PubMed Health⌕ Search

Biomedical subjects

R J Denver

Publications and source records attributed to R J Denver.

At least 19 recordsLinked to original sources
PubMed2001

Biochemical characterization and expression analysis of the Xenopus laevis corticotropin-releasing hormone binding protein.

Corticotropin-releasing hormone (CRH) plays a key role in the regulation of responses to stress. The presence of a high affinity binding protein for CRH (CRH-BP) has been reported in mammals. We have characterized the biochemical properties and expression of CRH-BP in the South African clawed frog, Xenopus laevis. Apparent inhibition constants (K(i[app])) for different ligands were determined by competitive binding assay. Xenopus CRH-BP (xCRH-BP) exhibited a high affinity for xCRH (K(i[app])=1.08 nM) and sauvagine (1.36 nM). Similar to rodent and human CRH-BPs, the frog protein binds urotensin I and urocortin with high affinity, and ovine CRH with low affinity. RT-PCR analysis showed that xCRH-BP is expressed in brain, pituitary, liver, tail, and intestine. Brain xCRH-BP mRNA is expressed at a relatively constant level throughout metamorphosis and increases slightly in the metamorphic frog. By contrast, the gene is strongly upregulated in the tail at metamorphic climax. Thus, regulation of xCRH-BP gene expression is tissue specific. Because xCRH-BP binds CRH-like peptides with high affinity the protein may regulated, the bioavailability of CRH in amphibia as it does in mammals.

Amino Acid Sequence↗
PubMed2001

Sublethal effects of chronic exposure to an organochlorine compound on northern leopard frog (Rana pipiens) tadpoles.

Global contamination with organochlorine compounds (OCs) has posed developmental and reproductive problems in wildlife worldwide. However, little is known about the impact of OCs or other pollutants on amphibians, despite mounting concerns about amphibian population declines and developmental deformities in the wild. Wildlife populations may be affected critically by sublethal impacts of anthropogenic disturbances, yet little research has focused on such effects in amphibians. In the current study, northern leopard frog (Rana pipiens) tadpoles were chronically exposed to a polychlorinated biphenyl (PCB) congener, 77-TCB, and effects on behavior, morphology, competitive performance, and corticosterone content were determined. R. pipiens activity levels and feeding rates were decreased by 77-TCB exposure, but morphology of mouthparts and body proportions were unaffected. 77-TCB enhanced growth and altered competitive interactions between R. pipiens and wood frog (Rana sylvatica) tadpoles. R. pipiens tadpoles exposed to 77-TCB showed decreased whole-body corticosterone content compared to controls both before and after injection with adrenocorticotropic hormone (ACTH). All of the factors examined in the current study play critical roles in tadpole development, growth, survivorship, and eventual reproductive success, suggesting negative population-level consequences for amphibians in PCB-contaminated habitats.

Animals↗
PubMed1999

Basic transcription element-binding protein (BTEB) is a thyroid hormone-regulated gene in the developing central nervous system. Evidence for a role in neurite outgrowth.

Thyroid hormone (3,5,3'-triiodothyronine; T(3)) is essential for normal development of the vertebrate brain, influencing diverse processes such as neuronal migration, myelin formation, axonal maturation, and dendritic outgrowth. We have identified basic transcription element-binding protein (BTEB), a small GC box-binding protein, as a T(3)-regulated gene in developing rat brain. BTEB mRNA levels in cerebral cortex exhibit developmental regulation and thyroid hormone dependence. T(3) regulation of BTEB mRNA is neural cell-specific, being up-regulated in primary cultures of embryonic neurons (E16) and in neonatal astrocytes (P2), but not in neonatal oligodendrocytes (P2). T(3) rapidly up-regulated BTEB mRNA in neuro-2a cells engineered to express thyroid hormone receptor (TR) beta1 but not in cells expressing TRalpha1, suggesting that the regulation of this gene is specific to the TRbeta1 isoform. Several lines of evidence support a transcriptional action of T(3) on BTEB gene expression. Overexpression of BTEB in Neuro-2a cells dramatically increased the number and length of neurites in a dose-dependent manner suggesting a role for this transcription factor in neuronal process formation. However, other T(3)-dependent changes were not altered; i.e. overexpression of BTEB had no effect on the rate of cell proliferation nor on the expression of acetylcholinesterase activity.

Animals↗
PubMed1999

Evolution of the corticotropin-releasing hormone signaling system and its role in stress-induced phenotypic plasticity.

Developing animals respond to variation in their habitats by altering their rates of development and/or their morphologies (i.e., they exhibit phenotypic plasticity). In vertebrates, one mechanism by which plasticity is expressed is through activation of the neuroendocrine system, which transduces environmental information into a physiological response. Recent findings of ours with amphibians and of others with mammals show that the primary vertebrate stress neuropeptide, corticotropin-releasing hormone (CRH), is essential for adaptive developmental responses to environmental stress. For instance, CRH-dependent mechanisms cause accelerated metamorphosis in response to pond-drying in some amphibian species, and intrauterine fetal stress syndromes in humans precipitate preterm birth. CRH may be a phylogenetically ancient developmental signaling molecule that allows developing organisms to escape deleterious changes in their larval/fetal habitat. The response to CRH is mediated by at least two different receptor subtypes and may also be modulated by a secreted binding protein.

Animals↗
PubMed1998

Hormonal correlates of environmentally induced metamorphosis in the Western spadefoot toad, Scaphiopus hammondii.

Tadpoles of several amphibian species have been shown to accelerate metamorphosis when their ponds dry. To understand the proximate mechanisms that mediate the developmental response to pond drying, I analyzed changes in endocrine activity in tadpoles of the Western spadefoot toad (Scaphiopus hammondii) exposed to experimental water volume reduction in the laboratory. Tadpoles exposed to a declining water level accelerated metamorphosis compared with tadpoles raised in a constant high water environment. The acceleration of development was associated with the precocious elevation of whole-body contents of the hormones that control metamorphosis, the thyroid hormones thyroxine (T4) and triidothyronine (T3), and the interrenal steroid corticosterone (CORT). The precocious activation of the thyroid system preceded external morphological change (i.e., increase in hind limb length, developmental stage) by 3 days. To test if tadpoles are capable of responding rapidly to water volume reduction, mid-prometamorphic tadpoles (Gosner Stage 37-38) were raised in a constant high water environment (10 L) and then transferred to either 1 or 10 L. Tadpoles transferred to 1 L exhibited significant metamorphic changes by 48 h after transfer. In addition, dramatic elevations in whole-body T4, T3, and CORT contents were evident at this time point. Thus, the metamorphic response to pond drying is likely driven by the activation of the thyroid and interrenal axes, the hormones of which control metamorphosis. Furthermore, this response is rapid, occurring within 48 h after exposure to the desiccating environment.

Animals↗
PubMed1998

The molecular basis of thyroid hormone-dependent central nervous system remodeling during amphibian metamorphosis.

Tadpole metamorphosis involves a coordinated series of changes in virtually every tissue of the body. This developmental process is induced by the single morphogen, thyroid hormone (TH). The amphibian central nervous system (CNS) is a primary target for TH, and it undergoes dramatic morphological and cytoarchitectural changes in response to the hormone. TH acts by regulating gene expression and its actions in metamorphosis are thought to result from its ability to induce tissue-specific genetic programs. Receptors for TH are ligand-dependent transcription factors whose mRNA expression is upregulated by TH during metamorphosis (receptor autoinduction). Studies on the tadpole CNS have identified four general classes of early TH response genes. These genes code for: (1) transcription factors, that are likely to be required for the expression of downstream genes (i.e. secondary response genes), (2) cellular enzymes, which carry out hormone conversions, energy transformations and may possibly mediate extranuclear effects of TH on neural cells, (3) cytoskeletal elements required for axonal development, and (4) secreted signaling molecules that control the production of TH. Recent studies suggest a critical, evolutionarily conserved role for the TH-induced transcription factor genes in controling neural cell proliferation and differentiation.

Amphibians↗
PubMed1997

Thyroid hormone-dependent gene expression program for Xenopus neural development.

Although thyroid hormone (TH) plays a significant role in vertebrate neural development, the molecular basis of TH action on the brain is poorly understood. Using polymerase chain reaction-based subtractive hybridization we isolated 34 cDNAs for TH-regulated genes in the diencephalon of Xenopus tadpoles. Northern blots verified that the mRNAs are regulated by TH and are expressed during metamorphosis. Kinetic analyses showed that most of the genes are up-regulated by TH within 4-8 h and 13 are regulated by TH only in the brain. All cDNA fragments were sequenced and the identities of seven were determined through homology with known genes; an additional five TH-regulated genes were identified by hybridization with known cDNA clones. These include five transcription factors (including two members of the steroid receptor superfamily), a TH-converting deiodinase, two metabolic enzymes, a protein disulfide isomerase-like protein that may bind TH, a neural-specific cytoskeletal protein, and two hypophysiotropic neuropeptides. This is the first successful attempt to isolate a large number of TH-target genes in the developing vertebrate brain. The gene identities allow predictions about the gene regulatory networks underlying TH action on the brain, and the cloned cDNAs provide tools for understanding the basic molecular mechanisms underlying neural cell differentiation.

Animals↗
PubMed1997

Environmental stress as a developmental cue: corticotropin-releasing hormone is a proximate mediator of adaptive phenotypic plasticity in amphibian metamorphosis.

Environmentally induced phenotypic plasticity allows developing organisms to respond adaptively to changes in their habitat. Desert amphibians have evolved traits which allow successful development in unpredictable environments. Tadpoles of these species can accelerate metamorphosis as their pond dries, thus escaping mortality in the larval habitat. This developmental response can be replicated in the laboratory, which allows elucidation of the underlying physiological mechanisms. Here I demonstrate a link between a classical neurohormonal stress pathway (involving corticotropin-releasing hormone, CRH) and the developmental response to habitat desiccation. Injections of CRH-like peptides accelerated metamorphosis in western spadefoot toad tadpoles. Conversely, treatment with two CRH antagonists, the CRH receptor antagonist alpha-helical CRH(9-41) and anti-CRH serum, attenuated the developmental acceleration induced by habitat desiccation. Tadpoles subjected to habitat desiccation exhibited elevated hypothalamic CRH content at the time when they responded developmentally to the declining water level. CRH injections elevated whole-body thyroxine, triiodothyronine, and corticosterone content, the primary hormonal regulators of metamorphosis. In contrast, alpha-helical CRH(9-41) reduced thyroid activity. These results support a central role for CRH as a neurohormonal transducer of environmental stimuli into the endocrine response which modulates the rate of metamorphosis. Because in mammals, increased fetal/placental CRH production may initiate parturition, and CRH has been implicated in precipitating preterm birth arising from fetal stress, this neurohormonal pathway may represent a phylogenetically ancient developmental regulatory system that allows the organism to escape an unfavorable larval/fetal habitat.

Animals↗
PubMed1994

Pancreatic hormones differentially regulate insulin-like growth factor (IGF)-I and IGF-binding protein production by primary rat hepatocytes.

We investigated the influence of and interactions among pancreatic hormones on the secretion of insulin-like growth factor-I (IGF-I) and IGF-binding proteins (IG-FBPs) by treating primary hepatocytes from young male Long-Evans rats with insulin or glucagon in combination with rat GH (rGH). The concentration of IGF-I secreted into the medium was estimated by radioimmunoassay after formic acid-acetone cryoextraction, and secreted IGFBPs were analysed by Western ligand blot and immunoblot; accumulation of IGF-I mRNA was analysed by Northern blot. Both insulin (0.1-100 nmol/l) and rGH (0.5, 5 and 50 pmol/l) produced a dose-dependent stimulation of IGF-I secretion over a 24-h incubation period. In contrast, glucagon (0.1-100 nmol/l) inhibited IGF-I production in a dose-related manner. Glucagon (10 nmol/l) also inhibited IGF-I secretion stimulated by rGH (5 pmol/l) and insulin (10 nmol/l). Northern blot analysis of total RNA isolated from rat hepatocytes revealed that rGH (5 pmol/l) elevated IGF-I mRNA levels, glucagon (10 nmol/l) alone had no effect on this parameter, but glucagon significantly reduced IGF-I transcript accumulation in response to rGH. IGFBPs secreted by rat hepatocytes run in two molecular weight ranges on SDS-PAGE: approximately 25 kDa (IGFBP-4) and approximately 29-31 kDa (IGFBP-1 and -2); the predominant hormonally regulated IGFBP was identified as IGFBP-1. Insulin produced a dose-dependent inhibition of production of IGFBP-1, while glucagon was stimulatory; when given together at an equivalent concentration (1 nmol/l), the effects of insulin were dominant to glucagon on IGFBP-1. These observations provide support for significant opposite roles for the pancreatic hormones, insulin and glucagon, in the regulation of liver IGF-I and IGFBP-1 production. As the production of pancreatic hormones is influenced by nutritional status, these polypeptides may mediate the effects of changing nutritional state on the hormonal control of protein anabolism and glucose homeostasis by directly influencing the circulating level of liver-derived IGF-I and its binding proteins.

Animals↗
PubMed1993

Acceleration of anuran amphibian metamorphosis by corticotropin-releasing hormone-like peptides.

Despite substantial information on the role of the pituitary-thyroid and pituitary-interrenal axes in controlling amphibian metamorphosis, the hypothalamic hormones responsible for controlling the activity of these axes have not been identified. The mammalian thyrotropin-releasing hormone (TRH) does not regulate the thyroid axis of tadpoles; however, corticotropin releasing hormone (CRH) stimulates the release of thyrotropin from bullfrog tadpole pituitary glands in vitro and may thus function as a central regulator of the thyroid axis during metamorphosis. I tested the possibility that a CRH-like peptide is involved in controlling amphibian development by treating tadpoles of two anuran species, the western spadefoot toad Scaphiopus hammondii, and the North American bullfrog, Rana catesbeiana, with neuropeptides and monitoring their effects on metamorphosis. Injection of spadefoot toad tadpoles with ovine (o) CRH (2 micrograms/animal every other day for 3 weeks) or the amphibian CRH-like peptide sauvagine (SV) significantly decreased their time from hatching to metamorphic climax (Gosner stage 42; frontlimb emergence) and their body weight and body length at climax compared with vehicle-injected controls; whereas, TRH had no effect and arginine vasotocin produced a small but significant lengthening of the larval period but did not alter body size at climax. In an acute response experiment, S. hammondii tadpoles (in Gosner stages 36-38--late prometamorphosis) treated with oCRH or SV (2 micrograms/animal) exhibited significantly elevated whole-body thyroxine (T4) content at 2 and 6 hr after injection; whereas, treatment with TRH (2 micrograms/animal) did not significantly alter whole-body T4. R. catesbeiana tadpoles treated with oCRH or SV (surgical implantation of ELVAX pellets impregnated with 100 micrograms peptide and injections of peptides at 5 micrograms/animal once every 3 days) exhibited accelerated spontaneous and triiodothyronine (T3)-induced metamorphosis as assessed by changes in tail height, hind limb development, and body weight; TRH had no effect. Injections of a pool of antisera generated against CRH-like peptides (rat/human CRH, oCRH, SV) slowed T3-induced metamorphosis when compared with normal serum-injected controls. These results support the hypothesis that a CRH-like peptide(s) is involved in the central control of metamorphosis of anuran amphibians, and may act, at least in part, through stimulation of the thyroid axis.

Animals↗
PubMed1991

Comparative survey of blood thyroxine binding proteins in turtles.

The nature of plasma thyroxine (T4) binding activity was surveyed in turtles; binding to [125I]T4 was measured on polyacrylamide gel electrophoresis--PAGE--and on minicolumns of Sephadex G-25. An electrophoretically distinct T4 binding protein was identified in all 8 species of Pseudemys studied and in 3 other genera (Chrysemys, Deirochelys, and Emyoidea) of the same family, Emydidae. Levels of this binding activity were highly variable among individuals, but they consistently showed a similar low relative mobility (Rf) compared to albumin, and a relatively low capacity was indicated by displacement with unlabeled T4. Two emydids (Terrapene, Clemmys) showed a similar slow migrating binding peak, but binding activity was low and not as easily displaced by unlabeled T4. T4 binding to albumins was minimal in most of these emydid species, even when binding to the higher affinity, low capacity component was low or displaced by unlabeled T4 (2.5 micrograms/ml). In contrast, there was no clear evidence for a similar high affinity, low capacity binding protein in any of the other 19 species representing 13 genera of 8 families from two suborders. In these species, binding activity on Sephadex G-25 was typically low and binding on PAGE was associated largely with albumin; binding levels for albumins were highly variable. In several nonemydids (from distant lineages), binding activity on Sephadex was elevated and PAGE showed a second binding protein distinct from albumin, but it had high capacity (not readily saturable). Thus, an evolutionary divergence in T4 transport proteins is suggested within Chelonia.

Animals↗
PubMed1991

Thyroidal inhibition of chicken pituitary growth hormone: alterations in secretion and accumulation of newly synthesized hormone.

Hypothyroidism reduces GH synthesis and release in several mammalian species, in which thyroid hormone directly stimulates GH gene transcription. In contrast, hypothyroidism stimulates GH secretion in birds, in which thyroid hormone directly inhibits pituitary GH release. We have, therefore, investigated the effects of thyroid status on the accumulation of newly synthesized GH in the pituitaries of 8- to 10-week-old Leghorn cockerels in vitro and in vivo. The incorporation of [35S]methionine into immunoprecipitable GH ([35S] GH) was increased, over a 4-h incubation period, in glands from birds made hypothyroid by injections of methimazole (50 mg/kg day for 10 days) in comparison with glands from vehicle-injected controls. Treatment with tri-iodothyronine (T3, 100 micrograms/kg per day for 10 days) in vivo did not significantly alter the accumulation of [35S]GH in vitro but did block the release of [35S]GH in response to a GH secretagogue (thyrotrophin-releasing hormone; exposure to 280 nmol/l for 30 min) and reduced immunoassayable pituitary GH content. Pretreatment of glands from euthyroid birds with T3 (100 nmol/l) in vitro (for 20 h) reduced the basal accumulation of [35S]GH as well as that induced by another GH secretagogue (GH-releasing factor; 100 nmol/l) during a 6-h labelling period. These results show that, unlike the generally stimulatory action of thyroid hormone in mammals, in birds, T3 exerts a direct inhibitory effect on the accumulation of newly synthesized pituitary GH.

Animals↗
PubMed1990

Relation of plasma thyroxine binding to thyroidal activity and determination of thyroxine binding proteins in a turtle, Pseudemys scripta.

The ability of plasma to bind thyroxine (T4) was examined in the turtle, Pseudemys scripta, in relation to variations in thyroidal state associated with age, sex, environment, and surgical and chemical manipulations. Relative plasma binding activity was assessed by use of binding to [125I]T4 on minicolumns of Sephadex G-25 (fine). Hypothyroidism induced by surgical thyroidectomy (Tx) or goitrogen (Methimazole) treatment resulted in a marked depression of plasma binding (50- to 100-fold) in juveniles, and T4 treatment restored binding after 4-6 weeks in long-term Tx animals and increased levels in intact animals. Among intact turtles or those made slightly hypothyroid by partial thyroidectomy, binding was consistently correlated with plasma T4. For example, juvenile turtles kept under continuous light and constant temperature (28 degrees) for 4.5 months showed a pronounced depression of plasma T4 (2.6 +/- 1.1 ng/ml) and binding capacity compared to animals raised under variable conditions (T4 = 69.6 +/- 22 ng/ml) for the last 2 months. Plasma T3 was less than 1 ng/ml in all cases. Binding levels in adult turtles were similar to juveniles, but females had significantly higher binding levels than males which paralleled differences in their plasma T4 (137 +/- 17.4 vs 83.9 +/- 13.8 ng/ml). These variations in binding were independent of total plasma protein and albumin. Plasma T4 binding measured on Sephadex G-25 was reversible and reduced by addition of exogenous T4. The affinity for T3 was 10- to 100-fold less than for T4. When plasma preincubated with [125I]T4 was electrophoresed on polyacrylamide slab gels (7% nonreducing) only a small percentage of radiolabel was associated with albumin and the majority with a slower migrating protein(s). Addition of unlabeled T4 displaced binding from the slower migrating region to the albumin and dye front (unbound). In contrast, plasma from Tx turtles showed only minimal binding and radiolabel was associated primarily with the albumin fraction. Elution of proteins from gels confirmed that only the slower migrating components bound T4 when tested on Sephadex G-25, and Tx animals lacked this binding component. The protein(s) responsible for most of the T4 binding appears to exist in low concentration. Limited comparative studies with human blood showed a similar binding activity on Sephadex G-25, but electrophoretic mobilities of binding proteins were distinct from those in the turtle. Evidence suggests that this binding protein is not prealbumin.(ABSTRACT TRUNCATED AT 400 WORDS)

Aging↗
PubMed1990

The role of hormone binding in the cold suppression of hormone stimulation of the pituitary, thyroid, and testis of the turtle.

The ability of hormones to bind to their functional receptors on turtle (Pseudemys scripta) endocrine target tissues in the cold was tested by treating tissues with secretagogues at low temperatures (5-15 degrees) and then following subsequent target stimulation in the absence of secretagogue at a warm temperature (28 degrees). Administration of thyrotropin-releasing hormone (TRH), corticotropin-releasing hormone, and growth hormone-releasing hormone to pituitaries at low temperatures (20 degrees or below) suppressed responses in growth hormone (GH) and thyrotropin (TSH) secretion and there was little or no response in pituitaries subsequent to warming. In contrast, gonadotropin-releasing hormone treatment of pituitaries, TSH treatment of thyroid glands, and gonadotropin (FSH and LH) treatment of testes in the cold (down to 5 degrees) was followed by a large response in the target glands (secretion of LH, thyroxine, and testosterone (T), respectively) following warming. Additional studies with FSH and LH showed that these hormones can bind to testes rapidly (within 5 min) at low temperatures where no acute response is observed, although the dose sensitivity and the extent of this priming in the cold are less than at warm temperatures. Thus, postreceptor events may be more important than binding per se for temperature effects on hormone responses of tissues, but even this component of cell function varies among tissues. The effects of a receptor-independent secretagogue (tetraethylammonium chloride), which causes cell depolarization by blocking K+ efflux, were also blocked at low temperatures in thyrotropes and somatotropes but not in gonadotropes. Rapid depressions in TSH and GH secretions following cooling of TRH-stimulated pituitaries and of T secretion in LH-stimulated testes provide further evidence for cold sensitivity of postreceptor processes in these tissues.

Animals↗
PubMed1990

Modulation of neuropeptide-stimulated pituitary hormone secretion in hatchling turtles.

Neuropeptides that have relatively narrow actions on mammalian pituitary secretion may have divergent effects on pituitary hormone secretion in ectothermal vertebrates. In turtles, secretion of both thyrotropin (TSH) and growth hormone (GH) can be stimulated in vitro by thyrotropin-releasing hormone (TRH) and by members of corticotropin-releasing hormone (CRH) and growth hormone-releasing hormone (GHRH) peptide families. To determine if these neuropeptides share common modes of action, and to study other potential regulators of the turtle pituitary, somatostatin-14 (SRIH) and monoamines were tested for direct effects on in vitro basal and neuropeptide-stimulated TSH and GH secretion. Pituitary glands from young turtles (Pseudemys scripta) were cultured in the presence of 25 nM TRH, ovine CRH, or rat GHRH with or without SRIH. Glands were incubated for several 2-hr periods in medium alone or in medium containing peptides. Preincubation for 4 hr with SRIH (6 or 60 nM) significantly reduced basal and TRH-stimulated TSH and GH output (SRIH present during entire incubation). In another experiment, basal hormone secretion was reduced when SRIH (60 nM) was present only during the 2-hr basal period; however, reduction of TSH and GH responses to TRH required the presence of SRIH (60 nM) during the basal period and the period of stimulation. TSH responses to 25 nM oCRH and rGHRH and GH responses to rGHRH were significantly reduced by preincubation with 60 nM SRIH. The biogenic amines, dopamine (DA), serotonin (5HT), and norepinephrine (NE) (50 or 500 nM) were tested for possible direct actions on basal and neuropeptide-stimulated pituitary TSH and GH secretion.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1990

Regulation of pituitary thyrotropin secretion.

The pituitary thyrotropin secreting cells of tetrapods share a common responsiveness to TRH, but the specificity of this response may differ among species. TSH responses in amphibians and reptiles appear to be somewhat less specific than in mammals, but each group differs in responsiveness to particular neuropeptides, and it is not clear that TRH is the main regulator of TSH in nonmammalian species. It is not yet known whether these diverse peptides are acting directly on the thyrotrope or possibly through a paracrine mechanism. A CRH-like peptide may be a common neuroregulator of the anuran thyroid and interrenal in metamorphosis. Inhibitory regulation including effects of neuropeptides and thyroid feedback at the pituitary level is evident in reptiles, but is not known for other nonmammalian groups. In ectotherms, the potential actions of temperature on TSH secretion must also be considered. In this regard, it is important to recognize that the thermal relations of the thyrotropin response may be distinct from other pituitary hormones, as well as other components of the hypothalamo-pituitary-thyroid axis (Licht et al., 1989).

Animals↗
PubMed1989

Temperature dependence of in vitro pituitary, testis, and thyroid secretion in a turtle, Pseudemys scripta.

In vitro culture was used to examine the direct actions of temperature at the level of pituitary hormone [luteinizing hormone (LH), thyrotropin (TSH), growth hormone (GH), prolactin (PRL)] responses to neuropeptides and two related peripheral endocrine responses [thyroid hormone (T4) and testicular androgen secretion] to pituitary hormones (TSH and gonadotropins) in a turtle, Pseudemys scripta. All these responses were fully suppressed at very low temperatures (5-6 degrees) and maximal near the species' preferred body temperature (28 degrees), but sensitivities differed markedly in intermediate ranges. At the pituitary level, the response of TSH, GH, and PRL to thyrotropin-releasing hormone (TRH) was considerably more temperature sensitive than the response of LH to gonadotropin-releasing hormone (GnRH) stimulation. TSH, GH, and PRL were unresponsive at 20 degrees or below, whereas LH secretion was stimulated almost equally between 12 and 28 degrees; the main effect of cooling on LH secretion was to reduce the duration of the response to GnRH. There was no clear effect of previous thermal history on temperature sensitivity of pituitary neuropeptide responsiveness although the general responsiveness of the gland was altered; however, these latter effects may also be related to variations in other factors such as photoperiod, season, and nutrition. Temperature sensitivities of the thyroid and testes also differed, but in the opposite way from the related pituitary cell types. Thyroid glands were relatively insensitive to temperature and responded to TSH between 12 and 32 degrees, with no difference between 20 and 28 degrees. In contrast, testicular androgen secretion showed an abrupt decline in gonadotropin responsiveness below 28 degrees; dose sensitivity, response rate, and maximal output were affected. Results were similar for sea turtle LH, snapping turtle LH, and ovine follicle-stimulating hormone. Thus, the temperature dependence of the two endocrine systems may have a different rate-limiting component.

Androgens↗