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Photobiomodulation enhancement of cell proliferation at 660 nm does not require cytochrome c oxidase.

08:00 EDT 22nd March 2019 | BioPortfolio

Summary of "Photobiomodulation enhancement of cell proliferation at 660 nm does not require cytochrome c oxidase."

Photobiomodulation (PBM) therapy is based on the use of specific light parameters to promote tissue repair. Although demonstrated in different cell models and tissues, the mechanism by which photobiomodulation operates is not well understood. Previous studies suggested that the cell proliferation enhancement triggered by red and near-infrared PBM involves the activation of the mitochondrial respiratory chain enzyme cytochrome c oxidase (CCO). It was suggested that light in this range would displace inhibitory nitric oxide bound to CCO. To test this mechanism, we took advantage of cell lines lacking CCO, including a mouse line knockout for Cox10 (a gene required for the synthesis of heme a, the prosthetic group of CCO) and a human cell line with an mtDNA mutation in the tRNA Lysine gene, leading to mitochondrial protein synthesis impairment and the lack of three critical CCO subunits. In both models we showed the complete absence of assembled CCO. PBM (660 nm) was applied to these proliferating cells using various parameters. In most of the conditions tested, increased cell proliferation was associated with PBM in both control and CCO negative cells, demonstrating that CCO is not required for PBM enhancement of cellular proliferation. Additional experiments showed that PBM increased both ATP levels and citrate synthase activity and levels. These results showed that although metabolic changes are associated with PBM, CCO is not required for its cell proliferation enhancing effect.

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Journal Details

This article was published in the following journal.

Name: Journal of photochemistry and photobiology. B, Biology
ISSN: 1873-2682
Pages: 71-75

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A multisubunit enzyme complex containing CYTOCHROME A GROUP; CYTOCHROME A3; two copper atoms; and 13 different protein subunits. It is the terminal oxidase complex of the RESPIRATORY CHAIN and collects electrons that are transferred from the reduced CYTOCHROME C GROUP and donates them to molecular OXYGEN, which is then reduced to water. The redox reaction is simultaneously coupled to the transport of PROTONS across the inner mitochondrial membrane.

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