Inhibition of Lonp1 induces mitochondrial remodeling and autophagy suppression in cervical cancer cells
Acta Histochemica, ISSN: 0065-1281, Vol: 125, Issue: 1, Page: 151986
2023
- 2Citations
- 5Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations2
- Citation Indexes2
- CrossRef1
- Captures5
- Readers5
Article Description
Lon protease 1(Lonp1) is an ATP-dependent protease located in the mitochondrial matrix and plays a crucial role in preserving normal mitochondrial function. Lonp1 overexpression is associated with tumorigenesis in various cancer types, including cervical cancer. In the present study, we show that the Lonp1 content is elevated in cervical cancer tissues compared to cervical paracancerous tissues. Conversely, Lonp1 knockdown suppresses cervical cancer cell proliferation, migration and invasion but promotes apoptosis. Mechanistically, Lonp1 knockdown decreases area of mitochondrial networks and induces mitochondrial depolarization. Furthermore, Lonp1 inhibition reduces the level of LC3-II/I, PINK1 and Parkin, but promotes the level of p62. Collectively, our study suggests that the anti-cancer effect caused by Lonp1 downregulation likely contributes to mitochondrial remodeling and suppression of autophagy and mitophagy.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0065128122001453; http://dx.doi.org/10.1016/j.acthis.2022.151986; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85143655809&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/36508908; https://linkinghub.elsevier.com/retrieve/pii/S0065128122001453; https://dx.doi.org/10.1016/j.acthis.2022.151986
Elsevier BV
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