@article{discovery10037991, volume = {10}, note = {Copyright {\copyright} The Author(s) 2017. This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/ publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.}, title = {Subunit composition of respiratory chain complex 1 and its responses to oxygen in mitochondria from human donor livers}, year = {2017}, month = {November}, journal = {BMC Research Notes}, keywords = {Complex 1, Donor after cardiac death, Liver transplantation, Mitochondria, Oxygen}, author = {Khorsandi, SE and Taanman, JW and Heaton, N}, url = {http://doi.org/10.1186/s13104-017-2863-7}, abstract = {OBJECTIVE: Donor liver function in transplantation is defined by mitochondrial function and the ability of mitochondria to recover from the sequence of warm and/or cold ischemia. Mitochondrial resilience maybe related to assembly and- subunit composition of Complex 1. The aim of this study was to determine if Complex 1 subunit composition was different in donor livers of varying quality and whether oxygen exposure had any effect. RESULTS: Five human livers not suitable for transplant were split. One half placed in cold static storage and the other half exposed to 40\% oxygen for 2�h. Protein was extracted for western blot. Membranes were probed with antibodies against {\ensuremath{\beta}}-actin and the following subunits of Complex 1: MTND1, NDUFA10, NDUFB6 and NDUFV2. No difference in steady state Complex 1 subunit composition was demonstrated between donor livers of varying quality, in terms of steatosis or mode of donation. Neither did exposure to oxygen influence Complex 1 subunit composition. This small observational study on subunit levels suggest that Complex 1 is fully assembled as no degradation of subunits associated with the different parts of the enzyme was seen.}, issn = {1756-0500} }