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, Henquin 2000 ). The hypothalamic neuropeptide corticotropin-releasing hormone (CRH) plays a central role in the mammalian response to stress and exerts a wide range of roles in the brain (e.g., mediating anxiety behavior) and peripheral tissues (e
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Department of Anatomy, Semmelweis University, Budapest, Hungary
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Department of Neuroscience, Karolinska Institutet, Stockholm, Sweden
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contain all mRNAs for the protein domain sustaining the regulated release of any neurotransmitter or neuroactive modulator. Here, we will review recent data on corticotropin-releasing hormone (CRH) mRNA -containing neurons in the mammalian hypothalamus to
Department of Biological Chemistry, University of Michigan, 109 Zina Pitcher Place, BSRB Room 5035, Ann Arbor, Michigan 48109, USA
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Department of Psychiatry, University of Michigan, 109 Zina Pitcher Place, BSRB Room 5035, Ann Arbor, Michigan 48109, USA
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Introduction Corticotropin-releasing hormone (CRH) is a key regulator of the endocrine, behavioral, and autonomic components of the mammalian stress response. Within the endocrine hypothalamic–pituitary–adrenal axis, this 41-amino acid peptide is
Department of Respiratory and Sleep Medicine, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
Neonatal Intensive Care Unit, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
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Department of Respiratory and Sleep Medicine, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
Neonatal Intensive Care Unit, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
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Department of Respiratory and Sleep Medicine, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
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Department of Respiratory and Sleep Medicine, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
Neonatal Intensive Care Unit, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
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Department of Respiratory and Sleep Medicine, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
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Department of Respiratory and Sleep Medicine, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
Neonatal Intensive Care Unit, Hunter Medical Research Institute, Newcastle, New South Wales, Australia
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Pathology 191 434 –442. Aguilera G , Nikodemova M, Wynn PC & Catt KJ 2004 Corticotropin releasing hormone receptors: two decades later. Peptides 25 319 –329. Algotsson A , Nordberg A
Department of Biological Pharmacy, School of Pharmacy, Shujitsu University, Okayama 703-8516, Japan
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Department of Biological Pharmacy, School of Pharmacy, Shujitsu University, Okayama 703-8516, Japan
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Department of Biological Pharmacy, School of Pharmacy, Shujitsu University, Okayama 703-8516, Japan
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Department of Biological Pharmacy, School of Pharmacy, Shujitsu University, Okayama 703-8516, Japan
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Department of Biological Pharmacy, School of Pharmacy, Shujitsu University, Okayama 703-8516, Japan
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corticosterone levels ( Pulichino et al. 2003 b ). Hypothalamic corticotropin-releasing hormone (CRH) stimulates transcription of POMC and secretion of ACTH in vivo ( Bruhn et al. 1984 ), in cultured anterior pituitary cells ( Loeffler et al
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Corticotropin-releasing hormone (CRH) has been shown to inhibit proliferation and modulate expression of inflammation markers in the epidermal cells. In the present study we report that CRH also stimulates nuclear factor-kappa B (NF-kappaB) activity. Incubation with CRH of human keratinocytes derived from primary cultures resulted in increased binding of DNA by NF-kappaB. CRH induced translocation of NF-kappaB subunit p65 from the cytoplasm to the nucleus and induced expression of kappaB-driven chloramphenicol acetyltransferase (CAT) reporter gene. NF-kappaB translocation was accompanied by degradation of the inhibitor of NF-kappaB alpha (IkappaB-alpha). Specificity of the CRH effect was demonstrated by the use of CRH-R antagonists antalarmin and alpha-helical CRH [9-41]. CRH-dependent stimulation of NF-kappaB activity is consistent with accumulated data about role of this neuropeptide in the regulation of local epidermal homeostasis.
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Corticotropin-releasing hormone (CRH) plays multiple roles in vertebrate species. In mammals, it is the major hypothalamic releasing factor for pituitary adrenocorticotropin secretion, and is a neurotransmitter or neuromodulator at other sites in the central nervous system. In non-mammalian vertebrates, CRH not only acts as a neurotransmitter and hypophysiotropin, it also acts as a potent thyrotropin-releasing factor, allowing CRH to regulate both the adrenal and thyroid axes, especially in development. The recent discovery of a family of CRH-like peptides suggests that multiple CRH-like ligands may play important roles in these functions. The biological effects of CRH and the other CRH-like ligands are mediated and modulated not only by CRH receptors, but also via a highly conserved CRH-binding protein (CRH-BP). The CRH-BP has been identified not only in mammals, but also in non-mammalian vertebrates including fishes, amphibians, and birds, suggesting that it is a phylogenetically ancient protein with extensive structural and functional conservation. In this review, we discuss the biochemical properties of the characterized CRH-BPs and the functional roles of the CRH-BP. While much of the in vitro and in vivo data to date support an 'inhibitory' role for the CRH-BP in which it binds CRH and other CRH-like ligands and prevents the activation of CRH receptors, the possibility that the CRH-BP may also exhibit diverse extra- and intracellular roles in a cell-specific fashion and at specific times in development is also discussed.
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Involvement of endogenous corticotropin releasing hormone (CRH) in the regulation of spontaneous growth hormone (GH) secretion was investigated. A CRH antagonist, α helical CRH 9–41, was intracerebroventricularly infused for 36 h at a rate of 1 μg/0·5 μl/h to freely moving, cannulated adult male rats. Serial blood samples were drawn every 20 min for the last 8 hours of α helical CRH 9–41 infusion. The treatment induced a marked increase in GH peak amplitude without affecting either trough levels or numbers of peaks. In parallel, levels of growth hormone releasing hormone (GHRH) mRNA in the arcuate nucleus, but not of somatotropin release inhibiting hormone (SRIH) mRNA in the periventricular and arcuate nuclei, were increased. These data suggest that, in addition to its action in the stress-induced inhibition of GH secretion through regulation of periventricular SRIH neurons, CRH can also act as a modulator of endogenous GH secretion through regulation of arcuate GHRH neurons. Whether the modulatory effects of CRH on GHRH neurons are direct or indirect remains to be established.
Journal of Endocrinology (1997) 152, 431–436
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Glucocorticoids regulate corticotropin-releasing hormone (CRH) gene expression in the placenta and the brain. In both the placenta and two extrahypothalamic sites in the brain (the amygdala and the bed nucleus of the stria terminalis), glucocorticoids elevate CRH gene expression. One functional role of the elevation of CRH by glucocorticoids may be to signal adversity. When CRH is over-expressed in the placenta, it may indicate that the pregnancy is in danger, and preterm labor may result. When CRH is over-expressed in the brains of animals, they may become more fearful. Both situations possibly reflect allostatic mechanisms and vulnerability to allostatic overload, a condition in which biological tissue may be compromised.
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High concentrations (up to 600 pg/ml) of corticotropin-releasing hormone (CRH) were detected in plasma of the teleost fish Oreochromis mossambicus (tilapia) when screening peripheral tissues of tilapia exposed to stress. Notably, the plasma CRH response to stressors in tilapia is much more pronounced than that in higher vertebrates, such as rats. After characterisation by RIA, by spiking plasma with synthetic tilapia CRH and by methanol-acid extraction, it is concluded that the immunoreactive (ir) material in plasma represents tilapia CRH(1-41). Results indicate that a CRH-binding protein is absent in tilapia plasma. Unstressed fish had plasma CRH levels under the limit of detection (<2 pg/ml), but following capture stress plasma CRH levels (170-300 pg/ml) as well as plasma cortisol levels (120 ng/ml) increased rapidly to plateau levels, which were reached after approximately 5 min. Tilapia CRH(1-41) tested at concentrations between 10(-11) and 10(-7) M in vitro did not stimulate the cortisol release from interrenal tissue. Also pretreatment of interrenal tissue with 10(-9) M CRH did not sensitise the cortisol-producing cells to a subsequent ACTH challenge. Forty-eight hours of net confinement or 48 h of cortisol treatment abolished the plasma CRH response and cortisol response to capture stress. The rapidity of the plasma CRH response and its inhibition after 48 h of stress or cortisol treatment point to release by central nervous tissue. Therefore the distribution of glucocorticoid receptors (GRs) in the brain and pituitary of tilapia was investigated. Main GR-ir cell clusters were found in the medial part (Dm) and posterior part of the dorsal telencephalon, in the preoptic region, in the inferior lobe of the hypothalamus and in the cerebellum. We conclude from comparison of CRH brain contents of unstressed and stressed fish that plasma CRH was released by CRH-ir cells located in the lateral part of the ventral telencephalon (Vl), and suggest that the cortisol feedback on CRH release by Vl is mainly exerted via the forebrain Dm region. We propose that CRH is mobilised during stress to fulfil peripheral functions, such as the regulation of circulating leukocytes or of cardiac output, as CRH receptors have been reported in these organs for fish species.
