Determination of the metabolic index using the fluorescence lifetime of free and bound nicotinamide adenine dinucleotide using the phasor approach.
FLIM
NADH
TCSPC
autofluorescence
lifetime
phasor
Journal
Journal of biophotonics
ISSN: 1864-0648
Titre abrégé: J Biophotonics
Pays: Germany
ID NLM: 101318567
Informations de publication
Date de publication:
11 2019
11 2019
Historique:
received:
27
04
2019
revised:
09
06
2019
accepted:
12
06
2019
pubmed:
14
6
2019
medline:
21
10
2020
entrez:
14
6
2019
Statut:
ppublish
Résumé
The fluorescence lifetime of nicotinamide adenine dinucleotide (NADH) is commonly used in conjunction with the phasor approach as a molecular biomarker to provide information on cellular metabolism of autofluorescence imaging of cells and tissue. However, in the phasor approach, the bound and free lifetime defining the phasor metabolic trajectory is a subject of debate. The fluorescence lifetime of NADH increases when bound to an enzyme, in contrast to the short multiexponential lifetime displayed by NADH in solution. The extent of fluorescence lifetime increase depends on the enzyme to which NADH is bound. With proper preparation of lactate dehydrogenase (LDH) using oxalic acid (OA) as an allosteric factor, bound NADH to LDH has a lifetime of 3.4 ns and is positioned on the universal semicircle of the phasor plot, inferring a monoexponential lifetime for this species. Surprisingly, measurements in the cellular environments with different metabolic states show a linear trajectory between free NADH at about 0.37 ns and bound NADH at 3.4 ns. These observations support that in a cellular environment, a 3.4 ns value could be used for bound NADH lifetime. The phasor analysis of many cell types shows a linear combination of fractional contributions of free and bound species NADH.
Identifiants
pubmed: 31194290
doi: 10.1002/jbio.201900156
pmc: PMC6842045
mid: NIHMS1042270
doi:
Substances chimiques
NAD
0U46U6E8UK
L-Lactate Dehydrogenase
EC 1.1.1.27
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
e201900156Subventions
Organisme : NIAMS NIH HHS
ID : P30 AR075047
Pays : United States
Organisme : NIGMS NIH HHS
ID : P41 GM103540
Pays : United States
Organisme : NIGMS NIH HHS
ID : P50 GM076516
Pays : United States
Organisme : NIH HHS
ID : P41-GM103540
Pays : United States
Informations de copyright
© 2019 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
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