Hormones and stress in birds: activation of the hypothalamo-pituitary-adrenal axis.
Explore the source record for details and available documents.
Animals↗
Biomedical subjects
S Harvey
Publications and source records attributed to S Harvey.
Developing a research team: involving staff nurses and students.
Explore the source record for details and available documents.
Clinical Nursing Research↗
Formation of cyclic enol ethers from a labile biological precursor: an example of analytical artifacts.
Three isomeric enol ethers are among those constituents apparently unique to mouse urine as identified by gas chromatographic analysis. These compounds appear to be artifacts arising from the cyclization and dehydration of 6-hydroxy-6-methyl-3-heptanone. Identification of the trimethylsilyl ether of 6-hydroxy-6-methyl-3-heptanone in the silylated ether extract of mouse urine indicates that the precursor keto alcohol is indeed present in the urine. Since similar heterocyclic compounds are often identified in urine samples analyzed by gas chromatography, formation of various analysis artifacts arising from analogous cyclization and dehydration reactions is likely.
Animals↗
Somatostatin inhibition of thyrotropin-releasing hormone- and growth hormone-releasing factor-induced growth hormone secretion in young and adult anesthetized chickens.
The present communication examines the influence of somatostatin (SRIF14) on basal and thyrotropin-releasing hormone (TRH)- or growth hormone-releasing factor (GRF)-induced GH secretion in young (6 week old) and adult male chickens. Studies were performed in sodium pentobarbitone-anesthetized chickens where basal plasma concentrations of GH are low and both TRH and GRF consistently stimulate GH release. In both young and adult chickens, basal GH secretion was reduced by SRIF14 infusion (3 micrograms/kg/min). Similarly, in adult and young birds, the GH secretory response to a challenge with a GRF bolus (10 micrograms/kg) was inhibited by the concomitant intravenous infusion of SRIF14 (0.3 or 3.0 micrograms/kg/min). In adult chickens, the GH response to TRH (10 micrograms/kg) was suppressed (by 93%) by SRIF14 infusion (3 micrograms/kg/min) and tended to be inhibited (by 29%) by a lower dose of SRIF14 (0.3 micrograms/kg/min). In contrast, in young chicks, GH release following TRH challenge (either 1 or 10 micrograms/kg) was only partially inhibited by SRIF14 infusion (3 micrograms/kg/min). The response to a TRH challenge (10 micrograms/kg) was unaffected by the low dosage of SRIF14 infusion (0.3 micrograms/kg/min). It is concluded that SRIF14 inhibits both GRF- and TRH-stimulated GH release in young and adult chickens.
Aging↗
Calcitonin gene-related peptide in neural tissues: a phylogenetic study.
A heterologous radioimmunoassay using a rabbit antiserum raised against human calcitonin gene-related peptide (CGRP) was used to measure levels of immunoreactive CGRP (IR-CGRP) in the brain, pituitary, and spinal cord in species representing all classes of vertebrates from cyclostomes to mammals, except amphibians. All the brain extracts except those from the trout, goldfish, and iguana demonstrated the presence of IR-CGRP. Pituitary extracts from all animals, except the ratfish, goldfish and trout, contained IR-CGRP. CGRP was present in all classes of animals tested and seems to be highly conserved in the nervous system, where it may act as a neurotransmitter or neuromodulator.
Animals↗
Thyroid function in sex-linked and autosomal dwarf chickens.
Thyrotropin-releasing hormone (TRH) and thyrotropin (TSH) elevated plasma thyroxine (T4) and triiodothyronine (T3) concentrations in a (euthyroid) control line of chickens and in an autosomal dwarf strain. These agents were ineffective in sex-linked dwarf (SLD) chickens. Similarly, while somatostatin (SRIF) lowered plasma T4 and T3 concentrations in autosomal dwarf (ADW) chickens and controls, it had no inhibitory effect in the SLD strain. These results suggest that an impairment in the hypothalamus-pituitary-thyroid axis is at least partly responsible for hypothyroidism in the SLD strain.
Animals↗
Effect of estrogen on calcium homeostasis and pituitary hormones in the growing chick.
An experiment was carried out to investigate the effect of a range of estradiol (E2) doses (0.1-6.5 micrograms/g body wt/day) on vitamin D metabolism and the plasma levels of growth hormone (GH) and prolactin (PRL) in the growing chick. Doses of 0.5-0.7 microgram/g E2, which are insufficient to raise the plasma calcium level, did induce an increase in growth rate, an increase in 25-hydroxyvitamin D 1 alpha-hydroxylase (1-hydroxylase) and 24-hydroxylase activities, and an increase in plasma GH level. These parameters leveled off or fell over the dose range 1-2 micrograms/g E2 but there was evidence of a second peak in 1-hydroxylase activity at 6 micrograms/g E2. At this high dose rate, the plasma Ca level rose to 8 mM, as it does in the laying hen; 24-hydroxylase activity, growth rate, and plasma GH and plasma PRL levels all decreased. It was concluded that the dose response to estrogen in the growing chick is not linear and, in the case of 1-hydroxylase activity, may even be biphasic.
Animals↗
Triiodothyronine inhibition of thyrotropin-releasing hormone- and growth hormone-releasing factor-induced growth hormone secretion in anesthetized chickens.
The ability of triiodothyronine (T3) to reduce basal and secretagogue-induced growth hormone (GH) release was examined in anesthetized young and adult male chickens. Infusion of T3 had no effect on basal plasma concentrations of GH in either young or adult chickens. However, GH secretion following challenge with either thyrotropin-releasing hormone (TRH) or growth hormone-releasing hormone (GRF) was reduced, in a dose-dependent manner, by the infusion of T3. In vivo sensitivity to T3 inhibition was greater with TRH- than GRF-stimulated GH release in either young (ED50 for TRH-induced GH release, 0.34 microgram T3/kg/min; ED50 for GRF-induced GH release, 0.49 microgram T3/kg/min) or adult chickens (ED50 for TRH-induced GH release, 0.11 microgram T3/kg/min; ED50 for GRF-induced GH release 1.89, micrograms T3/kg/min). Moreover, there was an increase in sensitivity of TRH-induced GH release to T3 with age.
Animals↗
Growth hormone and somatostatin in the plasma of transiently diabetic ducks: basal variation and response to glucose.
In the duck, subtotal pancreatectomy induces a transient diabetes, with decreased insulin and glucagon basal levels as well as responses to glucose. At the same time, a transient increase in basal peripheral somatostatin occurs, followed by an increase in growth hormone in the postdiabetic state. Intravenous glucose induces a slight decrease in somatostatin secretion in normal, but not in diabetic animals, and no significant variation in growth hormone secretion at any state. An obvious role of growth hormone or somatostatin in the development of this transient diabetes in the duck could not be detected in this study.
Animals↗
Androgens affect the processing of secretory protein precursors in the guinea pig seminal vesicle. I. Evidence for androgen-regulated proteolytic processing.
The guinea pig seminal vesicle epithelium synthesizes and secretes four major secretory proteins (SVP-1-4). Previous work has established that these four proteins are cleaved from two primary translation products in a complex series of protein processing reactions. The present studies suggest that these protein processing reactions are regulated by androgens. In vitro labeling of seminal vesicle proteins revealed significant differences in the patterns of secretory protein intermediates produced by tissue from intact and castrated animals. Seminal vesicle tissue explants from castrated animals secreted a subset of the processing intermediates secreted by tissue from intact animals. The changes in the patterns of secretory protein intermediates became more pronounced with increasing time after castration, and were fully reversible by treatment of castrated animals with testosterone, suggesting that androgens were affecting the processing or secretion of secretory protein precursors. Amino-terminal protein sequencing of secretory protein processing intermediates that accumulate in the seminal vesicle lumen after castration suggests that the guinea pig seminal vesicle contains an androgen-regulated proteolytic processing activity.
Animals↗
Androgens affect the processing of secretory protein precursors in the guinea pig seminal vesicle. II. Identification of conserved sites for protein processing.
The guinea pig seminal vesicle epithelium is an androgen-dependent tissue that synthesizes and secretes four major secretory proteins (SVP-1, SVP-2, SVP-3, and SVP-4). Sequencing of near full-length cDNA clones corresponding to the two most abundant mRNAs produced by the seminal vesicle reveals that all four secretory proteins are cleaved from two secretory protein precursors. Amino acid sequences from purified SVP-2 match the central region of the predicted amino acid sequences from the smaller cDNA clone, GP2 (581 nucleotides). Similar analysis demonstrates that the predicted amino acid sequence from the longer cDNA clone, GP1 (1368 nucleotides), codes for the related proteins SVP-3 and SVP-4 as well as SVP-1. The 43.2 kilodalton polyprotein precursor coded by GP1 contains two different sets of 24 amino acid tandemly repeated sequences. The two secretory protein precursors have extensive regions of peptide sequence homology, particularly in regions where protein processing must occur to produce the mature secretory proteins. Analysis of the predicted secondary structure of the two precursor polypeptides revealed a strong correlation between structural features and sites of protein processing.
Amino Acid Sequence↗
Thyrotrophin-releasing hormone (TRH)-induced growth hormone secretion in fowl: binding of TRH to pituitary membranes.
Heat-labile specific binding sites for [3H]3-methylhistidine2-TRH [( 3H]Me-TRH) were demonstrated on chicken adenohypophysial membranes. These binding sites were of both high affinity (dissociation constant, Kd = 15.53 nM) and low capacity (maximum binding capacity, Bmax = 8.73 pmol/g tissue) and of low affinity (Kd = 104.5 nM) and high capacity (Bmax = 32.41 pmol/g). Binding of [3H]Me-TRH to the pituitary membranes was greater at 4 degrees C than at 39 degrees C and occurred with rate constants (k1) of 1.6 x 10(6) and 3.39 x 10(6) M-1 min-1 respectively. Dissociation of [3H]Me-TRH binding at 4 degrees C occurred with a rate constant (k-1) of 0.125 min-1. Binding sites for [3H]Me-TRH were found in the cephalic lobe of the pituitary gland (the location of most lactotrophs and thyrotrophs) and in the caudal lobe (the location of most somatotrophs). The number of binding sites was greater in the caudal lobe than in the cephalic lobe, although the affinity of [3H]Me-TRH binding did not differ. The binding of [3H]Me-TRH to caudal lobe membranes was displaced by Me-TRH, TRH, pGlu-His-Pro-Gly-NH2 and [Glu1]-TRH, with half-maximal effective doses of 33 nM, 70.7 nM, 1.23 microM and 22 microM respectively, but not by [Phe2]-TRH, TRH free acid or His-Pro-diketopiperazine. The number of caudal lobe binding sites for [3H]Me-TRH in old birds was less than that in young ones, and the number of binding sites was increased in birds deprived of food for 48 h. TRH-induced GH secretion in birds would thus appear to be mediated by specific receptors on caudal lobe somatotrophs, and these results suggest that physiological changes in GH secretion (during growth and periods of fasting) are causally related to the abundance of TRH-binding sites.
Animals↗
Thyrotrophin-releasing hormone induces growth hormone secretion in adult hypothyroid fowl.
While thyrotrophin-releasing hormone (TRH) stimulated growth hormone (GH) secretion in adult anesthetized cockerels, the GH response was blocked in anesthetized birds pretreated with thyroxine (T4) or triiodothyronine (T3). Moreover, whereas GH secretion in conscious adult birds was poorly responsive to TRH stimulation, conscious birds made hypothyroid by goitrogen pretreatment (with propylthiouracil, methimazole, or thiourea) were responsive to TRH challenge. Basal circulating GH concentrations in the goitrogen-pretreated birds were also higher than in the vehicle-injected controls. Surgical thyroidectomy similarly increased the basal GH concentration in adult birds and promoted TRH-induced GH secretion. These results demonstrate inhibitory effects of the thyroid hormones on basal and stimulated GH secretion in adult domestic fowl and suggest that GH release in adults is partly under tonic thyroidal inhibition.
Animals↗
Characterization of antisera raised against hypocalcin (teleocalcin) purified from corpuscles of Stannius of rainbow trout, Salmo gairdneri.
Highly specific antisera were raised against hypocalcin, a 54-kDa glycoprotein purified from the corpuscles of Stannius (CS) of rainbow trout, Salmo gairdneri. The specificity of the antisera was determined by using Ouchterlony's double immunodiffusion test, radioimmunoassay (RIA), enzyme-linked immunosorbent assay (ELISA), and immunocytochemistry. In the double immunodiffusion test, a single precipitin line was formed between the antisera and hypocalcin. Both RIA and ELISA studies showed that serial dilutions of hypocalcin, teleocalcin, and CS extracts produced dose-response curves, whereas rat FSH, chicken LH, bovine TSH, salmon calcitonin, bovine parathyroid hormone, and human angiotensins I and II failed to cross-react with the antiserum. Immunoreactive hypocalcin was demonstrated in the plasma of a teleost (flounder), but not of an elasmobranch (dogfish). In the immunocytochemistry, most of the gland cells showed strong immunoreaction with the antisera, whereas some cells displayed no immunoreactivity.
Animals↗
Stimulation of corticosterone release in the fowl by recombinant DNA-derived chicken growth hormone.
The effects of recombinant DNA-derived chicken growth hormone (rcGH) on plasma corticosterone in young broiler cockerels were investigated. A single injection of 200 micrograms/kg rcGH significantly increased plasma corticosterone concentrations 2 hr (but not 20 or 40 min) after treatment. Administration of 10 or 100 micrograms/kg rcGH also significantly increased plasma corticosterone levels after 2 hr, with the higher dose eliciting greater responses. Chronic treatment with seven daily injections of the same doses of rcGH gave similar increases in plasma concentrations of corticosterone. No obvious difference in magnitude of plasma corticosterone was observed between acute and chronic exposure to rcGH. In a further experiment in which serial blood sampling was performed after a single injection or five daily injections of vehicle or 200 micrograms/kg rcGH, there were significant increases in plasma corticosterone concentrations 40 min after acute rcGH treatment and 40 and 80 min after chronic treatment when compared with plasma corticosterone concentrations of vehicle-injected controls. However, the increases could have incorporated a stress response due to repeated sampling because the control birds also showed elevated plasma corticosterone concentrations. The corticosterone response did not diminish with repeated GH challenge. These results suggest that GH may play a role in the acute regulation of corticosterone secretion in intact chickens.
Animals↗
Thyrotrophin-releasing hormone-induced growth hormone secretion in ducks: independence of peripheral plasma somatostatin, insulin, and glucagon.
In young, but not old, ducks the iv infusion of thyrotrophin-releasing hormone (TRH) markedly increased peripheral plasma growth hormone (GH) concentrations, which remained elevated throughout the 30-min period of infusion. This GH response to TRH was suppressed by the simultaneous infusion of somatostatin, which increased the level of circulating somatostatin-like immunoreactivity (SLI) to supraphysiological levels. Basal concentrations of plasma SLI in both young and old birds were suppressed by TRH infusion. Concentrations of glucagon-like immunoreactivity (GLI) were increased by the infusion of TRH in young birds but not in adults, whereas plasma immunoreactive insulin (IRI) was decreased in young birds and increased in adults following TRH infusion. These results indicate that TRH-induced GH secretion in ducks is unrelated to changes in peripheral plasma SLI, GLI, or IRI induced by TRH infusion.
Aging↗
Calcitonin gene-related peptide in the bullfrog, Rana catesbeiana: localization and vascular actions.
Calcitonin gene-related peptide (CGRP) was found using radioimmunoassay in the brain and spinal cord of the bullfrog, Rana catesbeiana. The brain extracts were found to contain 241.7 +/- 68.1 pg/mg tissue, and the spinal cord contained 1753.0 +/- 96.8 pg/mg tissue. An intense immunocytochemical reaction was observed in the dorsal spinal cord. Vascular studies using helical strips of the dorsal aorta, iliac artery, and femoral artery showed CGRP to exert a vasorelaxant effect which was most pronounced in the femoral artery and minimal in the aorta. As in the rat, CGRP was shown to exert its vasorelaxant effect by inhibiting the mobilization of intracellular calcium.
Animals↗
The effect of low levels of dietary protein and calcium on growth rate, growth hormone, and vitamin D metabolism in the chick.
Two experiments were carried out on 2-week-old chicks in which they were fed protein-deficient diets for varying lengths of time with or without calcium (Ca). All deficient diets depressed the rate of growth; this depression was more marked in chicks fed the protein-deficient diet for 21/2 days than in those fed the diet for 4 days. The circulating growth hormone level was high in all protein-deficient diets but low in the diet only deficient in calcium. The low Ca-induced-rise in renal vitamin D, 1-hydroxylase activity was reduced, and the plasma Ca level was particularly low, in chicks on the low protein/low Ca diet. The 24-hydroxylase activity was high on the low protein diets. It was concluded that adaptation to a low protein diet occurs over the first 4 days and that this may be associated with the high growth hormone level and also that adequate dietary protein is essential for maximal adaptation to dietary Ca deficiency.
24,25-Dihydroxyvitamin D 3↗