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Am J Physiol Endocrinol Metab (January 24, 2006). doi:10.1152/ajpendo.00594.2005
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Submitted on November 30, 2005
Accepted on January 18, 2006

Co-localization of MCT1, CD147 and LDH in mitochondrial inner membrane of L6 skeletal muscle cells: Evidence of a mitochondrial lactate oxidation complex

Takeshi Hashimoto1, Rajaa Hussien1, and George A Brooks1*

1 Department of Integrative Biology, University of California, Berkeley, CA, USA

* To whom correspondence should be addressed. E-mail: gbrooks{at}berkeley.edu.

Results of previous studies suggested a role of mitochondria (MI) in Intracellular and Cell-Cell Lactate Shuttles. Therefore, using a rat-derived L6 skeletal muscle cell line and confocal laser-scanning microscopy (CLSM) we examined the cellular locations of mitochondria, lactate dehydrogenase (LDH), the lactate/pyruvate transporter MCT1, and CD147, a purported chaperone protein for MCT1. CLSM showed that LDH, MCT1 and CD147 are co-localized with the mitochondrial reticulum. Western blots showed that cytochrome oxidase (COX), NADH-dehydrogenase (NADH-dh), LDH, MCT1 and CD147 are abundant in mitochondrial fractions of L6 cells. Interactions among COX, MCT1 and CD147 in mitochondria were confirmed by immunoblotting after immunoprecipitation. These findings support the presence of a mitochondrial lactate oxidation complex associated with the cytochrome oxidase end of the electron transport chain that may explain the oxidative catabolism of lactate and, hence, mechanism of the Intracellular Lactate Shuttle.




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