The Resource Phosphorylation of skeletal muscle acetyl-CoA carboxylase by AMPK enhances palmitoyl-CoA inhibition, by Dustin S. Rubink

Phosphorylation of skeletal muscle acetyl-CoA carboxylase by AMPK enhances palmitoyl-CoA inhibition, by Dustin S. Rubink

Label
Phosphorylation of skeletal muscle acetyl-CoA carboxylase by AMPK enhances palmitoyl-CoA inhibition
Title
Phosphorylation of skeletal muscle acetyl-CoA carboxylase by AMPK enhances palmitoyl-CoA inhibition
Statement of responsibility
by Dustin S. Rubink
Creator
Subject
Genre
Language
eng
Summary
Acetyl-CoA carboxylase (ACC) catalyzes the formation of malnoyl-CoA, which in turn controls the rate of fatty acid metabolism. ACC beta or 2 has been shown to be localized on the mitochondria in close proximity to carnintine palmitoyl transferase 1 (CPT-1), the enzyme responsible for the influx of acyl-CoA into the matrix where beta oxidation takes place. CPT-1 is inhibited by malonyl-CoA produced by ACC. It has been well documented that AMP activated kinase (AMPK) when activated phosphorylates and inactivates ACC. ACC is controlled allosterically by citrate, which activates, and by palmitoyl-COA, which inhibits. In this study, we asked the question, 3Does phosphorylation by AMPK effect the inhibition of ACC by palmitoyl-CoA?4 ACC was isolated and then subjected to phosphorylation and activity was measured in varying concentrations of acetyl-CoA and citrate. Phosphoryation reduced the substrate (acetyl-CoA) saturation activity curves for ACC at all levels of palmitoyl-CoA. The Ki for palmitoyl-CoA inhibition of ACC was reduced from 1.7 ł 0.25 æM to 0.85 ł 0.13 uM (p<0.05) as a consequence of phosphorylation. In addition the citrate activation curves for ACC were greatly reduced in the presence of palmitoyl-CoA. The data show that skeletal muscle ACC or ACC-beta is more potently inhibited by palmitoyl-CoA after phosphorylation by AMPK. During long-term exercise when AMPK is activated and muscle palmitoyl-CoA is elevated this may contribute to the low malonyl-CoA and increased fatty acid oxidation
Cataloging source
UPB
Degree
M.S.
Dissertation year
2004
Granting institution
Brigham Young University. Dept. of Physiology and Developmental Biology
Illustrations
illustrations
Index
no index present
Literary form
non fiction
Nature of contents
  • bibliography
  • theses
Label
Phosphorylation of skeletal muscle acetyl-CoA carboxylase by AMPK enhances palmitoyl-CoA inhibition, by Dustin S. Rubink
Link
http://hdl.lib.byu.edu/1877/etd622
Instantiates
Publication
Bibliography note
Includes bibliographical references (p. 15-21)
Carrier category
volume
Carrier MARC source
rdacarrier
Content category
text
Content type MARC source
rdacontent
Dimensions
28 cm.
Extent
viii, 28 p.
Media category
unmediated
Media MARC source
rdamedia
Other physical details
ill.
System control number
(OCoLC)ocn373671860
Label
Phosphorylation of skeletal muscle acetyl-CoA carboxylase by AMPK enhances palmitoyl-CoA inhibition, by Dustin S. Rubink
Link
http://hdl.lib.byu.edu/1877/etd622
Publication
Bibliography note
Includes bibliographical references (p. 15-21)
Carrier category
volume
Carrier MARC source
rdacarrier
Content category
text
Content type MARC source
rdacontent
Dimensions
28 cm.
Extent
viii, 28 p.
Media category
unmediated
Media MARC source
rdamedia
Other physical details
ill.
System control number
(OCoLC)ocn373671860

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