{"title":"Effects of cholera toxin on thyroid cyclic AMP-dependent protein kinase and ornithine decarboxylase activities.","authors":"Y Friedman, P Hladis, D Babiarz-Crowell, G Burke","doi":"10.3109/07435807909070885","DOIUrl":"https://doi.org/10.3109/07435807909070885","url":null,"abstract":"<p><p>Cholera toxin activated beef thyroid cyclic AMP-dependent protein kinase in a dose (0.2 to 8 microgram/ml)-related fashion. Thus, when beef thyroid slices were incubated with toxin (8 microgram/ml) for 90 minutes and then assayed for protein kinase, the activity ratio (i.e. -cyclic AMP/+cyclic AMP) increased from 0.32 +/- 0.02 to 0.77 +/- 0.06. The toxin (5 microgram/ml)-induced increase was abolished by inclusion of ganglioside GM1 in the incubation medium (I50, 0.7 microgram/ml), whereas, gangliosides GD1a and GT1 were without effect. In contrast, TSH-activated protein kinase was unaffected by ganglioside addition. Cholera toxin increased rat thyroid ornithine decarboxylase (ODC) activity in-vitro in a dose (0.1 to 10 microgram/ml)-related fashion [basal, 100 cf cholera toxin (10 microgram/ml), 1500 pmol 14CO2/g tissue/30 min]. The toxin (1 microgram/ml)- (but not TSH-) induced increase in ODC was abolished by inclusion of ganglioside Ga and GT1 were without effect. Cholera toxin stimulation of ODC was inhibited by indomethacin or iodide as are the stimulatory effects of TSH or dibutyryl cyclic AMP. These results demonstrate that although there are differences in the TSH and cholera toxin responses with respect to receptor (ganglioside) interaction, they nevertheless elicit similar intracellular responses in thyroid.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"6 1","pages":"71-92"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435807909070885","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11441343","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":"Molecular conformation of thyroid hormones: structure and binding interactions of thyroxine.","authors":"V Cody","doi":"10.1080/07435807909061100","DOIUrl":"https://doi.org/10.1080/07435807909061100","url":null,"abstract":"<p><p>In an accurately determined X-ray diffraction study of the thyroid hormone thyroxine (T4), the two independent conformations in the crystal lattice show significant differences in the outer phenyl ring geometry when compared with that of 3,5,3'-triiodothyronine (T3). The major differences between the T4 and T3 structures are a shortened C4'-O4' bond, contraction of the C3'-C4'-C5' angle and an increase in the C3' and C5' angles of T4. These changes can be correlated with the difference in acidity of the 4'-OH of T4 and T3 and help to explain binding affinity differences among thyroactive compounds. The hydrogen bond directionality observed in T4 and other thyroid structures offers an insight into the molecular details of the hormone-receptor site. The conformation of one T4 molecule is cisoid, that of the other transoid, the first such instance of different overall conformations to be found in the same crystal lattice. One T4 molecule has the side chain nearly coplanar with the inner ring, an unusual conformation among thyroid structures.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"6 2","pages":"123-34"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/07435807909061100","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11714169","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}
M K Vaughan, J Buchanan, D E Blask, R J Reiter, P J Sheridan
{"title":"Diurnal variation in uterine estrogen receptors in immature female rats--inhibition by arginine vasotocin.","authors":"M K Vaughan, J Buchanan, D E Blask, R J Reiter, P J Sheridan","doi":"10.3109/07435807909061794","DOIUrl":"https://doi.org/10.3109/07435807909061794","url":null,"abstract":"<p><p>A diurnal variation in uterine estrogen receptors from immature female rats was observed with the peak occurring during the mid-light phase (noon) of the cycle. Although no dose response was noted, all concentrations of arginine vasotocin ranging from 5 x 10(-7) to 5 x 10(-9) significantly inhibited binding of 3H-estradiol to estrogen receptors in the cytosol fraction of uteri obtained from immature female rats either during the light or dark phase of the photoperiod.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"6 3","pages":"191-201"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435807909061794","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11776840","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}
B A Roos, A W Lindall, S B Baylin, J O'Neil, A L Frelinger, R S Birnbaum, P W Lambert
{"title":"Plasma immunoreactive calcitonin in lung cancer.","authors":"B A Roos, A W Lindall, S B Baylin, J O'Neil, A L Frelinger, R S Birnbaum, P W Lambert","doi":"10.1080/07435807909061104","DOIUrl":"https://doi.org/10.1080/07435807909061104","url":null,"abstract":"<p><p>We have measured plasma calcitonin in 135 untreated eucalemic men with lung cancer and a control/smoker population. Calcitonin levels were determined by radioimmunoassay and validated by immunoextraction. Plasma immunoreactive calcitonin moieties were purified by immunoadsorbent chromatography, treated with mercaptoethanol and urea, and characterized by gel filtration. Artifacts in human calcitonin radioimmunoassays of cancer-patient plasmas were detected by parallel plasma incubations in a salmon calcitonin radioimmunoassay system which does not detect human calcitonin and by immunoprecipitation of tracer at the end of radioimmunoassay incubations. Heating fresh plasmas to 65 degrees C for 1.5 hours reduced radioimmunoassay artifacts without loss of calcitonin moieties. Such characterization of hypercalcitoninemia in each of the histopathological types of lung cancer has raised some important questions about the interpretation of plasma calcitonin radioimmunoassay measurements in lung cancer. Based on inhibition of tracer-antibody binding, plasma calcitonin seemed to be elevated in 18% (14/80) of basal plasma samples obtained from patients with epidermoid or with anaplastic lung cancer. Unequivocal hypercalcitoninemia (heat stable, causing no inhibition of antibody-tracer binding in the salmon calcitonin radioimmunoassays, and immunoextractable with human calcitonin antibodies) was not found in any of the apparently hypercalcitoninemic plasmas from persons with epidermoid or anaplastic lung cancer. By contrast, unequivocal hypercalcitoninemia was found in 27% (15/55) of plasmas from patients with small cell carcinoma or adenocarcinoma. Most of the immunoreactive calcitonin recovered from small cell and adenocarcinoma lung cancer plasmas with unequivocally elevated calcitonin is much larger than calcitonin monomer.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"6 2","pages":"169-90"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/07435807909061104","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11443910","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}
P R Marques, D D Williams, L Shen, D G Johnson, D J Baylink, C C Gale
{"title":"Parathyroid hormone release is not associated with acute sympathetic arousal in goats.","authors":"P R Marques, D D Williams, L Shen, D G Johnson, D J Baylink, C C Gale","doi":"10.3109/07435807909070884","DOIUrl":"https://doi.org/10.3109/07435807909070884","url":null,"abstract":"<p><p>Physiological activation of the sympathetic adrenomedullary (SAM) axis following both thermal and non thermal stress was assessed by changes in serum norepinephrine, glucose and/or protein as well as indices of peripheral blood flow. The occurrence of elevated serum parathyroid hormone (PTH) did not reliably reflect SAM activation as might be predicted from pharmacological studies that document a beta adrenergic receptor mechanism in the parathyroid gland that mediates catecholamine stimulated release of PTH into the circulation. The beta agonist isoproterenol at 1 microgram/min for 60 min did produce a transient increase in serum PTH at 20 min. Overall, the data raise doubts about the physiological significance of the adrenergic receptor in the parathyroid gland. Significant increases in serum PTH of 67% and 109% above basal respectively were seen following ruminal loading with cold and thermoneutral water. Associated with the PTH change were increased serum phosphorus and elevated or constant serum protein and serum total calcium.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"6 1","pages":"57-70"},"PeriodicalIF":0.0,"publicationDate":"1979-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435807909070884","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11692624","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":"Radioimmunoassay for partially degraded thyrotropin.","authors":"B C Nisula, P N Fredlund","doi":"10.3109/07435807809089013","DOIUrl":"https://doi.org/10.3109/07435807809089013","url":null,"abstract":"<p><p>A radioimmunoassay for partially pepsin degraded bovine thyrotropin (bTSH) was developed and used to examine human thyrotropin (hTSH) preparations and sera obtained from patients with Graves' ophthalmopathy for the presence of cross-reactivity. As little as 4 microunits of the hTSH (68/38) reference preparation produced inhibition of binding in the radioimmunoassay, but none of the sera obtained from patients with Graves' disease (n = 26) contained detectable cross-reactivity. These data indicate that there is a substantial amount of partially degraded thyrotropin in human pituitary extracts, but none detectable in the sera of patients with Graves' ophthalmopathy.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"5 2","pages":"125-34"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435807809089013","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11784639","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":"Pineal serotonin N-acetyltransferase activity and melatonin concentrations in prepubertal and adult Syrian hamsters exposed to short daily photoperiods.","authors":"E S Panke, R J Reiter, M D Rollag, T W Panke","doi":"10.1080/07435807809061095","DOIUrl":"https://doi.org/10.1080/07435807809061095","url":null,"abstract":"<p><p>Pineal serotonin N-acetyltransferase activity (NAT) and melatonin concentrations were determined at various intervals in prepubertal (35 days old) and adult male hamsters (74 day old) throughout a 24 hour period with the animals kept in a light:dark cycle of 6:18 (lights on at 0600 h and off at 1200 h). In prepubertal animals, daytime pineal NAT activity of 0.20-0.28 nmoles 14C-N-acetyltryptamine/pineal/hour was maintained for 8 hours after the initiation of darkness. Peak pineal NAT activity of 0.46 +/- 0.64 nmoles 14C-N-acetyltryptamine/pineal/hour occurred 13 hours after the onset of darkness and remained significantly elevated until 0400 h (p less than 0.001). Daytime pineal melatonin concentrations of 78-194 pg/pineal gland also were maintained for 8 hours after the initiation of darkness. At 13 hours into the dark period, pineal melatonin concentrations rose to 788 +/- 150 pg/pineal gland (p less than 0.01 vs all other time points except 0230 h and 0400 h). At one hour before the onset of light both the pineal NAT activity and pineal melatonin concentrations returned to daytime values. Adult male hamsters had diurnal pineal NAT and melatonin rhythms which are indistinguishable from those found in the prepubertal animals.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"5 4","pages":"311-24"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/07435807809061095","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11953023","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":"Corticosteroid response of rabbits and rats to exogenous ACTH.","authors":"C Boiti, R S Yalow","doi":"10.1080/07435807809073633","DOIUrl":"https://doi.org/10.1080/07435807809073633","url":null,"abstract":"<p><p>The dynamics of the alterations of the cortisol: corticosterone ratio in rabbits during porcine ACTH administration were studied on an almost daily basis and as a function of time after injection. In rabbits the cortisol: corticosterone ratio increased strikingly but variably during the treatment period. Rats responded to similar treatment only with increased corticosterone release. The differences are attributed to the presence of 1-39 ACTH as well as intermediate ACTH in the rabbit pituitary but not in the rat pituitary.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"5 1","pages":"21-33"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/07435807809073633","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11428688","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 effect of quipazine, a serotonin receptor agonist, on serum corticosterone concentration in rats.","authors":"R W Fuller, H D Snoddy, J A Clemens","doi":"10.3109/07435807809089015","DOIUrl":"https://doi.org/10.3109/07435807809089015","url":null,"abstract":"<p><p>Quipazine, a serotonin receptor agonist, increased serum corticosterone within 30 min after its i.p. injection (at 10 mg/kg) into rats; the effect persisted at 1 and 2 hrs, but not at 4 hrs. Elevation of serum corticosterone did not occur with a 1.25 mg/kg dose of quipazine but was dose-related over a 2.5-20 mg/kg dose range. The effect of quipazine was completely prevented by methergoline, a serotonin receptor antagonist. The effect of quipazine was present in rats pretreated with 5,7-dihydroxytryptamine to destroy serotonin nerves and was not enhanced (as was the effect of L-5-hydroxytryptophan) by fluoxetine pretreatment. These data are compatible with the idea that quipazine increases serum corticosterone as a consequence of direct stimulation of serotonin receptors in brain.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"5 2","pages":"161-71"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435807809089015","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11523142","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":"Studies on pituitary follitropin. IV. A conformation specific radioimmunoassay for the ovine hormone.","authors":"M R Sairam","doi":"10.1080/07435807809061093","DOIUrl":"https://doi.org/10.1080/07435807809061093","url":null,"abstract":"<p><p>An antiserum to partially purified ovine follitropin (50 x NIH-FSH-S10) shows species specificity. It is conformation dependent and requires the proper recombination of the alpha and beta subunits for maximal reactivity. The isolated alpha subunit is essentially inactive and the hormone specific beta subunit is weakly reactive. The homologous radioimmunoassay is valuable for estimating native ovine follitropin in the presence of free subunits. It also provides a sensitive method to study association-dissociation and structure-function relationships.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"5 4","pages":"279-91"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/07435807809061093","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11775253","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}