Document Detail


Proteolytic and lipolytic responses to starvation.
MedLine Citation:
PMID:  16815497     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Mammals survive starvation by activating proteolysis and lipolysis in many different tissues. These responses are triggered, at least in part, by changing hormonal and neural statuses during starvation. Pathways of proteolysis that are activated during starvation are surprisingly diverse, depending on tissue type and duration of starvation. The ubiquitin-proteasome system is primarily responsible for increased skeletal muscle protein breakdown during starvation. However, in most other tissues, lysosomal pathways of proteolysis are stimulated during fasting. Short-term starvation activates macroautophagy, whereas long-term starvation activates chaperone-mediated autophagy. Lipolysis also increases in response to starvation, and the breakdown of triacylglycerols provides free fatty acids to be used as an energy source by skeletal muscle and other tissues. In addition, glycerol released from triacylglycerols can be converted to glucose by hepatic gluconeogenesis. During long-term starvation, oxidation of free fatty acids by the liver leads to the production of ketone bodies that can be used for energy by skeletal muscle and brain. Tissues that cannot use ketone bodies for energy respond to these small molecules by activating chaperone-mediated autophagy. This is one form of interaction between proteolytic and lipolytic responses to starvation.
Authors:
Patrick F Finn; J Fred Dice
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  Nutrition (Burbank, Los Angeles County, Calif.)     Volume:  22     ISSN:  0899-9007     ISO Abbreviation:  Nutrition     Publication Date:    2006 Jul-Aug
Date Detail:
Created Date:  2006-07-03     Completed Date:  2006-11-22     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8802712     Medline TA:  Nutrition     Country:  United States    
Other Details:
Languages:  eng     Pagination:  830-44     Citation Subset:  IM    
Affiliation:
Department of Molecular and Cellular Physiology, Tufts University School of Medicine, Boston, Massachusetts, USA.
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MeSH Terms
Descriptor/Qualifier:
Acyl Coenzyme A / metabolism
Autophagy
Enzyme Activation
Fatty Acids, Nonesterified / metabolism
Humans
Ketone Bodies / metabolism
Lipolysis*
Lysosomes / metabolism
Molecular Chaperones / physiology
Muscle Proteins / metabolism
Muscle, Skeletal / chemistry
Peptide Hydrolases / metabolism*
Proteasome Endopeptidase Complex / metabolism
Starvation / metabolism*
Triglycerides / metabolism
Ubiquitin / metabolism
Chemical
Reg. No./Substance:
0/Acyl Coenzyme A; 0/Fatty Acids, Nonesterified; 0/Ketone Bodies; 0/Molecular Chaperones; 0/Muscle Proteins; 0/Triglycerides; 0/Ubiquitin; EC 3.4.-/Peptide Hydrolases; EC 3.4.25.1/Proteasome Endopeptidase Complex

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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