Author
CHINTAPALLI, SREE - Arkansas Children'S Nutrition Research Center (ACNC) | |
MCHAN, LARA - Arkansas Children'S Nutrition Research Center (ACNC) | |
BLACKBURN, MICHAEL - Arkansas Children'S Nutrition Research Center (ACNC) | |
ONO-MOORE, KIKUMI - Arkansas Children'S Nutrition Research Center (ACNC) | |
ROSE, SHANNON - University Arkansas For Medical Sciences (UAMS) | |
ANISHKIN, ANDRIY - University Of Maryland | |
JAYANTHI, SRINIVAS - University Of Arkansas | |
KRISHNASWAMY, THALLAPURANAM - University Of Arkansas | |
KUMAR, SURESH - Arkansas Children'S Nutrition Research Center (ACNC) | |
Ferruzzi, Mario |
Submitted to: Meeting Abstract
Publication Type: Abstract Only Publication Acceptance Date: 10/20/2017 Publication Date: N/A Citation: N/A Interpretive Summary: Technical Abstract: Myoglobin is one of the most abundant proteins in skeletal muscle (type 1, "slow twitch" fibers) and cardiomyocytes, and supports oxidative combustion of fuels. Myoglobin-abundant muscle types are adept at fatty acid oxidation, in contrast to "white" (type 2, "fast twitch") fibers that tend to rely on glucose catabolism and non-oxidative metabolism that generates lactic acid. The red color of oxidative muscle fibers is due to oxygenated myoglobin, analogous to bright red highly-oxygenated blood due to the related protein hemoglobin. We and others have characterized myoglobin as a fatty-acid (FA) binding protein, and our team has identified the likely binding pocket in oxygenated myoglobin. Importantly, de-oxygenated myoglobin does not bind FA except for less avid non-specific binding. More recently, we have made the novel observation that oxy-myoglobin also binds FA derivatives termed "acylcarnitines"—these otherwise physiological metabolites have been implicated in muscle cell stress pathways when they accumulate in excess (e.g., inherited disordered of fatty acid oxidation, cardiac ischemia). |