Photobiomodulation of Na,K-ATPase in native membrane fraction and reconstituted in DPPC:DPPE-liposome.

Abstract

Studies focusing on how photobiomodulation (PBM) can affect the structure and function of proteins are scarce in the literature. Few previous studies have shown that the enzymatic activity of Na,K-ATPAse (NKA) can be photo-modulated. However, the variability of sample preparation and light irradiation wavelengths have not allowed for an unequivocal conclusion about the PBM of NKA. Here, we investigate minimal membrane models containing NKA, namely, native membrane fraction and DPPC:DPPE proteoliposome upon laser irradiation at wavelengths 532, 650, and 780 nm. Interestingly, we show that the PBM on the NKA enzymatic activity has a bell-shaped profile with a stimulation peak (~15% increase) at around 20 J.cm^-2 and 6 J.cm^-2 for the membrane-bound and the proteoliposome samples, respectively, and are practically wavelength independent. Further, by normalizing the enzymatic activity by the NKA enzyme concentration, we show that the PBM response is related to the protein amount with small influence due to protein's environment. The stimulation decays over time reaching the basal level around 6 h after the irradiation for the three lasers and both NKA samples. Our results demonstrate the potential of using low-level laser therapy to modulate NKA activity, which may have therapeutic implications and benefits.