Document Detail


Stress-related alterations of acyl and desacyl ghrelin circulating levels: mechanisms and functional implications.
MedLine Citation:
PMID:  21782868     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Ghrelin is the only known peripherally produced and centrally acting peptide hormone that stimulates food intake and digestive functions. Ghrelin circulates as acylated and desacylated forms and recently the acylating enzyme, ghrelin-O-acyltransferase (GOAT) and the de-acylating enzyme, thioesterase 1/lysophospholipase 1 have been identified adding new layers of complexity to the regulation of ghrelin. Stress is known to alter gastrointestinal motility and food intake and was recently shown to modify circulating ghrelin and GOAT levels with differential responses related to the type of stressors including a reduction induced by physical stressors (abdominal surgery and immunological/endotoxin injection, exercise) and elevation by metabolic (cold exposure, acute fasting and caloric restriction) and psychological stressors. However, the pathways underlying the alterations of ghrelin under these various stress conditions are still largely to be defined and may relate to stress-associated autonomic changes. There is evidence that alterations of circulating ghrelin may contribute to the neuroendocrine and behavioral responses along with sustaining the energetic requirement needed upon repeated exposure to stressors. A better understanding of these mechanisms will allow targeting components of ghrelin signaling that may improve food intake and gastric motility alterations induced by stress.
Authors:
Andreas Stengel; Lixin Wang; Yvette Taché
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.; Review     Date:  2011-07-12
Journal Detail:
Title:  Peptides     Volume:  32     ISSN:  1873-5169     ISO Abbreviation:  Peptides     Publication Date:  2011 Nov 
Date Detail:
Created Date:  2011-11-21     Completed Date:  2012-04-16     Revised Date:  2013-06-28    
Medline Journal Info:
Nlm Unique ID:  8008690     Medline TA:  Peptides     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2208-17     Citation Subset:  IM    
Copyright Information:
Published by Elsevier Inc.
Affiliation:
CURE: Digestive Diseases Research Center, David Geffen School of Medicine, University of California Los Angeles and Veterans Affairs Greater Los Angeles Healthcare System, Los Angeles, CA 90073, United States. andreas.stengel@charite.de
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MeSH Terms
Descriptor/Qualifier:
Acyltransferases / genetics,  metabolism*
Animals
Autonomic Nervous System / metabolism
Eating / physiology
Fasting / metabolism
Gastrointestinal Motility
Gene Expression
Ghrelin / blood*,  genetics,  metabolism
Humans
Receptors, Ghrelin / metabolism*
Signal Transduction / physiology*
Somatostatin / genetics,  metabolism
Stomach / metabolism
Stress, Physiological*
Stress, Psychological / metabolism*
TOR Serine-Threonine Kinases / genetics,  metabolism
Thiolester Hydrolases / genetics,  metabolism*
Grant Support
ID/Acronym/Agency:
R01 DK033061/DK/NIDDK NIH HHS; R01 DK057238-10/DK/NIDDK NIH HHS; R01DK-33061/DK/NIDDK NIH HHS; R01DK-57238/DK/NIDDK NIH HHS; R37 DK033061-18/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Ghrelin; 0/Receptors, Ghrelin; 0/ghrelin, des-n-octanoyl; 51110-01-1/Somatostatin; EC 2.3.-/Acyltransferases; EC 2.3.-/ghrelin O-acyltransferase, human; EC 2.7.1.1/TOR Serine-Threonine Kinases; EC 3.1.2.-/LYPLA1 protein, human; EC 3.1.2.-/Thiolester Hydrolases
Comments/Corrections

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