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Article

Bioenergetic Alterations of Metabolic Redox Coenzymes as NADH, FAD and FMN by Means of Fluorescence Lifetime Imaging Techniques

by
Sviatlana Kalinina
1,*,
Christian Freymueller
2,3,
Nilanjon Naskar
1,
Bjoern von Einem
4,
Kirsten Reess
1,
Ronald Sroka
2,3 and
Angelika Rueck
1,*
1
Core Facility Confocal and Multiphoton Microscopy, Ulm University, Albert-Einstein-Allee 11, 89081 Ulm, Germany
2
Laser-Forschungslabor, LIFE Center, University Hospital, LMU Munich, Fraunhoferstrasse 20, 82152 Planegg, Germany
3
Department of Urology, University Hospital, LMU Munich, Marchioninistraße 15, 81377 Munich, Germany
4
Zentrum Biomedizinische Forschung (ZBMF), Department of Neurology, Ulm University, Helmholtzstrasse, 8/1, 89081 Ulm, Germany
*
Authors to whom correspondence should be addressed.
Int. J. Mol. Sci. 2021, 22(11), 5952; https://doi.org/10.3390/ijms22115952
Submission received: 18 May 2021 / Revised: 26 May 2021 / Accepted: 28 May 2021 / Published: 31 May 2021
(This article belongs to the Special Issue New Insights on Cell Metabolism)
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Abstract

Metabolic FLIM (fluorescence lifetime imaging) is used to image bioenergetic status in cells and tissue. Whereas an attribution of the fluorescence lifetime of coenzymes as an indicator for cell metabolism is mainly accepted, it is debated whether this is valid for the redox state of cells. In this regard, an innovative algorithm using the lifetime characteristics of nicotinamide adenine dinucleotide (phosphate) (NAD(P)H) and flavin adenine dinucleotide (FAD) to calculate the fluorescence lifetime induced redox ratio (FLIRR) has been reported so far. We extended the FLIRR approach and present new results, which includes FLIM data of the various enzymes, such as NAD(P)H, FAD, as well as flavin mononucleotide (FMN). Our algorithm uses a two-exponential fitting procedure for the NAD(P)H autofluorescence and a three-exponential fit of the flavin signal. By extending the FLIRR approach, we introduced FLIRR1 as protein-bound NAD(P)H related to protein-bound FAD, FLIRR2 as protein-bound NAD(P)H related to free (unbound) FAD and FLIRR3 as protein-bound NAD(P)H related to protein-bound FMN. We compared the significance of extended FLIRR to the metabolic index, defined as the ratio of protein-bound NAD(P)H to free NAD(P)H. The statistically significant difference for tumor and normal cells was found to be highest for FLIRR1.
Keywords: FLIM; NAD(P)H; FAD; FMN; NAD(P)H metabolic index; FLIRR index; extended FLIRR; cell metabolism; OXPHOS; glycolysis FLIM; NAD(P)H; FAD; FMN; NAD(P)H metabolic index; FLIRR index; extended FLIRR; cell metabolism; OXPHOS; glycolysis

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MDPI and ACS Style

Kalinina, S.; Freymueller, C.; Naskar, N.; von Einem, B.; Reess, K.; Sroka, R.; Rueck, A. Bioenergetic Alterations of Metabolic Redox Coenzymes as NADH, FAD and FMN by Means of Fluorescence Lifetime Imaging Techniques. Int. J. Mol. Sci. 2021, 22, 5952. https://doi.org/10.3390/ijms22115952

AMA Style

Kalinina S, Freymueller C, Naskar N, von Einem B, Reess K, Sroka R, Rueck A. Bioenergetic Alterations of Metabolic Redox Coenzymes as NADH, FAD and FMN by Means of Fluorescence Lifetime Imaging Techniques. International Journal of Molecular Sciences. 2021; 22(11):5952. https://doi.org/10.3390/ijms22115952

Chicago/Turabian Style

Kalinina, Sviatlana, Christian Freymueller, Nilanjon Naskar, Bjoern von Einem, Kirsten Reess, Ronald Sroka, and Angelika Rueck. 2021. "Bioenergetic Alterations of Metabolic Redox Coenzymes as NADH, FAD and FMN by Means of Fluorescence Lifetime Imaging Techniques" International Journal of Molecular Sciences 22, no. 11: 5952. https://doi.org/10.3390/ijms22115952

APA Style

Kalinina, S., Freymueller, C., Naskar, N., von Einem, B., Reess, K., Sroka, R., & Rueck, A. (2021). Bioenergetic Alterations of Metabolic Redox Coenzymes as NADH, FAD and FMN by Means of Fluorescence Lifetime Imaging Techniques. International Journal of Molecular Sciences, 22(11), 5952. https://doi.org/10.3390/ijms22115952

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