Thyrotropin action is impaired in the thyroid gland of old rats

1992 ◽  
Vol 126 (1) ◽  
pp. 55-63 ◽  
Author(s):  
Frédéric Reymond ◽  
Nicole Dénéréaz ◽  
Thérèse Lemarchand-Béraud
Keyword(s):  
Thyroid Gland ◽  
Adenylate Cyclase ◽  
Binding Sites ◽  
Hormone Secretion ◽  
Plasma Concentrations ◽  
Male Rats ◽  
High Affinity ◽  
Young Rats ◽  
Old Rats ◽  
Camp Formation

Aging in rats is characterized by low plasma concentrations of thyroid hormones with unchanged levels of TSH, suggesting an altered TSH action in addition to the impaired regulation of TSH secretion. To evaluate TSH action we determined TSH binding to thyroid membranes of young and old male rats (3–4 and 24–26 months of age), as well as the activity of adenylate cyclase in basal and stimulated conditions. Saturation analyses of [125I]-bTSH to thyroid membranes in the presence of increasing quantities of unlabelled bTSH (0.03–100 mU) show two types of binding sites, one of high affinity (Ka 1.5 109 mol l−1) the other of lower affinity (Ka 1.2 108 mol l−1), which are similar in both age groups. The number of TSH binding sites of high affinity is less in old rats than in young rats (7.6±0.9 vs 14.8±1.1 TSH mU/mg protein, N = 11 and 10 respectively, p< <0.001), whereas the number of binding sites of low affinity is not significantly different (76.0±8.2 vs 99.1±9.0 TSH mU/mg protein). The activity of adenylate cyclase determined in basal conditions is similar in both old and young rats (1.11±0.12 vs 1.04±0.9 nmol cAMP/2 h x mg/protein). TSH (10 mU) induced a significant increase in cAMP formation with the thyroid membranes from young rats but not with those from old rats. In contrast, the stimulation of cAMP formation by GTP (2 mmol/l) or forskolin (10 mmol/l), two direct stimulators of adenylate cyclase, is similar in both groups of rats (200% and 250%, respectively). These data suggest that the reduced action of TSH on the thyroid gland of old rats is due to the decreased number of TSH binding sites, which may also be partly responsible for the low thyroid hormone secretion with aging in spite of the unchanged levels of TSH. A postreceptor defect does not seem to be involved, since direct stimulations of adenylate cyclase by GTP or forskolin are just as effective in old rats as in young rats.

Effects of trenbolone acetate and testosterone on growth and on plasma concentrations of corticosterone and ACTH in rats

1990 ◽  
Vol 126 (3) ◽  
pp. 461-466 ◽  
Author(s):  
M. N. Sillence ◽  
R. G. Rodway
Keyword(s):  
Weight Gain ◽  
Growth Response ◽  
Plasma Concentrations ◽  
Female Rats ◽  
Male Rats ◽  
Adrenal Weight ◽  
Trenbolone Acetate ◽  
Male And Female Rats ◽  
Age Related ◽  
Old Rats

ABSTRACT The effects of trenbolone acetate (TBA) on growth and on plasma concentrations of corticosterone were examined in male and female rats. At 5 weeks of age, rats were injected with TBA (0·8 mg/kg) dissolved in peanut oil, or with oil alone, daily for 10 days. In female rats, TBA caused an increase in weight gain (20–38%), a reduction in adrenal weight (19%) and a reduction in plasma concentrations of corticosterone (55%). In contrast, TBA-treated male rats showed no significant increase in weight gain, no significant change in adrenal weight and no reduction in plasma concentrations of corticosterone. The mechanism by which adrenal activity was suppressed in TBA-treated female rats was examined and the response compared with that to testosterone. Female rats (8 weeks old) were injected daily either with oil vehicle, TBA (0·8 mg/kg) or testosterone propionate (0·8 mg/kg). Testosterone increased weight gain (24%), but the growth response to TBA treatment was significantly greater (97%). A reduction in plasma concentrations of corticosterone (45%) was again observed in response to TBA. However, testosterone increased plasma concentrations of corticosterone (52%) above those of control values. Neither androgen affected plasma concentrations of ACTH. Finally, the effects of TBA were examined in 6-week-old female rats, to characterize further the apparent age-related increase in responsiveness. The growth response of 6-week-old rats (60–74%) was intermediate between that seen in 5- and 8-week-old animals. It is concluded that part of the anabolic activity of TBA may be related to a reduction in circulating concentrations of corticosterone. The effect of TBA on corticosterone concentrations differs from that of the natural androgen, testosterone, and does not appear to be mediated by a reduction in plasma concentrations of ACTH. Journal of Endocrinology (1990) 126, 461–466

Differential effects of passive immunization with somatostatin antiserum on adenohypophysial hormone secretions in starved rats

1986 ◽  
Vol 109 (2) ◽  
pp. 169-174 ◽  
Author(s):  
J. N. Hugues ◽  
A. Enjalbert ◽  
E. Moyse ◽  
C. Shu ◽  
M. J. Voirol ◽  
...  
Keyword(s):  
Binding Capacity ◽  
Hormone Secretion ◽  
Plasma Concentrations ◽  
Passive Immunization ◽  
Negative Control ◽  
Prolactin Secretion ◽  
Male Rats ◽  
Minimal Effective Dose ◽  
Gh Secretion

ABSTRACT The role of somatostatin (SRIF) on adenohypophysial hormone secretion in starved rats was reassessed by passive immunization. Because of the absence of pulsatile GH secretion in starved rats, the effects of the injection of SRIF antiserum on GH levels can be clearly demonstrated. To determine whether starvation modifies the sensitivity of the adenohypophysis to SRIF, we measured 125I-labelled iodo-N-Tyr-SRIF binding. There was no difference in the dissociation constant (Kd) nor in the maximal binding capacity (Bmax) in fed (n = 15) and starved (n = 15) animals (Kd = 0·38 ± 0·09 (s.e.m.) and 0·45 ± 0·09 nmol; Bmax = 204 ± 39 and 205 ± 30 fmol/mg protein respectively). Administration of SRIF antiserum resulted in a dose-dependent increase in plasma concentrations of GH, TSH and prolactin. The minimal effective dose of SRIF antiserum was 50 μl for GH, 100 μl for TSH and 200 μl for prolactin. Our results show that: (1) starvation does not modify adenohypophysial SRIF-binding sites, (2) in starved male rats endogenous SRIF exerts a negative control on prolactin secretion in vivo and (3) sensitivity to endogenous SRIF seems to be different for each hypophysial cell type. J. Endocr. (1986) 109, 169–174

scholarly journals ENGLISH VERSION: AGE FEATURES OF RADIOACTIVE IODINE (131I) ABSORPTION BY RAT THYROID GLANDS IN CORRECTION OF THE DIETARY IODINE DEFICIENCY WITH ORGANIC IODINE

2021 ◽  
Vol 25 (1-2) ◽  
pp. 31-35
Author(s):  
O.I. Ryabukha
Keyword(s):  
Thyroid Gland ◽  
Iodine Deficiency ◽  
Radioactive Iodine ◽  
Male Rats ◽  
Organic Iodine ◽  
Study Results ◽  
Thyroid Glands ◽  
Immature Rats ◽  
Old Rats ◽  
Rat Thyroid

The structure of endocrine morbidity is characterized by a significant spread of thyroid pathology. The insufficient efficacy of inorganic iodine drugs poses the problem of search for new means for iodine deficiency treatment and prevention. Given the progressive aging of the population in economically developed countries, the purpose of the study was to clarify the effect of organic iodine on the features of absorption and elimination of radioactive iodine from the thyroid glands of variously aged rats in the conditions of iodine deficiency in the diet. The study was performed on nonlinear white male rats in two series of studies that were kept on iodine-deficient isocaloric starch-casein diet for 60 days: the first series included two groups of old rats weighing 0.400-0.450 kg, the second series – two groups of sexually immature rats weighing 0.060-0.090 kg. There were 5 rats in each group. In animals of the experimental groups in each series, 10% of casein in the diet was replaced with organic iodine, which came with iodine-protein preparation from the red Black Sea algae Phyllophora nervosa. The functional state of the thyroid gland was studied using the Sodium Iodide Na 131 I Injection drug. The dosimetry was performed using the STS-6 Geiger-Muller Detector. Radioindication of the thyroid gland was carried out after subcutaneous administration of 0.1 ml of 131I solution at the following time intervals: 0.5, 1, 2, 4, 6, 8, 10, 12, 24, 48, 72, and 96 hours after administration of 131I. The study results were presented as a percentage of the radioiodine dose administered, adjusted for natural radioactivity background and the radioactive decay of the drug. It was found that in the iodine deficiency conditions, the thyroid glands of old rats have higher rates of radioiodine absorption and a lower rate of its excretion than the glands of immature rats, which indicates their lower iodine reserve and greater liability to iodine deficiency pathology. Intake of organic iodine regardless of the rats’ age is accompanied by a decrease in radioiodine accumulation and acceleration of its excretion from the thyroid gland, which indicates a decrease in functional stress, but the glands of older rats absorb more iodine and excrete it more slowly, indicating less effective correction of iodine deficiency with age. Reduced functional activity of the thyroid glands in old rats can be used as a sensitive changes marker for the in-depth study of thyrotropic and thyroid disrupting effects.

scholarly journals Binding of malonyl-CoA to isolated mitochondria. Evidence for high- and low-affinity sites in liver and heart and relationship to inhibition of carnitine palmitoyltransferase activity

1984 ◽  
Vol 222 (3) ◽  
pp. 639-647 ◽  
Author(s):  
M I Bird ◽  
E D Saggerson
Keyword(s):  
Binding Sites ◽  
Maximal Activity ◽  
Liver Mitochondria ◽  
Carnitine Palmitoyltransferase ◽  
Male Rats ◽  
Heart Mitochondria ◽  
Binding Characteristics ◽  
Functional Sites ◽  
High Affinity ◽  
Malonyl Coa

[14C]Malonyl-CoA bound to intact mitochondria isolated from rat liver and heart in a manner consistent with the presence of two independent classes of binding sites in each tissue. The binding characteristics for mitochondria obtained from fed male rats were: for heart, KD(1) = 11-18nM, KD(2) = 30 microM, N1 = 7pmol/mg of protein, N2 = approx. 660pmol/mg of protein; for liver, KD(1) = 0.1 microM, KD(2) = 5.6 microM, N1 = 11pmol/mg of protein, N2 = 165pmol/mg of protein. In the presence of 40 microM-palmitoyl-CoA the characteristics of binding at the high-affinity sites were changed, so that for heart KD(1) = 0.26 microM, with no change in N1 and for liver KD(1) = approx. 2 microM, with N1 increased to approx. 40pmol/mg of protein. Differences between the two tissues in tightness of malonyl-CoA binding at the high-affinity sites explains the considerably greater sensitivity of heart CPT1 (overt form of carnitine palmitoyltransferase) to inhibition by malonyl-CoA [Saggerson & Carpenter, (1981) FEBS Lett. 129, 229-232; McGarry, Mills, Long & Foster (1983) Biochem. J. 214, 21-28]. Starvation (24h) did not change the characteristics of [14C]malonyl-CoA binding to liver mitochondria and did not alter the I50 (concentration giving 50% inhibition) for displacement of [14C]malonyl-CoA by palmitoyl-CoA. Therefore the decreased sensitivity of liver CPT1 to inhibition by malonyl-CoA in starvation [Saggerson & Carpenter (1981) FEBS Lett. 129, 225-228; Bremer (1981) Biochim. Biophys. Acta 665, 628-631] is not explained by differences in malonyl-CoA binding. Percentage occupancy of the high-affinity sites in heart mitochondria by malonyl-CoA correlated closely with percentage inhibition of CPT1 measured under similar conditions. This finding supports the proposal that the high-affinity binding sites are the functional sites mediating inhibition of CPT1 by malonyl-CoA. Similar experiments with liver mitochondria also suggested that the occupancy of high-affinity sites by malonyl-CoA regulates CPT1 activity. 5,5′-Dithiobis-(2-nitrobenzoic acid), which decreased the sensitivity of heart or liver CPT1 to inhibition by malonyl-CoA [Saggerson & Carpenter (1982) FEBS Lett. 137, 124-128], also decreased [14C]malonyl-CoA binding to the high-affinity sites of heart mitochondria. N1 values for [14C]malonyl-CoA binding to high-affinity sites in liver mitochondria were determined in various physiological states which encompassed a 7-fold range of CPT1 maximal activity (fed, starved, pregnant, hypothyroid, foetal). The N1 value did not change in these states.(ABSTRACT TRUNCATED AT 400 WORDS)

scholarly journals P0529THE DIFFERENCE IN DIETARY RESTRICTION-INDUCED NEPHROPROTECTIVE MECHANISMS IN YOUNG AND OLD ANIMALS

2020 ◽  
Vol 35 (Supplement_3) ◽  
Author(s):  
Nadezda Andrianova ◽  
Ljubava Zorova ◽  
Irina Pevzner ◽  
Vasily Popkov ◽  
Denis Silachev ◽  
...  
Keyword(s):  
Lipid Peroxidation ◽  
Dietary Restriction ◽  
Kidney Tissue ◽  
Kidney Injury ◽  
Male Rats ◽  
Kidney Cells ◽  
Lipid Peroxidation Products ◽  
Kidney Slices ◽  
Young Rats ◽  
Old Rats

Abstract Background and Aims Acute kidney injury (AKI) is a widespread disease affecting mostly old people. Dietary restriction (DR), based on the reduction of food intake, is believed to be one of the most efficient approaches ameliorating damage in different pathological conditions including age-associated diseases. The aim of the study was to investigate the protective mechanisms of DR in the model of AKI in young and old rats. Method All experiments were made on young (3-4 months) and old (22-24 months) male rats. DR was performed by limiting the amount of food for 35% of the ad libitum (AL) daily intake. Since earlier, we showed ineffectiveness of 4-weeks DR in old rats, in this study we applied 35% DR lasting 8 weeks for old rats and 4 weeks for young rats. During DR, we registered the weight loss and measured the level of adiponectin, as this hormone is closely associated with adipose tissue metabolism. Renal ischemia/reperfusion (I/R) was used as a model of ischemic AKI. I/R was performed by clamping the left renal pedicle for 40 minutes followed by reperfusion with simultaneous contralateral nephrectomy. The severity of AKI was evaluated by measuring blood urea nitrogen (BUN), serum creatinine (SCr) and the levels of protein biomarkers of AKI (NGAL and L-FABP) in urine. Proliferation in kidney epithelium in response to I/R was analyzed by PCNA protein level in kidney tissue. We evaluated the function of mitochondria by measuring TMRE/MitoTracker Green ratio in vital kidney slices; in kidney homogenates, we also analyzed levels of Bcl-XL and Bcl-XS proteins. The production of reactive oxygen species (ROS) was evaluated by staining vital kidney slices with DCF. The content of lipid peroxidation products was measured using Image-iT Lipid Peroxidation Kit, and the level of carbonylated proteins was determined by OxyBlot Protein Oxidation Detection Kit. The activation of autophagic-lysosomal system was estimated by western blotting to LC3 II/LC3 I ratio and LAMP1 level, as well as by staining vital kidney slices with LysoTracker Green probe. Results The body weight of rats during DR dropped as far as 20% by the end of 4 weeks in young rats and 30% by the end of 8 weeks in old rats. Nevertheless, adiponectin concentration elevated during DR only in the serum of young rats. DR strongly influenced mitochondria function, in particular, elevated mitochondrial membrane potential both in kidney cells of young and old rats. DR also resulted in increasing the Bcl-XL level. We revealed the decrease of ROS and lipid peroxidation products in vital kidney slices, but only in kidneys of young rats. However, DR reduced the content of carbonyl groups more than 2 times in animals of both ages. We showed that activation of autophagy in response to DR and I/R occurred only in the kidneys of young rats, indicating deterioration of autophagy signaling in old animals. We also found that 48 h after I/R PCNA level increased 19 times in young kidney, although old rats showed only 4-fold elevation of kidney cells proliferation. Estimation of kidney injury markers (NGAL, L-FABP) in urine revealed that 2-month DR led to some protection in old rats. Nonetheless, despite all positive alterations in kidney tissue of old rats, DR was not able to ameliorate impairment of kidney function after I/R, whereas all young rats showed significant improvement of SCr and BUN levels. Conclusion Short-term DR has a significant nephroprotective effect against renal I/R in young rats. Old animals require longer periods of food restriction, after which some protective alterations are observed. We propose, protection of kidney in old and young rats is implemented through slightly different mechanisms and some of them are missing in old animals.

Characterization of cholecystokinin binding sites in goldfish brain and pituitary

1996 ◽  
Vol 271 (1) ◽  
pp. R137-R143 ◽  
Author(s):  
B. A. Himick ◽  
S. R. Vigna ◽  
R. E. Peter
Keyword(s):  
Binding Sites ◽  
Hormone Secretion ◽  
Pituitary Hormone ◽  
Tissue Sections ◽  
High Affinity ◽  
Hypothalamic Nuclei ◽  
High Affinity Binding Site ◽  
Vagal Lobe ◽  
Feeding Center ◽  
Reversible Time

The characterization and distribution of cholecystokinin (CCK)/gastrin binding sites were determined in the goldfish central nervous system (CNS). Binding of 125I-sulfated CCK octapeptide (125I-CCK-8s) in tissue sections was found to be saturable, reversible, time dependent, and displaceable by CCK/gastrin-like peptides. Analysis of saturable equilibrium binding revealed a high-affinity binding site (dissociation constant of 0.706 +/- 0.188 nM), which also displayed high affinity for gastrin-17s and caerulein. Lower affinities were observed for the nonsulfated forms of CCK-8 and gastrin-17. These findings suggest that a single primitive CCK/gastrin receptor exists in the goldfish CNS. The distribution of CCK/gastrin binding sites in the goldfish brain and pituitary revealed high densities within the telencephalon and preoptic hypothalamus, as well as within hypothalamic nuclei associated with the brain feeding center. High densities of binding sites were also localized within the midbrain tegmentum and optic tectum of the midbrain, the facial lobe and vagal lobe of the hindbrain, and within the pituitary pars distalis. Overall, these findings support previous studies that indicate that CCK/gastrin-like peptides play a role in the central regulation of feeding behavior and pituitary hormone secretion in fish.

RADIOACTIVE INULIN, SULPHATE AND CHLORIDE SPACES AND ELECTROLYTES IN THE THYROID GLAND OF RATS AT DIFFERENT AGES

1969 ◽  
Vol 45 (2) ◽  
pp. 197-205
Author(s):  
S. Y. CHOW ◽  
D. M. WOODBURY
Keyword(s):  
Thyroid Gland ◽  
Epithelial Cells ◽  
Thyroid Tissue ◽  
Volume Of Distribution ◽  
Male Rats ◽  
Tissue Concentrations ◽  
Young Rats ◽  
Electrolyte Content ◽  
Inulin Space ◽  
Different Ages

SUMMARY [14C]Inulin, 35SO42- and 36Cl- spaces, 131I- thyroid: serum (T:S) ratio, histological measurements of follicles and electrolyte content of the thyroid gland were determined in male rats 3–17 weeks of age. The thyroid [14C]inulin space of animals of different ages was not significantly different. The thyroid 35SO42- space, however, varied with age. The youngest rats had the largest 35SO42- space. Histological measurements indicated that in the thyroid follicles the epithelial cells were much thinner and the luminal volume was much larger in the younger rats than in older animals. In the older rats, the 35SO42- space was equal to the sum of [14C]inulin (stromal) and the histologically determined luminal spaces. In the younger animals, although the 35SO42- space was larger than in the older animals, it was still not large enough to equal the sum of the volumes determined by the [14C]inulin and the direct histological measurements of the lumen. This is due to the high colloid content in the follicular lumen of the young rats. The lower thyroid 131I- T:S ratio in younger rats also indicated that the thyroid gland was less active than in older animals. The volume of distribution of thyroid Cl- calculated from the chemically determined data of the plasma and of the thyroid tissue concentrations of rats of different ages was the same as that determined by 36Cl-.

Effects of post-mortem delay on high affinity forskolin binding sites and adenylate cyclase activity in rat and human striatum and cerebral cortex

1993 ◽  
Vol 629 (2) ◽  
pp. 225-230 ◽  
Author(s):  
Brian Ross ◽  
Deborah Dawson ◽  
Deborah Dewar ◽  
Mhairi Macrae ◽  
John Knowler ◽  
...  
Keyword(s):  
Cerebral Cortex ◽  
Adenylate Cyclase ◽  
Binding Sites ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Post Mortem ◽  
High Affinity

ANDROGEN RECEPTORS IN THE RAT BRAIN, ANTERIOR PITUITARY GLAND AND VENTRAL PROSTATE GLAND: EFFECTS OF ORCHIDECTOMY AND AGEING

1979 ◽  
Vol 81 (1) ◽  
pp. 75-81 ◽  
Author(s):  
B. D. GREENSTEIN
Keyword(s):  
Pituitary Gland ◽  
Binding Sites ◽  
Anterior Pituitary ◽  
Androgen Receptors ◽  
Prostate Gland ◽  
Anterior Pituitary Gland ◽  
Male Rats ◽  
Ventral Prostate ◽  
Binding Reaction ◽  
Old Rats

Available high-affinity binding sites for 5α-dihydrotestosterone (DHT) were measured in cytosols obtained from the amygdala, hypothalamus, anterior pituitary gland and ventral prostate gland of 12-week-old rats at various times after orchidectomy, and in the corresponding tissues of 18-month-old male rats. It is suggested that the lower affinity of the DHT binding reaction in brain and ventral prostatic cytosols after orchidectomy or ageing respectively, may explain, at least in part, the changes in the responsiveness of the tissues to androgens.

Role of the adenylate cyclase system in altered insulin release from islets of Langerhans of aging rats

1981 ◽  
Vol 96 (2) ◽  
pp. 222-226 ◽  
Author(s):  
Loren G. Lipson ◽  
Michael J. Bush ◽  
Gretchen E. Tietjen ◽  
Aeree Yoon
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Insulin Release ◽  
Islets Of Langerhans ◽  
Male Rats ◽  
Adenylate Cyclase System ◽  
Control Male ◽  
Aging Rats ◽  
Amp System ◽  
Old Rats

Abstract. In attempting to understand the causes of the hyperglycaemia observed in aging populations and to determine the mechanism(s) for the diminished in vitro insulin release from islets of Langerhans of older rats, the adenylate cyclase-cyclic AMP system was studied in isolated islets from 12 month old and 2½ month old (control) male rats to determine its role in this altered insulin secretion. Islets of Langerhans were isolated by collagenase digestion and then either incubated in the presence of low or high concentrations of glucose for studies of insulin release or were sonicated and assayed for determinations of activities of adenylate cyclase and phosphodiesterase. Insulin release was identical from islets of 12 month old and 2½ month old rats to 2.8 mm D-glucose, while in the presence of 16.7 mm D-glucose, insulin release was decreased by 33% (P < 0.02) from islets of the older animals. Adenylate cyclase activity was diminished by 60% (P < 0.005) from the 12 month old rats as compared with islets from the 2½ month old controls, while low Km phosphodiesterase activity was similar in islets from both groups of animals. From these studies it appears that the adenylate cyclase-cyclic AMP system may play a role in the altered insulin release from islets of aging rats.

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