{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T12:36:42Z","timestamp":1791981402235,"version":"4.4.0"},"reference-count":259,"publisher":"The Endocrine Society","issue":"2","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,4,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>TRH is a tripeptide amide that functions as a neurotransmitter but also serves as a neurohormone that has a critical role in the central regulation of the hypothalamic-pituitary-thyroid axis. Hypophysiotropic TRH neurons involved in this neuroendocrine process are located in the hypothalamic paraventricular nucleus and secrete TRH into the pericapillary space of the external zone of the median eminence for conveyance to anterior pituitary thyrotrophs. Under basal conditions, the activity of hypophysiotropic TRH neurons is regulated by the negative feedback effects of thyroid hormone to ensure stable, circulating, thyroid hormone concentrations, a mechanism that involves complex interactions between hypophysiotropic TRH neurons and the vascular system, cerebrospinal fluid, and specialized glial cells called tanycytes. Hypophysiotropic TRH neurons also integrate other humoral and neuronal inputs that can alter the setpoint for negative feedback regulation by thyroid hormone. This mechanism facilitates adaptation of the organism to changing environmental conditions, including the shortage of food and a cold environment. The thyroid axis is also affected by other adverse conditions such as infection, but the central mechanisms mediating suppression of hypophysiotropic TRH may be pathophysiological. In this review, we discuss current knowledge about the mechanisms that contribute to the regulation of hypophysiotropic TRH neurons under physiological and pathophysiological conditions.<\/jats:p>","DOI":"10.1210\/er.2013-1087","type":"journal-article","created":{"date-parts":[[2014,1,14]],"date-time":"2014-01-14T05:06:25Z","timestamp":1389675985000},"page":"159-194","source":"Crossref","is-referenced-by-count":319,"title":["Central Regulation of Hypothalamic-Pituitary-Thyroid Axis Under Physiological and Pathophysiological Conditions"],"prefix":"10.1210","volume":"35","author":[{"given":"Csaba","family":"Fekete","sequence":"first","affiliation":[{"name":"Department of Endocrine Neurobiology (C.F.), Institute of Experimental Medicine, Hungarian Academy of Sciences, 1083 Budapest, Hungary;"},{"name":"Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism (C.F., R.M.L.), Tupper Research Institute, Tufts Medical Center, Boston, Massachusetts 02111;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ronald M.","family":"Lechan","sequence":"first","affiliation":[{"name":"Department of Endocrine Neurobiology (C.F.), Institute of Experimental Medicine, Hungarian Academy of Sciences, 1083 Budapest, Hungary;"},{"name":"Department of Medicine, Division of Endocrinology, Diabetes, and Metabolism (C.F., R.M.L.), Tupper Research Institute, Tufts Medical Center, Boston, Massachusetts 02111;"},{"name":"Department of Neuroscience (R.M.L.), Tufts University School of Medicine, Boston, Massachusetts 02111"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"80","published-online":{"date-parts":[[2013,12,13]]},"reference":[{"key":"2020071612022784100_B1","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/B978-008045046-9.01176-1","article-title":"Hypothalamic-pituitary-thyroid axis: organization, neural\/endocrine control of TRH","volume-title":"Encyclopedia of Neuroscience","author":"Lechan","year":"2009"},{"key":"2020071612022784100_B2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1749-6632.1989.tb46627.x","article-title":"TRH: historical aspects","volume":"553","author":"Reichlin","year":"1989","journal-title":"Ann NY Acad Sci"},{"key":"2020071612022784100_B3","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1016\/0006-291X(69)90868-7","article-title":"The identity of chemical and hormonal properties of the thyrotropin releasing hormone and pyroglutamyl-histidyl-proline amide","volume":"37","author":"Boler","year":"1969","journal-title":"Biochem Biophys Res Commun"},{"key":"2020071612022784100_B4","first-page":"1870","article-title":"[Molecular structure of the hypothalamic hypophysiotropic TRF factor of ovine origin: mass spectrometry demonstration of the PCA-His-Pro-NH2 sequence]","volume":"269","author":"Burgus","year":"1969","journal-title":"C R Acad Sci Hebd Seances Acad Sci D"},{"key":"2020071612022784100_B5","doi-asserted-by":"crossref","first-page":"33365","DOI":"10.1074\/jbc.M006819200","article-title":"cAMP response element-binding protein-binding protein mediates thyrotropin-releasing hormone signaling on thyrotropin subunit genes","volume":"275","author":"Hashimoto","year":"2000","journal-title":"J Biol Chem"},{"key":"2020071612022784100_B6","doi-asserted-by":"crossref","first-page":"941","DOI":"10.1089\/thy.1998.8.941","article-title":"Hypothalamic thyrotropin-releasing hormone and thyrotropin biological activity","volume":"8","author":"Persani","year":"1998","journal-title":"Thyroid"},{"key":"2020071612022784100_B7","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1172\/JCI108955","article-title":"The physiological role of thyrotropin-releasing hormone in the regulation of thyroid-stimulating hormone and prolactin secretion in the rat","volume":"61","author":"Harris","year":"1978","journal-title":"J Clin Invest"},{"key":"2020071612022784100_B8","doi-asserted-by":"crossref","first-page":"1450","DOI":"10.1210\/me.2004-0017","article-title":"Generation of thyrotropin-releasing hormone receptor 1-deficient mice as an animal model of central hypothyroidism","volume":"18","author":"Rabeler","year":"2004","journal-title":"Mol Endocrinol"},{"key":"2020071612022784100_B9","doi-asserted-by":"crossref","first-page":"29378","DOI":"10.1074\/jbc.270.49.29378","article-title":"Expression of human thyrotropin in cell lines with different glycosylation patterns combined with mutagenesis of specific glycosylation sites. 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