skip to main content
Guest
e-Shelf
My Account
Sign out
Sign in
This feature requires javascript
Tags
e-Journals
e-Books
Databases
USP Libraries
Help
Help
Language:
English
Spanish
Portuguese (Brazil)
This feature required javascript
This feature requires javascript
Primo Search
General Search
General Search
Physical Collection
Physical Collections
USP Intelectual Production
USP Production
Search For:
Clear Search Box
Search in:
General Search
Or hit Enter to replace search target
Or select another collection:
Search in:
General Search
Advanced Search
Browse Search
This feature requires javascript
Resource type
criteria input
anywhere in the record
in the title
as author/creator
in subject
Creation Date
lsr01
lsr02
lsr03
lsr04
Supervisor
Show Results with:
in the title
Show Results with:
anywhere in the record
in the title
as author/creator
in subject
Creation Date
lsr01
lsr02
lsr03
lsr04
Supervisor
Show Results with:
criteria input
that contain my query words
with my exact phrase
starts with
Show Results with:
Index
criteria input
AND
OR
NOT
This feature requires javascript
Investigating mitochondrial redox state using NADH and NADPH autofluorescence
Blacker, Thomas S. ; Duchen, Michael R.
Free radical biology & medicine, 2016-11, Vol.100, p.53-65
[Peer Reviewed Journal]
United States: Elsevier Inc
Full text available
Citations
Cited by
View Online
Details
Reviews & Tags
More
Times Cited
This feature requires javascript
Actions
Add to e-Shelf
Remove from e-Shelf
E-mail
Print
Permalink
Citation
EasyBib
EndNote
RefWorks
Delicious
Export RIS
Export BibTeX
This feature requires javascript
Title:
Investigating mitochondrial redox state using NADH and NADPH autofluorescence
Author:
Blacker, Thomas S.
;
Duchen, Michael R.
Subjects:
Energy Metabolism
;
FLIM
;
Fluorescence
;
Humans
;
Microscopy
;
Microscopy, Fluorescence - methods
;
Mitochondria
;
Mitochondria - metabolism
;
NAD - chemistry
;
NAD - metabolism
;
Nadh
;
NADP - chemistry
;
NADP - metabolism
;
Nadph
;
Oxidation-Reduction
;
Redox
;
Review
Is Part Of:
Free radical biology & medicine, 2016-11, Vol.100, p.53-65
Notes:
ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
Description:
The redox states of the NAD and NADP pyridine nucleotide pools play critical roles in defining the activity of energy producing pathways, in driving oxidative stress and in maintaining antioxidant defences. Broadly speaking, NAD is primarily engaged in regulating energy-producing catabolic processes, whilst NADP may be involved in both antioxidant defence and free radical generation. Defects in the balance of these pathways are associated with numerous diseases, from diabetes and neurodegenerative disease to heart disease and cancer. As such, a method to assess the abundance and redox state of these separate pools in living tissues would provide invaluable insight into the underlying pathophysiology. Experimentally, the intrinsic fluorescence of the reduced forms of both redox cofactors, NADH and NADPH, has been used for this purpose since the mid-twentieth century. In this review, we outline the modern implementation of these techniques for studying mitochondrial redox state in complex tissue preparations. As the fluorescence spectra of NADH and NADPH are indistinguishable, interpreting the signals resulting from their combined fluorescence, often labelled NAD(P)H, can be complex. We therefore discuss recent studies using fluorescence lifetime imaging microscopy (FLIM) which offer the potential to discriminate between the two separate pools. This technique provides increased metabolic information from cellular autofluorescence in biomedical investigations, offering biochemical insights into the changes in time-resolved NAD(P)H fluorescence signals observed in diseased tissues. •NAD plays a central role in energy-producing pathways.•NADP is crucial for maintaining the antioxidant defence.•The reduced forms, NADH and NADPH, are naturally fluorescent inside living tissues.•Cellular autofluorescence can be used to investigate NAD(P)H redox state.•NAD(P)H FLIM allows the contributions from NADH and NADPH to be separated.
Publisher:
United States: Elsevier Inc
Language:
English
Links
View this record in MEDLINE/PubMed
This feature requires javascript
This feature requires javascript
Back to results list
Previous
Result
5
Next
This feature requires javascript
This feature requires javascript
Searching Remote Databases, Please Wait
Searching for
in
scope:(USP_VIDEOS),scope:("PRIMO"),scope:(USP_FISICO),scope:(USP_EREVISTAS),scope:(USP),scope:(USP_EBOOKS),scope:(USP_PRODUCAO),primo_central_multiple_fe
Show me what you have so far
This feature requires javascript
This feature requires javascript