| Homologous and heterologous down-regulation of leptin receptor messenger ribonucleic acid in rat adrenal gland. | |
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MedLine Citation:
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PMID: 11115775 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Leptin, the adipocyte-produced hormone that plays a key role in body weight homeostasis, has recently been found to be involved in the regulation of the hypothalamic-pituitary-adrenal axis. Moreover, reciprocal interactions between leptin and glucocorticoids have been described. In the present communication, two different strategies were undertaken to explore the mode of action of leptin in the direct control of rat adrenal function. First, a synthetic peptide approach demonstrated that the inhibitory effect of leptin on basal and ACTH-stimulated corticosterone secretion in vitro is, at least partially, mapped to a domain of the native protein between amino acids 116 and 130, i.e. an area of the molecule also relevant in terms of regulation of food intake and endocrine control. Secondly, semi-quantitative RT-PCR analysis indicated a complex pattern of adrenal leptin receptor (Ob-R) mRNA expression, with predominant expression of the Ob-Ra and Ob-Rb isoforms, as well as moderate levels of the Ob-Rc and Ob-Rf variants, whereas negligible signals for the Ob-Re isoform were detected. Interestingly, such an expression pattern appeared hormonally regulated as exposure to human recombinant leptin (10(-7 )M) or ACTH (10(-7 )M) significantly decreased Ob-R isoform mRNA expression. Indeed, dose-dependent ligand-induced Ob-Ra and Ob-Rb mRNA down-regulation was further confirmed by adrenal stimulation with increasing concentrations (10(-9)-10(-5 )M) of the active leptin fragment, leptin 116-130 amide. Overall, our results provide evidence for a novel regulatory step at the level of Ob-R mRNA expression in the interplay between ACTH and leptin for the tuning of rat adrenal corticosterone secretion. Furthermore, our data showing down-regulation of Ob-R mRNA expression by its cognate ligand may well be relevant to leptin physiology and its alteration in various disease states. |
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Authors:
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M Tena-Sempere; L Pinilla; L C González; F F Casanueva; C Diéguez; E Aguilar |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The Journal of endocrinology Volume: 167 ISSN: 0022-0795 ISO Abbreviation: J. Endocrinol. Publication Date: 2000 Dec |
Date Detail:
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Created Date: 2001-01-30 Completed Date: 2001-10-04 Revised Date: 2007-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0375363 Medline TA: J Endocrinol Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 479-86 Citation Subset: IM |
Affiliation:
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Department of Physiology, University of Córdoba, 14004 Córdoba, Spain. fi1tesem@uco.es |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adrenal Glands
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metabolism*,
secretion Adrenocorticotropic Hormone / pharmacology Analysis of Variance Animals Carrier Proteins / genetics* Corticosterone / analysis, secretion Depression, Chemical Gene Expression Regulation / physiology* Humans Male Organ Culture Techniques Peptide Fragments / pharmacology Protein Isoforms / genetics RNA, Messenger / analysis, metabolism* Rats Rats, Wistar Receptors, Cell Surface* Receptors, Leptin Recombinant Proteins / pharmacology Reverse Transcriptase Polymerase Chain Reaction |
| Chemical | |
Reg. No./Substance:
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0/Carrier Proteins; 0/Peptide Fragments; 0/Protein Isoforms; 0/RNA, Messenger; 0/Receptors, Cell Surface; 0/Receptors, Leptin; 0/Recombinant Proteins; 0/leptin receptor, human; 0/leptin(116-130) amide; 50-22-6/Corticosterone; 9002-60-2/Adrenocorticotropic Hormone |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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