Artículos de revista
Permanent URI for this collectionhttps://repositorio.inprf.gob.mx/handle/123456789/5
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Item Thyroxine-induced expression of pyroglutamyl peptidase II and inhibition of TSH release precedes suppression of TRH mRNA and requires type 2 deiodinase(2011) Marsili, Alessandro; Sánchez, Edith; Singru, Praful; Harney, John W.; Zavacki, Ann Marie; Lechan, Ronald M.; Larsen, P.R.; Thyroid Section, Division of Endocrinology, Diabetes and Hypertension, Brigham and Women's Hospital and Harvard Medical School, Harvard Institutes of Medicine, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA.; plarsen@partners.orgItem Distribution of hypophysiotropic thyrotropin-releasing hormone (TRH)-synthesizing neurons in the hypothalamic paraventricular nucleus of the mouse(2010) Kádár, Andrea; Sánchez, Edith; Wittmann, Gábor; Singru, Praful S.; Füzesi, Tamás; Marsili, Alessandro; Larsen, P. Reed; Liposits, Zsolt; Lechan, Ronald M.; Fekete, Csaba; Department of Endocrine Neurobiology, Institute of Experimental Medicine, Hungarian Academy of Sciences, Budapest, Hungary 1083Item Differential response of TRHergic neurons of the hypothalamic paraventricular nucleus (PVN) in female animals submitted to food-restriction or dehydration-induced anorexia and cold exposure(2008) Jaimes-Hoy, Lorraine; Joseph-Bravo, Patricia; Gortari, Patricia de; División de Investigaciones en Neurociencias, Instituto Nacional de Psiquiatría RFM, México D.F., México.; gortari@imp.edu.mxItem Amygdala kindling differentially regulates the expression of the elements involved in TRH transmission(2006) De Gortari, P.; Uribe, R.M.; García-Vázquez, A.; Aguilar-Valles, A.; Martínez, A.; Valdés, A.; Charli, J.L.; Fernández-Guardiola, A.; Joseph-Bravo, P.; Dept. Neurociencias, Instituto Nacional de Psiquiatría Ramón de la Fuente Muñíz, Czda. México-Xochimilco 102, Sn. Lorenzo Huipulco, México D.F. 14370, Mexico; joseph@ibt.unam.mxItem Chronic ethanol or glucose consumption alter TRH content and pyroglutamyl aminopeptidase II activity in rat limbic regions(2005) De Gortari, P.; Cisneros, M.; Joseph-Bravo, P.; División de Investigación en Neurociencias, Instituto Nacional de Psiquiatría Ramón de la Fuente Muñiz, Calzada México-Xochimilco 101, Col. San Lorenzo Huipulco, C.P. 14370, México D.F., México.; gortari@imp.edu.mxItem Acute administration of alcohol modulates pyroglutamyl amino peptidase II activity and mRNA levels in rat limbic regions(2005) De Gortari, P.; Romero, F.; Cisneros, M.; Joseph-Bravo, P.; Department Neurociencias, Instituto Nacional de Psiquiatría, Ramón de la Fuente Muñiz, Calzada México-Xochimilco 101, Col. San Lorenzo Huipulco, C.P. 14370, Mexico.; gortari@imp.edu.mxItem Chronic ingestion of ethanol or glucose solutions affects hypothalamic and limbic TRH metabolism in dams and their pups(2002) De Gortari, P.; Cisneros, M.; Medellín, M.A.; Joseph-Bravo, P.; Depart. of Neuroscience, Instituto Nacional de Psiquiatría Ramón de la Fuente Muñiz, Calzada México-Xochimilco #101, San Lorenzo Huipulco, Mexico D.F. 14370, Mexico.; gortari@imp.edu.mxItem Acute ethanol administration induces changes in TRH and proenkephalin expression in hypothalamic and limbic regions of rat brain(2000) De Gortari, P.; Méndez, M.; Rodríguez-Keller, I.; Pérez-Martínez, L.; Joseph-Bravo, P.; Dept. Nutrición, Universidad Iberoamericana, Mexico; pgortari@ibt.unam.mxItem TRH inactivation in the extracellular compartment: role of pyroglutamyl peptidase II(1998) Charli, J.L.; Vargas, M.A.; Cisneros, M.; De Gortari, P.; Baeza, M.A.; Jasso, P.; Bourdais, J.; Pérez, L.; Uribe, R.M.; Joseph-Bravo, P.; Departamento de Genética y Fisiología Molecular, Universidad Nacional Autónoma de México, Cuernavaca.TRH (pGlu-His-ProNH2) inactivation in the brain and pituitary extracellular fluid is reviewed. While TRH could be eliminated by alternative mechanisms, i.e. uptake or internalization, modification, hydrolysis by broad specificity peptidases such as pyroglutamyl peptidase I and prolyl endopeptidase, evidence accumulates to support a specific neuroectopeptidase as the main mechanism responsible for its extracellular inactivation. Pyroglutamyl peptidase II (PPII; E.C. 3.4.19.6) is a narrow specificity zinc metallopeptidase hydrolyzing the pyroglutamyl-histidyl peptide bond of TRH. PPII is an integral membrane protein with a small intracellular domain, a transmembrane segment and a large extracellular domain that contains the catalytic site. It is therefore idealy situated to degrade TRH present in the extracellular space. PPII is highly enriched in brain, specifically present in neuronal cells. PPII inhibition enhances recovery of TRH released in vitro. In situ hybridization studies demonstrate that PPII mRNA colocalizes with TRH-receptor mRNA in various brain regions. However, the existence of exceptions suggest that alternative inactivation mechanisms for TRH may operate. PPII activity is regulated in various pharmacological or pathophysiological conditions which alter TRH transmission. It is also present in adenohypophysis, preferentially on lactotrophs, where its activity is stringently regulated by hormones and hypothalamic factors. PPII activity regulation may contribute to adjust TRH neural and hormonal transmissions.