Histological and biochemical methods to assess aminoacyl-tRNA synthetase expression in human post-mortem brain tissue

Abstract

Aminoacyl-tRNA synthetases are essential, non-redundant enzymes that catalyze the charging of tRNAs with their cognate amino acids. This reaction is a prerequisite for protein translation in all cells. Mutations in human aminoacyl-tRNA synthetases are often associated with defects of the peripheral and central nervous system and are the underlying cause of many rare diseases including neuropathies and leukodystrophies. A comprehensive understanding of aminoacyl-tRNA synthetase expression domains is key to understanding these disorders and developing novel targeted treatment strategies. Here, we describe histological and biochemical methods to analyze the expression pattern of the aspartyl-tRNA synthetase AspRS in human post-mortem brain tissue. The same methods can readily be applied to other members of the aminoacyl-tRNA synthetase superfamily or, more generally, to other cytosolic proteins in the human brain.