J Teodorczyk-Injeyan, M A Jewett, J A Kellen, A Malkin
{"title":"Gonadoliberin (LHRH) mediated release of choriogonadotropin in experimental human and animal tumors in vitro.","authors":"J Teodorczyk-Injeyan, M A Jewett, J A Kellen, A Malkin","doi":"10.1080/07435808109065980","DOIUrl":"https://doi.org/10.1080/07435808109065980","url":null,"abstract":"Luteinizing hormone-releasing hormone (LHRH) stimulates a rapid release of chorionic gonadotropin (CG) in vitro from cell cultures of the JEG-3 choriocarcinoma and the R3230AC experimental rat mammary adenocarcinoma. The release of CG is time dependent: and dose-related. The addition of insulin or thyrotropin releasing hormone (TRH) to the cell cultures does not alter basal CG production.","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"8 1","pages":"19-24"},"PeriodicalIF":0.0,"publicationDate":"1981-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/07435808109065980","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17838493","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}
{"title":"Hyperglycemic activity of the 20,000-dalton variant of human growth hormone.","authors":"U J Lewis, R N Singh, G F Tutwiler","doi":"10.3109/07435808109045736","DOIUrl":"https://doi.org/10.3109/07435808109045736","url":null,"abstract":"<p><p>The 20,000-dalton structural variant of human growth hormone was inactive as a hyperglycemic agent in dogs when injected 10 h prior to a glucose tolerance test. Limited digestion with subtilisin did not generate hyperglycemic activity. These results are in contrast to those obtained with human growth hormone where subtilisin treatment potentiated the weak hyperglycemic activity of the undigested hormone. The results suggest that the 15 amino acid sequence that is deleted from the variant is either directly responsible for hyperglycemic activity or that a modification in tertiary structure produced by the deletion prevents a necessary proteolytic processing.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"8 3","pages":"155-64"},"PeriodicalIF":0.0,"publicationDate":"1981-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435808109045736","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18083896","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}
{"title":"Reciprocal relationship between the concentrations of serotonin and the activity of serotonin-N-acetyltransferase in rat pineal glands in culture.","authors":"A Chan, M Ebadi","doi":"10.1080/07435808109065981","DOIUrl":"https://doi.org/10.1080/07435808109065981","url":null,"abstract":"Serotonin is a co-substrate for catabolism of acetyl CoA by serotonin N-acetyltransferase (NAT), and acetyl CoA is the most potent known stabilizer of NAT activity against rapid thermal inactivation in pineal homogenate. The possibility that serotonin may modulate NAT activity was considered and subjected to experimentation. Chlorophenylalanine (4 mM) and R04–4602 (100 μM) enhanced the nor- epinephrine (NE)-induced stimulation of NAT activity in rat pineal glands in culture; whereas, 5-hydroxytryptophan (1 mM) attenuated it. Chlorophenylalanine (4 mM) decreased the fall of NAT activity induced by Z-propranolol; whereas, reserpine (50 μM) and serotonin (0.5 mM) had no effect. In contrast, 5-hydroxytryptophan (1 mM) accelerated the fall of NAT activity induced by Z-propranolol. Consequently, a reciprocal relationship appears to exist between the serotonin concentrations and NAT activity in pineal gland. Comparing the kinetics of native and NE-stimulated NAT, there occurred changes in Vmax with regard to bot...","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"8 1","pages":"25-44"},"PeriodicalIF":0.0,"publicationDate":"1981-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/07435808109065981","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17325860","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}
{"title":"Isolation and characterization of the subunits of porcine follicle-stimulating hormone.","authors":"R J Whitley, H T Keutmann, R J Ryan","doi":"10.1080/07435808109065984","DOIUrl":"https://doi.org/10.1080/07435808109065984","url":null,"abstract":"<p><p>The alpha and beta subunits of porcine FSH were isolated and purified to homogeneity as judged by SDS disc gel electrophoresis. The isolated subunits had less than 1% of the biological activity of the native hormone but were capable of recombining to generate at least 23% of the activity of the native hormone. The molecular weights calculated from hydrodynamic properties were 12,600 for pFSH alpha and 17,200 for pFSH beta. Total carbohydrate (g/100 g) was 18.9 for alpha and 15.1 for beta. The sialic acid content of alpha (3.8 g/100 g) exceeded that of beta (0.2 g/100 g). The alpha subunit contained significantly more lysine, alanine phenylalanine and methionine and significantly less aspartic acid, threonine, valine, isoleucine, leucine and tryptophan than the beta subunit. Evidence was found for N-terminal heterogeneity and an internal cleavage in the isolated alpha subunit.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"8 1","pages":"61-81"},"PeriodicalIF":0.0,"publicationDate":"1981-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/07435808109065984","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17838494","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}
{"title":"Age-associated changes in pineal serotonin N-acetyltransferase activity and melatonin content in the male gerbil.","authors":"T S King, B A Richardson, R J Reiter","doi":"10.3109/07435808109045744","DOIUrl":"https://doi.org/10.3109/07435808109045744","url":null,"abstract":"<p><p>Pineal serotonin N-acetyltransferase (NAT) activity and melatonin content were measured in 2- and 15-month old male gerbils at various times over a 24h light:dark cycle (LD 14:10). A nocturnal increase over the low daytime values in NAT activity and melatonin content was noted in both 2- and 15-month old gerbils, suggesting the continued existence of a circadian rhythm in each of these biochemical parameters of pineal secretory function at least until 15-months of age. Notable differences in the levels of NAT activity and melatonin content between 2- and 15-month old gerbils included (1) a phase shift in peak NAT activity and melatonin content in 15-month old versus 2-month old gerbils and (2) a latent decrease in NAT activity in 15-month old gerbils after the onset of the light period relative to that in 2-month old gerbils.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"8 4","pages":"253-62"},"PeriodicalIF":0.0,"publicationDate":"1981-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435808109045744","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18349876","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}
{"title":"Metabolism of asialotranscortin by hepatocytes and cortisol binding to hepatocytes.","authors":"K L Hossner, R B Billiar","doi":"10.1080/07435808109049842","DOIUrl":"https://doi.org/10.1080/07435808109049842","url":null,"abstract":"<p><p>Binding and catabolism of iodinated human transcortin and asialotranscortin were studied in isolated rat hepatocytes. Human transcortin binding to hepatocytes was very low (less than 3%) while 40-60% of the asialotranscortin bound to the hepatocytes. Asialofetuin inhibited asialotranscortin binding to hepatocytes, producing 50% inhibition of binding at 5 x 10-9M, but had no effect on transcortin binding. The lysosomal inhibitors leupeptin (0.05 mM) and ammonium chloride (10 mM) had no effect on asialotranscortin binding but prevented the latter's catabolism, suggesting lysosomal involvement in asialotranscortin degradation. Both transcortin and asialotranscortin inhibited the binding of [3H]cortisol to the hepatocytes in a dose-dependent manner.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"8 2","pages":"111-25"},"PeriodicalIF":0.0,"publicationDate":"1981-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/07435808109049842","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17236223","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}
{"title":"Binding of thyroid hormone by human erythrocyte cytosol proteins.","authors":"K Yoshida, P J Davis","doi":"10.3109/07435808009065971","DOIUrl":"https://doi.org/10.3109/07435808009065971","url":null,"abstract":"<p><p>Gel filtration (G-100, 0.01 M Tris, pH 7.4) of post-100,000 x g supernatant from lysate of washed human erythrocytes (RBC) revealed 3 fractions (R-1, R-2, R-3) which bound labeled T3 and T4. Major peak R-2 emerged with the mehoglobin fraction (A560 nm) and binding by this fraction was partially dissociable; the dissociable site bound D-T4, but not tetraidothyroacetic acid or reverse T3. Non-dissociable binding characterized peaks R-1 and R-3. R-1, R-2, and R-3 were pronase-digestible and R-1 binding was acid-unstable (pH 6.8 vs. 7.4). Evidence developed herein and elsewhere indicates that hemoglobin, itself, accounts for the binding within fraction R-2. Intact RBCs maintained for 72 hr at 4C in buffer enriched with T3 or T4 showed progressive incorporation with time of iodothyronines into the hemoglobin fraction.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"7 3","pages":"177-88"},"PeriodicalIF":0.0,"publicationDate":"1980-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435808009065971","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17828759","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}
{"title":"Ouabain effects on hormonally-stimulated bone resorption and cyclic AMP content in cultured fetal rat bones.","authors":"T J Hahn, T F DeBartolo, L R Halstead","doi":"10.3109/07435808009065972","DOIUrl":"https://doi.org/10.3109/07435808009065972","url":null,"abstract":"<p><p>Ouabain in concentrations from 20-100 micromoles produced a dose-related inhibition of in vitro stimulation of bone resorption by parathyroid hormone, 1,25-dihydroxyvitamin D3 and calcium ionophore A23187, as measured by 45Ca and [3H]-hydroxyproline release in 5-day cultures of fetal rat forelimb rudiments. The inhibitory effect on 45Ca release was completely reversed by subsequent incubation in ouabain-free medium. At a concentration of 100 micromoles ouabain virtually abolished active bone resorption; however, basal and stimulated bone cyclic AMP (cAMP) content were significantly increased above levels observed in the absence of ouabain. The increased cAMP content did not appear to be the result of phosphodiesterase inhibition. It is concluded that intact Na/K ATPase function is required for hormonally-stimulated bone resorptive processes and that the inhibitory effect of ouabain on bone resorption is produced at a point subsequent to cyclic AMP generation.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"7 3","pages":"189-200"},"PeriodicalIF":0.0,"publicationDate":"1980-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435808009065972","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17315010","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}
{"title":"The effects of estrogen on prolactin cells of the male rat pituitary. An immunocytologic and autoradiographic study.","authors":"B Corenblum, K Kovacs, G Penz, C Ezrin","doi":"10.3109/07435808009065967","DOIUrl":"https://doi.org/10.3109/07435808009065967","url":null,"abstract":"<p><p>Both immunoperoxidase staining (to identify specifically prolactin cells) and autoradiography after labelling with 3H-thylmidine (to demonstrate those cells which actively produce DNA) were performed on the same sections from normal male rat pituitaries and on those from rats treated with 17 beta-estradiol. In normal pituitaries, 3.3% of prolactin cells appeared to take up 3H-thymidine. Estrogen stimulation produced an increase in the weight of the pituitary and in the percentage of immunostained as well as of labelled prolactin cells, indicating that proliferation of prolactin cells at least in part accounted for the enlargement of the pituitary. The question, whether prolactin cell hyperplasia was due to multiplication of pre-existing, well differentiated prolactin cells or of immature prolactin cell precursors, remains to be elucidated.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"7 3","pages":"137-44"},"PeriodicalIF":0.0,"publicationDate":"1980-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435808009065967","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18429078","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}
{"title":"A membrane abnormality in lymphocytes from diabetic subjects.","authors":"H C Cheung, E C Almira, P C Kansal, W J Reddy","doi":"10.3109/07435808009065968","DOIUrl":"https://doi.org/10.3109/07435808009065968","url":null,"abstract":"<p><p>The fluorescence properties of the hydrophobic probe 1,6-diphenyl1-1,3,5-hexatriene incorporated in the lymphocytes of 30 diabetic patients and 21 normal control subjects were studied. The mean value of the probe polarization was 0.314 for the control group and 0.294 for the patient group. The difference was significant at p < 0.001. The decreased polarization was correlated with the level of plasma glucose in the patients (p < 0.01). Nanosecond fluorescence results obtained from the lymphocytes of 7 patients and 5 controls indicated that there was no significant difference in the probe lifetimes between the two groups of subjects and suggest that the decreased polarization of the probe in the patient group resulted from a more fluid lipid environment of cell membranes.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"7 3","pages":"145-56"},"PeriodicalIF":0.0,"publicationDate":"1980-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435808009065968","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18429081","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}