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Instituto de Biología Molecular y Celular del Cáncer, CSIC-University of Salamanca, Salamanca, Spain
Centro de Investigación Biomédica en Red de Cáncer (CIBERONC), CSIC-University of Salamanca, Salamanca, Spain
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Instituto de Biología Molecular y Celular del Cáncer, CSIC-University of Salamanca, Salamanca, Spain
Centro de Investigación Biomédica en Red de Cáncer (CIBERONC), CSIC-University of Salamanca, Salamanca, Spain
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Instituto de Biología Molecular y Celular del Cáncer, CSIC-University of Salamanca, Salamanca, Spain
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Centro de Investigación en Medicina Molecular e Enfermidades Crónicas, University of Santiago de Compostela, Santiago de Compostela, Spain
Centro de Investigación Biomédica en Red de Cáncer sobre la Fisiopatología de la Obesidad y Nutrición (CIBEROBN), University of Santiago de Compostela, Santiago de Compostela, Spain
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Instituto de Biología Molecular y Celular del Cáncer, CSIC-University of Salamanca, Salamanca, Spain
Centro de Investigación Biomédica en Red de Cáncer (CIBERONC), CSIC-University of Salamanca, Salamanca, Spain
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Instituto de Biología Molecular y Celular del Cáncer, CSIC-University of Salamanca, Salamanca, Spain
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Instituto de Biología Molecular y Celular del Cáncer, CSIC-University of Salamanca, Salamanca, Spain
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Instituto de Biología Molecular y Celular del Cáncer, CSIC-University of Salamanca, Salamanca, Spain
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Centro de Investigación en Medicina Molecular e Enfermidades Crónicas, University of Santiago de Compostela, Santiago de Compostela, Spain
Centro de Investigación Biomédica en Red de Cáncer sobre la Fisiopatología de la Obesidad y Nutrición (CIBEROBN), University of Santiago de Compostela, Santiago de Compostela, Spain
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Centro de Investigación en Medicina Molecular e Enfermidades Crónicas, University of Santiago de Compostela, Santiago de Compostela, Spain
Centro de Investigación Biomédica en Red de Cáncer sobre la Fisiopatología de la Obesidad y Nutrición (CIBEROBN), University of Santiago de Compostela, Santiago de Compostela, Spain
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Instituto de Biología Molecular y Celular del Cáncer, CSIC-University of Salamanca, Salamanca, Spain
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-associated thermogenesis as well as to transient increases in blood pressure, ventilation activity and vasomotor tone ( Guyenet 2006 , Lambert et al. 2010 ). One of the key brainstem centers controlling the sympathetic outflow is the rostral ventrolateral medulla (RVLM
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nuclear c-Fos in C57BL6 animals within neurons located in the area postrema, NTS, ventrolateral medulla, paraventricular nucleus and dorsomedial nucleus in fixed brain tissue collected 2 h following vehicle ( Fig. 6A , B , C , D and E ) or IL-1β ( Fig
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ABSTRACT
Plasma vasopressin (AVP) levels were measured at rest (mean arterial pressure 80–85 mmHg) and during hypotension (mean arterial pressure 38–45 mmHg) induced by ganglionic blockade (trimethaphan) in halothane-anaesthetized respirated rats with end-tidal pCO2 maintained at 34–40 mmHg. Hypotension (15 min) produced a 310% increase in plasma AVP (±60% s.e.m.) which was not reduced significantly by prior baro- and chemoreceptor denervation. The hypotension-induced rise in AVP was blocked by bilateral microinjections (40 nl) of the GABA-mimetic agent muscimol (151 pmol) into the ventrolateral medulla at obex level and significantly attenuated by injections of the same amount in the nucleus tractus solitarius. The rise in AVP was unaffected by microinjections in the pontine locus coeruleus. It was also blocked by bilateral microinjections of the glutamate-receptor antagonist kynurenate (40 nl, 1·8 nmol) into the ventrolateral medulla but unaffected by microinjections of the inactive analogue xanthurenic acid (40 nl, 1·8 nmol). A significantly smaller rise in plasma AVP (88%) was observed following bilateral nephrectomy. It is concluded that, in this preparation, hypotension produces the release of AVP via a mechanism largely independent of baro- and chemoreceptors, which requires the activation of neurones located in the caudal medulla oblongata. The same or closely related neurones may be activated by a neural or hormonal signal generated by the kidney.
J. Endocr. (1988) 118, 101–111
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School of Medicine, State Key Laboratory for Medical Genomics, Laboratory of Development and Diseases, Shanghai Institute of Endocrinology and Metabolism, Shanghai Clinical Center for Endocrine and Metabolic Disease
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-positive cells in these species. The existing results mainly indicate the expression of CHGA protein in adrenal medulla and gastro-entero-pancreatic system that abounds with various endocrine cells ( Kent & Coupland 1989 , Mahata et al . 1993 , Wang et
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Dorsomedial +++/c Cental +++/c Ventrolateral +++/c Lateral mammillary nucleus ++/+++ Medial mammillary nucleus + Supramammillary nucleus −/+ Ventral tuberomammillary nucleus + Midbrain/pons Deep mesencephalic nucleus − Edinger–Westphal nucleus
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al. (1992) , in multiple species by Smeets and Gonzalez (2000) and in the mouse by Paxinos and Franklin (2001) . CVO, circumventricular organ. CA group CVO Area postrema (AP) −7.48 A1 Ventrolateral medulla (VLM) −7.48, −7.32 A2 Nucleus of the
Institute of Physiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic
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Institute of Physiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic
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University of Chemistry and Technology, Prague, Czech Republic
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neurons in brain regions involved in food intake regulation, where PrRP is expressed (ventromedial nucleus (VMH) of hypothalamus and ventrolateral medulla (VLM) and nucleus tractus solitarius (NTS) of brainstem), also contain leptin receptors ( Ellacott
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Department of Pharmacology and Therapeutics, Department of Veterans Affairs, College of Medicine, University of Florida, PO Box 100267, Gainesville, Florida 32610, USA
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Department of Pharmacology and Therapeutics, Department of Veterans Affairs, College of Medicine, University of Florida, PO Box 100267, Gainesville, Florida 32610, USA
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shown) and unstained bright-field images ( Fig. 8 ). Expression was robust in NTS, with abundant numbers of GFP somata in medial, intermediate, and ventrolateral subdivisions. GFP cells were exclusively neuronal based on size and morphology and were
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reduction of ROS generation and activation of Akt ( Zeng et al . 2010 ), while the chronotropic effect of apelin-13 in the rostral ventrolateral medulla (RVLM) appears to be mediated by NAPDH oxidase-derived superoxide production ( Yao et al . 2011
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cytoarchitecture and integrality through thionin staining ( Fig. 2C and D ) and by the presence of ERα in the ventrolateral part of the VMH (VMHvl; Fig. 2E and F ), but no changes were observed in SF1 Socs3 KO mice. Figure 2 Characterization of SF1 Socs