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Mol Cell Neurosci. 2017 Jul;82:137-142. doi: 10.1016/j.mcn.2017.04.007. Epub 2017 Apr 29.

Divergent lactate dehydrogenase isoenzyme profile in cellular compartments of primate forebrain structures.

Author information

1
Department of Anthropology and Center for the Advanced Study of Human Paleobiology, The George Washington University, Washington, DC 20052, USA.
2
Department of Anthropology and School of Biomedical Sciences, Kent State University, Kent, OH 44242, USA.
3
MAEBIOS, Alamogordo, NM 88330, USA.
4
Fishberg Department of Neuroscience and Friedman Brain Institute, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.
5
Department of Molecular and Integrative Physiology and Carl R. Woese Institute for Genomic Biology, University of Illinois, Urbana-Champaign, Urbana, IL 61801, USA.
6
Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, MI 48201, USA.
7
Department of Anthropology and Center for the Advanced Study of Human Paleobiology, The George Washington University, Washington, DC 20052, USA. Electronic address: sherwood@gwu.edu.

Abstract

The compartmentalization and association of lactate dehydrogenase (LDH) with specific cellular structures (e.g., synaptosomal, sarcoplasmic or mitochondrial) may play an important role in brain energy metabolism. Our previous research revealed that LDH in the synaptosomal fraction shifts toward the aerobic isoforms (LDH-B) among the large-brained haplorhine primates compared to strepsirrhines. Here, we further analyzed the subcellular localization of LDH in primate forebrain structures using quantitative Western blotting and ELISA. We show that, in cytosolic and mitochondrial subfractions, LDH-B expression level was relatively elevated and LDH-A declined in haplorhines compared to strepsirrhines. LDH-B expression in mitochondrial fractions of the neocortex was preferentially increased, showing a particularly significant rise in the ratio of LDH-B to LDH-A in chimpanzees and humans. We also found a significant correlation between the protein levels of LDH-B in mitochondrial fractions from haplorhine neocortex and the synaptosomal LDH-B that suggests LDH isoforms shift from a predominance of A-subunits toward B-subunits as part of a system that spatially buffers dynamic energy requirements of brain cells. Our results indicate that there is differential subcellular compartmentalization of LDH isoenzymes that evolved among different primate lineages to meet the energy requirements in neocortical and striatal cells.

KEYWORDS:

Cellular subfractions; Haplorhine; Lactate dehydrogenase; Metabolism; Mitochondria; Primate forebrain; Strepsirrhine

PMID:
28461219
PMCID:
PMC5531073
DOI:
10.1016/j.mcn.2017.04.007
[Indexed for MEDLINE]
Free PMC Article

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