Cloning and functional pharmacology of two corticotropin-releasing factor receptors from a teleost fish

Pohl, Sigrun; Darlison, Mark G.; Clarke, W. Craig; Lederis, K.; Richter, Dietmar

doi:10.1016/s0014-2999(01)01391-7

Cited by 62 publications

(49 citation statements)

References 40 publications

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“…Peripheral actions of plasma CRH are consistent with the expression of CRH receptors in heart, gills (Pohl et al 2001) and spleen (Arai et al 2001) of fish. We have no evidence for direct actions of CRH or of CRH in combination with a subsequent ACTH pulse on the interrenal cells, but CRH could regulate circulating leukocytes during stress, as CRH stimulates activated peripheral leukocytes of channel catfish (Ictalurus punctatus) in vitro to secrete ACTH-ir (Arnold & Rice 2000).…”

Section: Functionsupporting

confidence: 67%

“…Also circulating CRH may regulate cardiac output during stress. In the catfish Ameiurus nebulosus (Arai et al 2001) and in salmon Oncorhynchus keta (Pohl et al 2001), CRH-R2 are most abundantly expressed peripherally in the atrium. In contrast to mammals the fish CRF-R1 and R2 receptors display similar affinities to U-I and to CRH (Arai et al 2001).…”

Section: Functionmentioning

confidence: 99%

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Corticotropin-releasing hormone in the teleost stress response: rapid appearance of the peptide in plasma of tilapia (Oreochromis mossambicus)

Pepels¹,

Helvoort²,

Bonga³

et al. 2004

Journal of Endocrinology

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High concentrations (up to 600 pg/ml) of corticotropinreleasing 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 . 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 cortisolproducing cells to a subsequent ACTH challenge. Fortyeight 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.

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Section: Functionsupporting

confidence: 67%

Section: Functionmentioning

confidence: 99%

Corticotropin-releasing hormone in the teleost stress response: rapid appearance of the peptide in plasma of tilapia (Oreochromis mossambicus)

Pepels¹,

Helvoort²,

Bonga³

et al. 2004

Journal of Endocrinology

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“…The cloned cDNAs encoded a receptor of 415 residues and a second splice variant with a 29-residue extension. Further cloning studies indicated that the CRH1 receptor showed a considerable structural variability and varied from 415 to over 440 residues (Arai et al 2001, Pohl et al 2001, Huising et al 2004, Hauger et al 2006. For example, the human CRH1 gene possesses 14 exons spanning 20 kb (Sakai et al 1998), whereas the rat gene possesses only 13 exons (Tsai-Morris et al 1996).…”

Section: Corticotrophinmentioning

confidence: 99%

MOLECULAR EVOLUTION OF GPCRS: CRH/CRH receptors

Lovejoy¹,

Chang²,

Lovejoy³

et al. 2014

Journal of Molecular Endocrinology

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Corticotrophin-releasing hormone (CRH) is the pivotal neuroendocrine peptide hormone associated with the regulation of the stress response in vertebrates. However, CRH-like peptides are also found in a number of invertebrate species. The origin of this peptide can be traced to a common ancestor of lineages leading to chordates and to arthropods, postulated to occur some 500 million years ago. Evidence indicates the presence of a single CRH-like receptor and a soluble binding protein system that acted to transduce and regulate the actions of the early CRH peptide. In vertebrates, genome duplications led to the divergence of CRH receptors into CRH1 and CRH2 forms in tandem with the development of four paralogous ligand lineages that included CRH; urotensin I/urocortin (Ucn), Ucn2 and Ucn3. In addition, taxon-specific genome duplications led to further local divergences in CRH ligands and receptors. Functionally, the CRH ligand-receptor system evolved initially as a molecular system to integrate early diuresis and nutrient acquisition. As multicellular organisms evolved into more complex forms, this ligand-receptor system became integrated with the organismal stress response to coordinate homoeostatic challenges with internal energy usage. In vertebrates, CRH and the CRH1 receptor became associated with the hypothalamo-pituitary-adrenal/interrenal axis and the initial stress response, whereas the CRH2 receptor was selected to play a greater role in diuresis, nutrient acquisition and the latter aspects of the stress response.

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“…Here too, the Lederis laboratory, in collaboration with the Richter laboratory, has provided a basis for further work. Beginning in the 1980s, the Lederis-Richter team (Karl doing the fishing using nets, with the help of his long-time Calgary colleague, Henk Zwiers; Dietmar fishing with molecular probes) was able to clone and sequence a variety of peptide receptor and neuropeptide genes from teleosts, focusing not only on the teleost homologues of CRF 1 and CRF 2 (Pohl et al, 2001), but also on receptors for vasotocin (Mahlmann et al, 1994), isotocin (Hausmann et al, 1995), TRH (Harder et al, 2001) and opiates (Darlison et al, 1997). The cloning of the receptors from the teleost source took its place beside the parallel cloning of a number of neuropeptides (isotocin, vasotocin, CRF) (Okawara et al, 1988;Heierhorst et al, 1989;Figueroa et al, 1989).…”

Section: Teleost Neuropeptide Receptors and Their Ligands: Crf 1 /Crfmentioning

confidence: 99%

Urotensin I–CRF–Urocortins: A mermaid’s tail

Pittman¹,

Hollenberg²

2009

General and Comparative Endocrinology

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From the individual perspective of the two authors who were long-time colleagues of Karl Lederis at the University of Calgary, the events and personal interactions are described, that are relevant to the discovery of Urotensin I (UI) in the Lederis laboratory, along with the concurrent discovery of Urotensin II (UII) in the Bern laboratory and corticotropin-releasing factor (CRF/CRH) in the Vale laboratory. The fortuitous sabbatical experiences that put Professors Lederis and Bern on the track of the Urotensins, along with the essential isolation paradigm that resulted in the complete sequencing and synthesis of UI and UII are summarized. The chance interaction between Drs. Vale and Lederis who, prior to the publications of the sequences of UI and CRF, realized the sequence commonalities of these peptides with the vasoactive frog peptide, sauvagine, is outlined. Further, the relationship between the pharmacological studies done with UI in the Calgary laboratory and the more recent understanding of the biology and receptor pharmacology for the entire Urotensin I-CRF-Urocortin peptide family is dealt with. The value of a comparative endocrinology approach to understanding hormone action is emphasized, along with a projection to the future, based on new hypotheses that can be generated by unexplained data already in the literature. Based on the previously described pharmacology of the UI-CRF-Urocortin peptides in a number of target tissues, it is suggested that the use of current molecular approaches can be integrated with a 'classical' pharmacological approach to generate new insights about the UI-CRF-Urocortin hormone family.

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Cloning and functional pharmacology of two corticotropin-releasing factor receptors from a teleost fish

Cited by 62 publications

References 40 publications

Corticotropin-releasing hormone in the teleost stress response: rapid appearance of the peptide in plasma of tilapia (Oreochromis mossambicus)

Corticotropin-releasing hormone in the teleost stress response: rapid appearance of the peptide in plasma of tilapia (Oreochromis mossambicus)

MOLECULAR EVOLUTION OF GPCRS: CRH/CRH receptors

Urotensin I–CRF–Urocortins: A mermaid’s tail

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