Open AccessDual-process brain mitochondria isolation preserves function and clarifies protein composition
Author(s) -
Maria Noterman,
Kalyani Chaubey,
Kristi LinRahardja,
Anjali M. Rajadhyaksha,
Andrew A. Pieper,
Eric B. Taylor
Publication year - 2021
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2019046118
Subject(s) - mitochondrion , biochemistry , biology , transporter , microbiology and biotechnology , gene
Significance The unique aspects of brain mitochondria composition and function are incompletely understood, and new approaches are required to understand their relationship. We addressed this challenge through a dual-process isolation procedure that yields both semipure brain mitochondria suitable for functional studies but not protein localization and ultrapure brain mitochondria that are suitable for determining protein localization but functionally compromised. We observed that contrary to the published literature, N-methyl-D-aspartate receptor, ryanodine receptor 1, glyceraldehyde 3-phosphate dehydrogenase, monocarboxylate transporter 1, excitatory amino acid transporter 1, and the L-type calcium channel Cav 1.2α1 subunit are absent from brain mitochondria. Utilization of this dual-process brain mitochondria isolation technique will foster clarity on mechanisms of brain health and disease.