ concentration to 25 mM. At a non-stimulatory concentration of 3 mM glucose, a high concentration (2 microM) of okadaic acid inhibited insulin release induced by high K+ or 12-O-tetradecanoylphorbol-13-acetate (TPA), an activator of protein kinase C, but a low concentration (1 microM) of okadaic acid did not significantly inhibit TPA-induced insulin release. Calyculin A also inhibited glucose-induced insulin release, and the effect was greater than that of okadaic acid. The data suggest that protein phosphatases may play an important role in the regulation of insulin release.
{"title":"Effects of the protein phosphatase inhibitors okadaic acid and calyculin A on insulin release from rat pancreatic islets.","authors":"T Tamagawa, A Iguchi, K Uemura, H Miura, K Nonogaki, T Ishiguro, N Sakamoto","doi":"10.1507/endocrj1954.39.325","DOIUrl":"https://doi.org/10.1507/endocrj1954.39.325","url":null,"abstract":"<p><p>The role of protein phosphatases in the regulation of insulin release from rat pancreatic islets was studied with protein phosphatase inhibitors, okadaic acid and calyculin A. Okadaic acid inhibited glucose- and glyceraldehyde-induced insulin release dose-dependently and also inhibited the potentiation of glucose-induced release either by adding forskolin, an activator of adenylate cyclase or by increasing K+ concentration to 25 mM. At a non-stimulatory concentration of 3 mM glucose, a high concentration (2 microM) of okadaic acid inhibited insulin release induced by high K+ or 12-O-tetradecanoylphorbol-13-acetate (TPA), an activator of protein kinase C, but a low concentration (1 microM) of okadaic acid did not significantly inhibit TPA-induced insulin release. Calyculin A also inhibited glucose-induced insulin release, and the effect was greater than that of okadaic acid. The data suggest that protein phosphatases may play an important role in the regulation of insulin release.</p>","PeriodicalId":11534,"journal":{"name":"Endocrinologia japonica","volume":"39 3","pages":"325-9"},"PeriodicalIF":0.0,"publicationDate":"1992-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1507/endocrj1954.39.325","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12503199","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1992-04-01DOI: 10.1507/endocrj1954.39.177
H Kouhara, T Tatekawa, M Koga, S Hiraga, N Arita, H Mori, B Sato
A case of a 29-year-old man with an ACTH-producing pituitary tumor disseminated into the subarachnoid space is described. After total adrenalectomy for Cushing's disease at the age of 15, Nelson's syndrome developed. Transsphenoidal adenomectomy at 17 and 21 years of age, pituitary irradiation and medical therapies with sodium valproate, baclofen and bromocriptine failed to lower his plasma ACTH level. Multiple intracranial and intraspinal tumors associated with the symptoms of left hemiparesis developed. The removal of a tumor grown at the level of C1-3 was performed with successful palliation of his symptoms. Histologically, the tumor cells showed sinusoidal, papillary and diffuse patterns with a preponderance of the former over the latter two, although the papillary pattern predominated in the primary pituitary tumor. Immunohistochemical analysis demonstrated most cells to be positive for ACTH in the metastatic tumor as well as the primary adenoma. The clinical significance of his course is discussed with a review of 11 reported cases with metastatic ACTH-producing pituitary tumors.
{"title":"Intracranial and intraspinal dissemination of an ACTH-secreting pituitary tumor.","authors":"H Kouhara, T Tatekawa, M Koga, S Hiraga, N Arita, H Mori, B Sato","doi":"10.1507/endocrj1954.39.177","DOIUrl":"https://doi.org/10.1507/endocrj1954.39.177","url":null,"abstract":"<p><p>A case of a 29-year-old man with an ACTH-producing pituitary tumor disseminated into the subarachnoid space is described. After total adrenalectomy for Cushing's disease at the age of 15, Nelson's syndrome developed. Transsphenoidal adenomectomy at 17 and 21 years of age, pituitary irradiation and medical therapies with sodium valproate, baclofen and bromocriptine failed to lower his plasma ACTH level. Multiple intracranial and intraspinal tumors associated with the symptoms of left hemiparesis developed. The removal of a tumor grown at the level of C1-3 was performed with successful palliation of his symptoms. Histologically, the tumor cells showed sinusoidal, papillary and diffuse patterns with a preponderance of the former over the latter two, although the papillary pattern predominated in the primary pituitary tumor. Immunohistochemical analysis demonstrated most cells to be positive for ACTH in the metastatic tumor as well as the primary adenoma. The clinical significance of his course is discussed with a review of 11 reported cases with metastatic ACTH-producing pituitary tumors.</p>","PeriodicalId":11534,"journal":{"name":"Endocrinologia japonica","volume":"39 2","pages":"177-84"},"PeriodicalIF":0.0,"publicationDate":"1992-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1507/endocrj1954.39.177","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12500890","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1992-04-01DOI: 10.1507/endocrj1954.39.217
Y Ito, K Yasuda, N Takeda, S Goto, M Hayashi, H Inoue, K Aoyama, K Miura
In order to identify insulin receptors in the bovine adrenal cortex and medulla, we have studied 125I-porcine insulin binding to the membrane preparations from the bovine adrenal cortex and medulla. 125I-porcine insulin bound not only to the bovine adrenal cortex but to the medulla in time-, temperature-, and pH-dependent manners. The maximum levels of 125I-porcine insulin binding in the two tissues were observed at 4 degrees C for 24 h of incubation, and its optimum pH ranged from 7.6 to 8.0. Under these conditions, at tracer concentration of porcine insulin (200 pg/ml), 10.4% and 6.6% of 125I-porcine insulin added to each reaction tube bound specifically to 10(5) x g-pellet fractions (microsomal membrane) from the cortical tissue (0.3 mg of protein) and from the medullary tissue (2 mg of protein), respectively. 125I-porcine insulin binding was observed predominantly in the microsomal membrane from the bovine adrenal cortex, and in a 15,000 x g- pellet fraction (synaptosomal membrane) from the bovine adrenal medulla. Scatchard analysis of binding data yielded curvilinear plots in each tissue. Analysis of curvilinear plots based on two sites model revealed similar affinity constant between the cortex and medulla. Receptor concentration of the cortex was several times higher than that of the medulla. In the two bovine adrenal tissues, human proinsulin and insulin-like growth factor I (IGF-I) had about 1/100 potency compared to porcine insulin in displacing 125I-porcine insulin binding. Porcine glucagon added with concentration up to 10(-6) M did not inhibit 125I-porcine insulin binding to both the cortex and the medulla.(ABSTRACT TRUNCATED AT 250 WORDS)
{"title":"Characterization of insulin receptors in the bovine adrenal cortex and medulla.","authors":"Y Ito, K Yasuda, N Takeda, S Goto, M Hayashi, H Inoue, K Aoyama, K Miura","doi":"10.1507/endocrj1954.39.217","DOIUrl":"https://doi.org/10.1507/endocrj1954.39.217","url":null,"abstract":"<p><p>In order to identify insulin receptors in the bovine adrenal cortex and medulla, we have studied 125I-porcine insulin binding to the membrane preparations from the bovine adrenal cortex and medulla. 125I-porcine insulin bound not only to the bovine adrenal cortex but to the medulla in time-, temperature-, and pH-dependent manners. The maximum levels of 125I-porcine insulin binding in the two tissues were observed at 4 degrees C for 24 h of incubation, and its optimum pH ranged from 7.6 to 8.0. Under these conditions, at tracer concentration of porcine insulin (200 pg/ml), 10.4% and 6.6% of 125I-porcine insulin added to each reaction tube bound specifically to 10(5) x g-pellet fractions (microsomal membrane) from the cortical tissue (0.3 mg of protein) and from the medullary tissue (2 mg of protein), respectively. 125I-porcine insulin binding was observed predominantly in the microsomal membrane from the bovine adrenal cortex, and in a 15,000 x g- pellet fraction (synaptosomal membrane) from the bovine adrenal medulla. Scatchard analysis of binding data yielded curvilinear plots in each tissue. Analysis of curvilinear plots based on two sites model revealed similar affinity constant between the cortex and medulla. Receptor concentration of the cortex was several times higher than that of the medulla. In the two bovine adrenal tissues, human proinsulin and insulin-like growth factor I (IGF-I) had about 1/100 potency compared to porcine insulin in displacing 125I-porcine insulin binding. Porcine glucagon added with concentration up to 10(-6) M did not inhibit 125I-porcine insulin binding to both the cortex and the medulla.(ABSTRACT TRUNCATED AT 250 WORDS)</p>","PeriodicalId":11534,"journal":{"name":"Endocrinologia japonica","volume":"39 2","pages":"217-22"},"PeriodicalIF":0.0,"publicationDate":"1992-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1507/endocrj1954.39.217","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12567710","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1992-04-01DOI: 10.1507/endocrj1954.39.185
N Mimou, R Takeda
To assess the possible role of mineralocorticoids in the onset and maintenance of hypertension in adrenal regeneration hypertensive (ARH) rats, the change in plasma mineralocorticoids, with adrenal regeneration after enucleation in ARH rats was investigated and compared with those in unilaterally nephroadrenalectomized, 1% saline-fed (UNA) rats, sham-operated, 1% saline-fed (1% NaCl) rats and water-fed (water) rats. Plasma aldosterone was determined by RIA and the other mineralocorticoids were measured by HPLC. How plasma PRL, a marker of central dopaminergic activity, affected aldosterone secretion was determined by RIA. In ARH, plasma corticosterone (B), 18-OH-DOC and aldosterone levels 2 weeks after operation were as low as 20-30% of corresponding values, but the plasma DOC level was almost 100% of the corresponding value in the other groups. Four weeks after operation plasma B increased to a level comparable with that in the other groups and the plasma aldosterone level remained low. However, plasma DOC and 18-OH-DOC levels 4 weeks after operation were as high as 120-200% of corresponding values in the other groups. Six weeks after operation, the plasma aldosterone level returned to a value comparable with that in UNA and 1% NaCl and plasma DOC and 18-OH-DOC levels returned to corresponding values in the other groups. The plasma PRL level 4 weeks after operation was significantly lower in ARH than in the other groups. These results suggest that transient DOC and 18-OH-DOC increases observed in ARH may be important in the onset of hypertension, while other factors may be involved in its maintenance and that the transient central dopaminergic hyperactivity observed in ARH may be responsible for a delayed return from aldosterone deficiency.
{"title":"Altered secretion of corticosteroids and prolactin in adrenal regeneration hypertensive rats.","authors":"N Mimou, R Takeda","doi":"10.1507/endocrj1954.39.185","DOIUrl":"https://doi.org/10.1507/endocrj1954.39.185","url":null,"abstract":"<p><p>To assess the possible role of mineralocorticoids in the onset and maintenance of hypertension in adrenal regeneration hypertensive (ARH) rats, the change in plasma mineralocorticoids, with adrenal regeneration after enucleation in ARH rats was investigated and compared with those in unilaterally nephroadrenalectomized, 1% saline-fed (UNA) rats, sham-operated, 1% saline-fed (1% NaCl) rats and water-fed (water) rats. Plasma aldosterone was determined by RIA and the other mineralocorticoids were measured by HPLC. How plasma PRL, a marker of central dopaminergic activity, affected aldosterone secretion was determined by RIA. In ARH, plasma corticosterone (B), 18-OH-DOC and aldosterone levels 2 weeks after operation were as low as 20-30% of corresponding values, but the plasma DOC level was almost 100% of the corresponding value in the other groups. Four weeks after operation plasma B increased to a level comparable with that in the other groups and the plasma aldosterone level remained low. However, plasma DOC and 18-OH-DOC levels 4 weeks after operation were as high as 120-200% of corresponding values in the other groups. Six weeks after operation, the plasma aldosterone level returned to a value comparable with that in UNA and 1% NaCl and plasma DOC and 18-OH-DOC levels returned to corresponding values in the other groups. The plasma PRL level 4 weeks after operation was significantly lower in ARH than in the other groups. These results suggest that transient DOC and 18-OH-DOC increases observed in ARH may be important in the onset of hypertension, while other factors may be involved in its maintenance and that the transient central dopaminergic hyperactivity observed in ARH may be responsible for a delayed return from aldosterone deficiency.</p>","PeriodicalId":11534,"journal":{"name":"Endocrinologia japonica","volume":"39 2","pages":"185-96"},"PeriodicalIF":0.0,"publicationDate":"1992-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1507/endocrj1954.39.185","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12568423","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1992-04-01DOI: 10.1507/endocrj1954.39.157
S Shima, H Fukase, N Akamatsu
Effects of short and long exposure to the diabetic state induced by an injection of streptozotocin to young female rats on glucagon- and catecholamine-sensitive adenylate cyclase activity and adrenergic receptors of hepatic membranes have been studied. The short period of exposure to the diabetic state exhibited an increase in the sensitivity of the enzyme to isoproterenol without changes in the affinity and the number of beta-adrenergic receptors. The increased response of adenylate cyclase activity to isoproterenol was accompanied with a greater GTP-induced lowering of the affinity to the beta-adrenergic agonist in diabetic membranes than in the controls. The chronic diabetic state produced a decrease in the adenylate cyclase activity to hormonal or non-hormonal stimuli with a fall in the number of alpha- and beta-adrenergic receptors. These results suggest that the observed effects of the diabetic state on hormonally sensitive adenylate cyclase activities and their receptor binding sites of the hepatic membranes would vary depending on the duration and/or severity of the diabetic state experimentally induced.
{"title":"Adrenergic receptors and adenylate cyclase activity in hepatocytes of the streptozotocin-diabetic rat.","authors":"S Shima, H Fukase, N Akamatsu","doi":"10.1507/endocrj1954.39.157","DOIUrl":"https://doi.org/10.1507/endocrj1954.39.157","url":null,"abstract":"<p><p>Effects of short and long exposure to the diabetic state induced by an injection of streptozotocin to young female rats on glucagon- and catecholamine-sensitive adenylate cyclase activity and adrenergic receptors of hepatic membranes have been studied. The short period of exposure to the diabetic state exhibited an increase in the sensitivity of the enzyme to isoproterenol without changes in the affinity and the number of beta-adrenergic receptors. The increased response of adenylate cyclase activity to isoproterenol was accompanied with a greater GTP-induced lowering of the affinity to the beta-adrenergic agonist in diabetic membranes than in the controls. The chronic diabetic state produced a decrease in the adenylate cyclase activity to hormonal or non-hormonal stimuli with a fall in the number of alpha- and beta-adrenergic receptors. These results suggest that the observed effects of the diabetic state on hormonally sensitive adenylate cyclase activities and their receptor binding sites of the hepatic membranes would vary depending on the duration and/or severity of the diabetic state experimentally induced.</p>","PeriodicalId":11534,"journal":{"name":"Endocrinologia japonica","volume":"39 2","pages":"157-63"},"PeriodicalIF":0.0,"publicationDate":"1992-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1507/endocrj1954.39.157","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12568421","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1992-04-01DOI: 10.1507/endocrj1954.39.203
K Ichikawa, K Hashizume, M Kobayashi, Y Nishii, A Sakurai, T Takeda, S Suzuki, T Yamada
Human beta thyroid hormone receptor (c-erb A beta protein) produced by an Escherichia coli expression system was purified by sequential column chromatography followed by electroelution from an electrophoresis gel and an antibody was prepared. The antibody recognized a 56 kDa protein band in a partially purified rat hepatic nuclear thyroid hormone receptor fraction on Western blotting. Although multiple bands appeared on Western blotting of crude rat hepatic receptor preparations, a 56 kDa band was the most prominent and preadsorption of the antibody by purified c-erb A protein resulted in almost complete disappearance of the 56 kDa band, indicating that the 56 kDa band was formed by a specific antigen-antibody interaction. Furthermore, the 56 kDa protein appeared to co-elute with 3, 5, 3'-triiodo-L-thyronine binding activity in hydroxylapatite, Sephacryl S-200, and DNA-cellulose column chromatography of rat hepatic nuclear receptor, and sequential column purification resulted in selective enrichment of the 56 kDa band. These results suggest that the 56 kDa protein may be the major component of the rat hepatic thyroid hormone receptor.
利用大肠杆菌表达体系制备的人β甲状腺激素受体(c-erb A β蛋白),经序列柱层析和电泳凝胶电泳纯化,制备抗体。该抗体在Western blotting上识别部分纯化的大鼠肝核甲状腺激素受体片段中的56 kDa蛋白带。虽然在大鼠肝受体粗制剂的Western blotting上出现多个条带,但56 kDa条带最为突出,纯化的c-erb a蛋白预吸附抗体后,56 kDa条带几乎完全消失,表明56 kDa条带是由特异性抗原-抗体相互作用形成的。此外,56 kDa蛋白似乎与大鼠肝核受体羟基磷灰石、Sephacryl S-200和dna -纤维素柱层析中的3,5,3 '-三碘- l -甲状腺原氨酸结合活性共洗脱,顺序柱纯化导致56 kDa条带选择性富集。这些结果表明,56 kDa蛋白可能是大鼠肝甲状腺激素受体的主要成分。
{"title":"Recognition of a 56 kDa protein in partially purified rat hepatic nuclear thyroid hormone receptor by anti-human c-erb A beta antibody.","authors":"K Ichikawa, K Hashizume, M Kobayashi, Y Nishii, A Sakurai, T Takeda, S Suzuki, T Yamada","doi":"10.1507/endocrj1954.39.203","DOIUrl":"https://doi.org/10.1507/endocrj1954.39.203","url":null,"abstract":"<p><p>Human beta thyroid hormone receptor (c-erb A beta protein) produced by an Escherichia coli expression system was purified by sequential column chromatography followed by electroelution from an electrophoresis gel and an antibody was prepared. The antibody recognized a 56 kDa protein band in a partially purified rat hepatic nuclear thyroid hormone receptor fraction on Western blotting. Although multiple bands appeared on Western blotting of crude rat hepatic receptor preparations, a 56 kDa band was the most prominent and preadsorption of the antibody by purified c-erb A protein resulted in almost complete disappearance of the 56 kDa band, indicating that the 56 kDa band was formed by a specific antigen-antibody interaction. Furthermore, the 56 kDa protein appeared to co-elute with 3, 5, 3'-triiodo-L-thyronine binding activity in hydroxylapatite, Sephacryl S-200, and DNA-cellulose column chromatography of rat hepatic nuclear receptor, and sequential column purification resulted in selective enrichment of the 56 kDa band. These results suggest that the 56 kDa protein may be the major component of the rat hepatic thyroid hormone receptor.</p>","PeriodicalId":11534,"journal":{"name":"Endocrinologia japonica","volume":"39 2","pages":"203-7"},"PeriodicalIF":0.0,"publicationDate":"1992-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1507/endocrj1954.39.203","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12568424","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1992-04-01DOI: 10.1507/endocrj1954.39.197
K Kadowaki, K Koike, K Hirota, M Ohmichi, H Kurachi, A Miyoke, O Tanizawa
The effect of vasoactive intestinal peptide (VIP) and PHI-27 on dopamine accumulation in cultured rat hypothalamic cells was investigated. VIP enhanced [3H]dopamine accumulation dose dependently. This effect was significant at 10(-8)-10(-5) M VIP with a concomitant increase in intracellular cyclic AMP (cAMP), and reached its plateau level at 10(-6) M VIP. VIP increased [3H]dopamine accumulation significantly within 15 min. PHI-27 and dibutyryl cAMP ((Bu)2-cAMP) also enhanced [3H]dopamine accumulation. These results suggest that VIP enhances dopamine accumulation in hypothalamic cells by increasing intracellular cAMP.
{"title":"Vasoactive intestinal peptide enhances dopamine accumulation in primary cell culture of rat hypothalamus.","authors":"K Kadowaki, K Koike, K Hirota, M Ohmichi, H Kurachi, A Miyoke, O Tanizawa","doi":"10.1507/endocrj1954.39.197","DOIUrl":"https://doi.org/10.1507/endocrj1954.39.197","url":null,"abstract":"<p><p>The effect of vasoactive intestinal peptide (VIP) and PHI-27 on dopamine accumulation in cultured rat hypothalamic cells was investigated. VIP enhanced [3H]dopamine accumulation dose dependently. This effect was significant at 10(-8)-10(-5) M VIP with a concomitant increase in intracellular cyclic AMP (cAMP), and reached its plateau level at 10(-6) M VIP. VIP increased [3H]dopamine accumulation significantly within 15 min. PHI-27 and dibutyryl cAMP ((Bu)2-cAMP) also enhanced [3H]dopamine accumulation. These results suggest that VIP enhances dopamine accumulation in hypothalamic cells by increasing intracellular cAMP.</p>","PeriodicalId":11534,"journal":{"name":"Endocrinologia japonica","volume":"39 2","pages":"197-202"},"PeriodicalIF":0.0,"publicationDate":"1992-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1507/endocrj1954.39.197","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12500891","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1992-04-01DOI: 10.1507/endocrj1954.39.209
T Murai, K Noguchi, A Nagamoto, M Hosaka
To examine whether immature rat Sertoli cells in culture secrete a factor(s) which stimulates testosterone production by mature mouse Leydig cells, Sertoli cell-enriched cultures were prepared from 3-week-old male rats with trypsin and collagenase. Sertoli cells were plated at an initial density of 3-5 x 10(6) cells/35 mm well and cultured in 3 ml serum free media supplemented with insulin (10 micrograms/ml). Sertoli cell culture medium (SCCM) collected every 3rd day was added to Leydig cells (10(6) cells in 1 ml of MEM with 2% steroid-free FCS) prepared from 10-week-old mice by mechanical separation and incubated for 3 h at 34 degrees C. Secreted testosterone was determined by RIA. SCCM 15 times concentrated by Amicon YM10 membrane demonstrated a dose-dependent stimulation of testosterone production, whereas there was no effect on testosterone secretion when Leydig cells were maximally stimulated by LH. Leydig cell stimulating activity was retained by both a dialysis membrane with a pore size of 24 A and an ultrafiltration membrane with a molecular weight cut-off of 10 kDa. However, activity was reduced by heating at 60 degrees C for 30 min and almost lost after incubation with 0.1% trypsin for 1 h at 37 degrees C. This activity was not retained by means of a Con A-Agarose column and was demonstrated only in break-through fractions. HPLC gel filtration of a 15 times concentrated SCCM preparation on a TSK gel G3000SW revealed Leydig cell-stimulating activity at approximately 13 kDa.(ABSTRACT TRUNCATED AT 250 WORDS)
{"title":"A partial characterization of a Sertoli cell-secreted protein stimulating Leydig cell testosterone production.","authors":"T Murai, K Noguchi, A Nagamoto, M Hosaka","doi":"10.1507/endocrj1954.39.209","DOIUrl":"https://doi.org/10.1507/endocrj1954.39.209","url":null,"abstract":"<p><p>To examine whether immature rat Sertoli cells in culture secrete a factor(s) which stimulates testosterone production by mature mouse Leydig cells, Sertoli cell-enriched cultures were prepared from 3-week-old male rats with trypsin and collagenase. Sertoli cells were plated at an initial density of 3-5 x 10(6) cells/35 mm well and cultured in 3 ml serum free media supplemented with insulin (10 micrograms/ml). Sertoli cell culture medium (SCCM) collected every 3rd day was added to Leydig cells (10(6) cells in 1 ml of MEM with 2% steroid-free FCS) prepared from 10-week-old mice by mechanical separation and incubated for 3 h at 34 degrees C. Secreted testosterone was determined by RIA. SCCM 15 times concentrated by Amicon YM10 membrane demonstrated a dose-dependent stimulation of testosterone production, whereas there was no effect on testosterone secretion when Leydig cells were maximally stimulated by LH. Leydig cell stimulating activity was retained by both a dialysis membrane with a pore size of 24 A and an ultrafiltration membrane with a molecular weight cut-off of 10 kDa. However, activity was reduced by heating at 60 degrees C for 30 min and almost lost after incubation with 0.1% trypsin for 1 h at 37 degrees C. This activity was not retained by means of a Con A-Agarose column and was demonstrated only in break-through fractions. HPLC gel filtration of a 15 times concentrated SCCM preparation on a TSK gel G3000SW revealed Leydig cell-stimulating activity at approximately 13 kDa.(ABSTRACT TRUNCATED AT 250 WORDS)</p>","PeriodicalId":11534,"journal":{"name":"Endocrinologia japonica","volume":"39 2","pages":"209-15"},"PeriodicalIF":0.0,"publicationDate":"1992-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1507/endocrj1954.39.209","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12567709","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}