Mitochondrial proteome of mouse oocytes and cisplatin-induced shifts in protein profile.

Acta Pharmacol Sin

Center for Reproductive Medicine, Department of Obstetrics and Gynecology, Peking University Third Hospital, Beijing, 100191, China.

Published: December 2021

AI Article Synopsis

  • Mitochondria are vital for energy production and various cellular functions, particularly in mammalian oocytes, where they are crucial for germ cell development and avoiding inherited disorders.
  • A systematic analysis of oocyte mitochondria was hindered by both the scarcity of oocyte samples and technical issues in studying mitochondrial proteins in live cells.
  • This study utilized proximity labeling proteomics to identify 158 mitochondrial proteins in live mouse oocytes and demonstrated how exposure to the chemotherapy drug cisplatin caused changes in the levels of specific mitochondrial proteins.

Article Abstract

Mitochondria are essential organelles that provide energy for mammalian cells and participate in multiple functions, such as signal transduction, cellular differentiation, and regulation of apoptosis. Compared with the mitochondria in somatic cells, oocyte mitochondria have an additional level of importance since they are required for germ cell maturation, dysfunction in which can lead to severe inherited disorders. Thus, a systematic proteomic profile of oocyte mitochondria is urgently needed to support the basic and clinical research, but the acquisition of such a profile has been hindered by the rarity of oocyte samples and technical challenges associated with capturing mitochondrial proteins from live oocytes. Here, in this work, using proximity labeling proteomics, we established a mitochondria-specific ascorbate peroxidase (APEX2) reaction in live GV-stage mouse oocytes and identified a total of 158 proteins in oocyte mitochondria. This proteome includes intrinsic mitochondrial structural and functional components involved in processes associated with "cellular respiration", "ATP metabolism", "mitochondrial transport", etc. In addition, mitochondrial proteome capture after oocyte exposure to the antitumor chemotherapeutic cisplatin revealed differential changes in the abundance of several oocyte-specific mitochondrial proteins. Our study provides the first description of a mammalian oocyte mitochondrial proteome of which we are aware, and further illustrates the dynamic shifts in protein abundance associated with chemotherapeutic agents.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8632880PMC
http://dx.doi.org/10.1038/s41401-021-00687-4DOI Listing

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