{"title":"Serum thyroxine, triiodothyronine, and TSH levels and TSH release after TRH in aging male and female rats.","authors":"G H Greeley, M A Lipton, J S Kizer","doi":"10.3109/07435808209045762","DOIUrl":"https://doi.org/10.3109/07435808209045762","url":null,"abstract":"<p><p>Serum levels of TSH, T3 and T4, pituitary responsiveness to TRH, and T3-resin uptake were examined in aging male and female rats. Despite normal serum TSH levels, serum T3 and T4 levels were significantly reduced in old male rats (19-26 months of age) when compared to young (120-150 days of age) and middle-aged males (12-1- months of age). In old female rats, serum TSH and T3 levels were not significantly (p greater than 0.05) different from those of young or middle-aged females. Serum T4 levels were significantly lower in old females when compared to younger rats. The T3-resin uptake of old rats was not significantly different from the value of young rats. Serum T4 levels, 3 hours after TRH induced TSH release, were significantly depressed in old male and female rats. Pituitary sensitivity to TRH was unaltered in old rats. These findings suggest that thyroidal release of T4 and T3 is depressed, and that the hypothalamic-pituitary axis is insensitive to diminished thyroid hormone feedback in old rats.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"9 3-4","pages":"169-77"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435808209045762","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17871812","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}
J. Mcarthur, B. Bullen, I. Beitins, M. Pagano, T. Badger, A. Klibanski
{"title":"Hypothalamic amenorrhea in runners of normal body composition.","authors":"J. Mcarthur, B. Bullen, I. Beitins, M. Pagano, T. Badger, A. Klibanski","doi":"10.1097/00006254-198102000-00016","DOIUrl":"https://doi.org/10.1097/00006254-198102000-00016","url":null,"abstract":"Three amenorrheic runners of normal body weight, in whom organic disease had been excluded, were found to exhibit: (1) normal body composition, (2) low baseline concentrations of serum LH and normal concentrations of FSH, (3) normal to hyper-responsiveness of LH and FSH to GnRH testing, and (4) normal and possibly increased frequency of LH pulsations. In one of the 3 runners, the administration of naloxone was followed by a pronounced increase in the amplitude of the LH pulsations.","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"7 1 1","pages":"13-25"},"PeriodicalIF":0.0,"publicationDate":"1981-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1097/00006254-198102000-00016","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"61929261","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 pineal does not concentrate arginine vasotocin from biological fluids in vivo.","authors":"L A Fisher, A J Schlosberg, J D Fernstrom","doi":"10.1080/07435808109049844","DOIUrl":"https://doi.org/10.1080/07435808109049844","url":null,"abstract":"<p><p>The ability of the pineal gland to concentrate circulating arginine vasotocin (AVT) from biological fluids in vivo was examined in rats. Intraventricular and intracisternal injections of AVT failed to elevate net pineal AVT content, even though CSF AVT levels were greatly increased by these treatments. Intravenous injection of AVT did elicit a light increase in pineal AVT, but plasma peptide levels wee elevated enormously. Thus, it seems unlikely that an active uptake process for AVT functions in this gland.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"8 2","pages":"135-44"},"PeriodicalIF":0.0,"publicationDate":"1981-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/07435808109049844","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18312030","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}
D B Ray, I A Horst, R W Jansen, R A Littlejohn, J Kowal
{"title":"Glucocorticoid regulation of alpha-lactalbumin production in long-term cultures of normal rat mammary cells.","authors":"D B Ray, I A Horst, R W Jansen, R A Littlejohn, J Kowal","doi":"10.3109/07435808109045737","DOIUrl":"https://doi.org/10.3109/07435808109045737","url":null,"abstract":"<p><p>Cultures of normal rat mammary cells have been developed which produce alpha-lactalbumin (a-LA) for several months in response to physiological levels of corticosterone whereas none is measureable without glucocorticoid. In contrast to recent studies in short-term organ cultures, these long-term cell cultures derived from virginal or mid-pregnant rats show no inhibition of a-LA production at high glucocorticoid concentrations. Comparable a-LA production was observed after a few months whether cells were initially cultured into media with various corticosterone levels or initially into high levels of corticosterone for 3 weeks prior to the shift to various lower doses.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"8 3","pages":"165-78"},"PeriodicalIF":0.0,"publicationDate":"1981-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435808109045737","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18085540","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":"Comparison of inhibition of bone resorption and escape with calcitonin and dibutyryl 3',5' cyclic adenosine monophosphate.","authors":"J F McLeod, L G Raisz","doi":"10.1080/07435808109065983","DOIUrl":"https://doi.org/10.1080/07435808109065983","url":null,"abstract":"<p><p>Both parathyroid hormone (PTH) and calcitonin (CT) can increase the concentration of cyclic 3',5' adenosine monophosphate (cAMP) in fetal rat bone in organ culture. Moreover, dibutyryl cAMP (dbcAMP) can both stimulate and inhibit 45Ca release from such bones depending on dose and experimental conditions. In this study we compared dbcAMP and CT for their effects on bones pretreated with PTH. Both compounds produced transient inhibition of bone resorption followed by escape. Escape from dbcAMP was independent of prostaglandin synthesis, since it occurred both in the presence and absence of indomethacin, a prostaglandin cyclo-oxygenase inhibitor.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"8 1","pages":"49-59"},"PeriodicalIF":0.0,"publicationDate":"1981-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/07435808109065983","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17325861","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":"Effect of MgATP on cAMP-dissociation kinetics of lactating rat mammary gland.","authors":"F Y Tang, L Catapano","doi":"10.3109/07435808109045747","DOIUrl":"https://doi.org/10.3109/07435808109045747","url":null,"abstract":"<p><p>Mammary gland cytosols exhibit temperature-dependent interconversion of cAMP-dissociation rates from low to high affinity (k-1 = 0.14 min-1 at 0 degree C to k-1 = 0.02 min-1 at 24 degrees association). This interconversion corresponds to a change from a site 2 to a site 1 cAMP-dissociation rate for the type II cAMP-dependent protein kinase in mammary gland cytosols. This report presents data which indicates a requirement for MgATP in the temperature-dependent interconversion of cAMP-dissociation rates. The effect of MgATP on the generation of the high affinity state was observed at 24 degrees C but not 0 degree C association. The effect of MgATP was not mimicked by equimolar MgAMP-PNP, but did require an intact type II protein kinase holoenzyme which can undergo autophosphorylation of its regulatory subunit. The effect of MgATP was reproduced with partially purified preparations of beef heart type II protein kinase. These results suggest that MgATP may act through autophosphorylation of the type II holoenzyme. The data suggest a novel role of MgATP in the regulation of cAMP binding to cAMP-dependent protein kinase II.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"8 4","pages":"285-95"},"PeriodicalIF":0.0,"publicationDate":"1981-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435808109045747","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17341096","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":"Effects of prostacyclin on rat seminal vesicle contractility in vitro.","authors":"R E Powers, C M Fredericks, H T Jonsson","doi":"10.1080/07435808109065982","DOIUrl":"https://doi.org/10.1080/07435808109065982","url":null,"abstract":"Prostacyclin (PGI2) caused a dose-dependent increase in the tonus of the rat seminal vesicle (RSV) in vitro. The sensitivity of the RSV to the prostaglandins examined was: PGE2 > PGI2 > 6-keto PGF1α.","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"8 1","pages":"45-8"},"PeriodicalIF":0.0,"publicationDate":"1981-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/07435808109065982","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18065217","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 importance of biopharmaceutic considerations in biological assays of LHRH and its analogs.","authors":"D W Hahn, A Phillips-Probst, J L McGuire","doi":"10.3109/07435808109045746","DOIUrl":"https://doi.org/10.3109/07435808109045746","url":null,"abstract":"<p><p>The choice of vehicle, route of administration and actual biological end-point utilized to measure the potency of LHRH analogs can have marked effects on the results of such studies. The activities of LHRH and an analog (D-TRP6,Pro9-NEt-LHRH) suspended in two vehicles were evaluated in two different biological tests including induction of ovulation in androgen sterilized rats and stimulation of uterine growth in immature mice. Our data clearly demonstrate that variables inherent in bioassays used to study LHRH analogs must be controlled if valid conclusions are to be made regarding the relative pharmacological activity and potency of these peptides.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"8 4","pages":"273-83"},"PeriodicalIF":0.0,"publicationDate":"1981-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435808109045746","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18087406","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":"Effect of relaxin on bound cAMP in rat uterus.","authors":"B M Sanborn, O D Sherwood","doi":"10.3109/07435808109045738","DOIUrl":"https://doi.org/10.3109/07435808109045738","url":null,"abstract":"<p><p>Relaxin was able to elevate uterine bound cAMP in the presence of 3-isobutyl-1-xanthine in buffers of low or high (0.5 M NaCl) ionic strength. Significant elevation was observed 10 min after exposure to the hormone. The peak in bound cAMP preceded that in total cAMP (15 vs 20 min, respectively, under isometric conditions). The response was concentration-dependent, with maximal elevation in bound cAMP observed at 0.1-0.4 microgram/ml relaxin. The effect of relaxin on bound cAMP represented a change in a sizable proportion of the total available binding sites. However, relaxin did not elevate bound cAMP in the absence of phosphodiesterase inhibitors under conditions where it clearly inhibited contractile activity. These data suggest that although relaxin can alter the level of bound cAMP in the rat uterus under some conditions, these effects may not be involved in the acute changes elicited by this hormone which result in the rapid inhibition of spontaneous contractile activity.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"8 3","pages":"179-92"},"PeriodicalIF":0.0,"publicationDate":"1981-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3109/07435808109045738","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17239623","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":"Phenol, a potent stimulator of adenylate cyclase in human thyroid membranes.","authors":"S M Amir, N J Mulrow, S H Ingbar","doi":"10.1080/07435808109049840","DOIUrl":"https://doi.org/10.1080/07435808109049840","url":null,"abstract":"<p><p>Among several commercial hCG preparations tested for their ability to stimulate adenylate cyclase in a human thyroid particulate fraction, only a pharmaceutical preparation (APL) was active. Activity of this preparation was lost during dialysis, but could be restored fully by the addition of phenol and partially by the addition of benzyl alcohol, the two additives present in APL. Phenol itself (0.040 - 2.0 mg/ml) induced a potent, dose-dependent stimulation of adenylate cyclase activity in a human thyroid particulate fraction and was also active in plasma membranes from rat liver and kidney cortex. Phenol exerted a biphasic effect on [125I]-bTSH binding to human thyroid membranes. Concentrations between 0.33 and 3.3 mg/ml were stimulatory to binding, while higher concentrations were inhibitory.</p>","PeriodicalId":75821,"journal":{"name":"Endocrine research communications","volume":"8 2","pages":"83-95"},"PeriodicalIF":0.0,"publicationDate":"1981-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/07435808109049840","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18312031","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}