Unveiling OSCP as the potential therapeutic target for mitochondrial dysfunction-related diseases

Life Sci. 2024 Jan 1:336:122293. doi: 10.1016/j.lfs.2023.122293. Epub 2023 Nov 27.

Abstract

Mitochondria are important organelles in cells responsible for energy production and regulation. Mitochondrial dysfunction has been implicated in the pathogenesis of many diseases. Oligomycin sensitivity-conferring protein (OSCP), a component of the inner mitochondrial membrane, has been studied for a long time. OSCP is a component of the F1Fo-ATP synthase in mitochondria and is closely related to the regulation of the mitochondrial permeability transition pore (mPTP). Studies have shown that OSCP plays an important role in cardiovascular disease, neurological disorders, and tumor development. This review summarizes the localization, structure, function, and regulatory mechanisms of OSCP and outlines its role in cardiovascular disease, neurological disease, and tumor development. In addition, this article reviews the research on the interaction between OSCP and mPTP. Finally, the article suggests future research directions, including further exploration of the mechanism of action of OSCP, the interaction between OSCP and other proteins and signaling pathways, and the development of new treatment strategies for mitochondrial dysfunction. In conclusion, in-depth research on OSCP will help to elucidate its importance in cell function and disease and provide new ideas for the treatment and prevention of related diseases.

Keywords: Cancer; Cardiovascular disease; F1Fo-ATP synthase; Mitochondrial permeability transition pore (mPTP); Neurodegenerative diseases; Oligomycin sensitivity-conferring protein (OSCP).

Publication types

  • Review

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Cardiovascular Diseases*
  • Carrier Proteins / metabolism
  • Humans
  • Mitochondrial Diseases* / drug therapy
  • Mitochondrial Proton-Translocating ATPases
  • Neoplasms* / drug therapy

Substances

  • oligomycin sensitivity-conferring protein
  • Adenosine Triphosphatases
  • Carrier Proteins
  • Mitochondrial Proton-Translocating ATPases