Regulation of thyrotropin-releasing hormone (TRH)-degrading enzymes.
Item
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Title
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Regulation of thyrotropin-releasing hormone (TRH)-degrading enzymes.
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Identifier
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AAI9029982
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identifier
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9029982
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Creator
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Suen, Chen-Shian.
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Contributor
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Adviser: Sherwin Wilk
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Date
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1990
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Language
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English
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Publisher
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City University of New York.
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Subject
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Biology, Neuroscience | Biology, Animal Physiology
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Abstract
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Thyrotropin releasing hormone (TRH, pGlu-His-Pro-NH{dollar}\sb2{dollar}) is degraded by three enzymes. The pGlu-His bond is cleaved by pyroglutamyl peptidases I and II separately and the Pro-NH{dollar}\sb2{dollar} bond is cleaved by prolyl endopeptidase. Pyroglutamyl peptidase I (EC 3.4.19.3) and prolyl endopeptidase (EC 3.4.21.26) are widely distributed cytosolic proteases and have a broad substrate specificity. Pyroglutamyl peptidase II (EC 3.4.19.{dollar}-{dollar}), a membrane-bound metalloprotease, is a highly specific TRH degrading enzyme. It has been known that thyroid hormone negatively regulates TRH action at the pituitary gland. The molecular mechanism of TRH action in GH{dollar}\sb3{dollar} cells has been extensively studied. Activation of TRH receptors leads to the hydrolysis of phosphatidyl inositol, generating the dual signals inositol triphosphate (IP{dollar}\sb3{dollar}) and diacylglycerol (DG). DG is an endogenous activator of protein kinase C. The effects of thyroid hormone, the protein kinase C activator (TPA), and sodium butyrate on TRH degrading enzymes was investigated. These studies were carried out either in cell culture (GH{dollar}\sb3{dollar} Cells and Y-79 retinoblastoma cells) or in vivo. (Abstract shortened with permission of author.).
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Type
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dissertation
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Source
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PQT Legacy CUNY.xlsx
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degree
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Ph.D.
