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Klugmann et al. Rare Dis Orphan Drugs J 2023;2:8                    Rare Disease and
               DOI: 10.20517/rdodj.2023.05
                                                                            Orphan Drugs Journal




               Technical Note                                                                Open Access



               Histological and biochemical methods to assess
               aminoacyl-tRNA synthetase expression in human

               post-mortem brain tissue


               Matthias Klugmann, Alexandra K. Suchowerska, Gary D. Housley, Dominik Fröhlich
               Translational Neuroscience Facility & Department of Physiology, School of Biomedical Sciences, UNSW Sydney, Sydney NSW
               2052, Australia.

               Correspondence to: Dominik Fröhlich, MSc, PhD, Translational Neuroscience Facility & Department of Physiology, School of
               Biomedical Sciences, UNSW Sydney, Sydney NSW 2052, Australia. E-mail: d.frohlich@unsw.edu.au

               How to cite this article: Klugmann M, Suchowerska AK, Housley GD, Fröhlich D. Histological and biochemical methods to assess
               aminoacyl-tRNA synthetase expression in human post-mortem brain tissue. Rare Dis Orphan Drugs J 2023;2:8.
               https://dx.doi.org/10.20517/rdodj.2023.05
               Received: 28 Jan 2023  First Decision: 2 Mar 2023  Revised: 15 Mar 2023  Accepted: 10 Apr 2023  Published: 20 Apr 2023

               Academic Editors: Daniel SCHERMAN, Jacques S Beckmann  Copy Editor: Ying Han  Production Editor: Ying Han

               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.
               Keywords: Aminoacyl-tRNA synthetase, aspartyl-tRNA synthetase, AspRS, DARS1, post-mortem brain tissue




               INTRODUCTION
               Protein synthesis is an evolutionarily highly conserved process that requires an intimate interplay of






                           © The Author(s) 2023. Open Access This article is licensed under a Creative Commons Attribution 4.0
                           International License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, sharing,
                           adaptation, distribution and reproduction in any medium or format, for any purpose, even commercially, as
               long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and
               indicate if changes were made.

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