Nox NADPH oxidases and the endoplasmic reticulum.
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Journal: 2014/December - Antioxidants and Redox Signaling
ISSN: 1557-7716
Abstract:
CONCLUSIONS
Understanding isoform- and context-specific subcellular Nox reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidase compartmentalization allows relevant functional inferences. This review addresses the interplay between Nox NADPH oxidases and the endoplasmic reticulum (ER), an increasingly evident player in redox pathophysiology given its role in redox protein folding and stress responses.
BACKGROUND
Catalytic/regulatory transmembrane subunits are synthesized in the ER and their processing includes folding, N-glycosylation, heme insertion, p22phox heterodimerization, as shown for phagocyte Nox2. Dual oxidase (Duox) maturation also involves the regulation by ER-resident Duoxa2. The ER is the activation site for some isoforms, typically Nox4, but potentially other isoforms. Such location influences redox/Nox-mediated calcium signaling regulation via ER targets, such as sarcoendoplasmic reticulum calcium ATPase (SERCA). Growing evidence suggests that Noxes are integral signaling elements of the unfolded protein response during ER stress, with Nox4 playing a dual prosurvival/proapoptotic role in this setting, whereas Nox2 enhances proapoptotic signaling. ER chaperones such as protein disulfide isomerase (PDI) closely interact with Noxes. PDI supports growth factor-dependent Nox1 activation and mRNA expression, as well as migration in smooth muscle cells, and PDI overexpression induces acute spontaneous Nox activation.
RESULTS
Mechanisms of PDI effects include possible support of complex formation and RhoGTPase activation. In phagocytes, PDI supports phagocytosis, Nox activation, and redox-dependent interactions with p47phox. Together, the results implicate PDI as possible Nox organizer.
CONCLUSIONS
We propose that convergence between Noxes and ER may have evolutive roots given ER-related functional contexts, which paved Nox evolution, namely calcium signaling and pathogen killing. Overall, the interplay between Noxes and the ER may provide relevant insights in Nox-related (patho)physiology.
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Antioxid Redox Signal 20(17): 2755-2775
PMID: 24386930

Nox NADPH Oxidases and the Endoplasmic Reticulum

Vascular Biology Laboratory, Heart Institute (InCor), University of São Paulo School of Medicine, São Paulo, Brazil.
Corresponding author.
Address correspondence to:, Prof. Francisco R.M. Laurindo, Vascular Biology Laboratory, Heart Institute (InCor), University of São Paulo School of Medicine, Av Eneas C Aguiar, 44-Annex 2, 9th floor, São Paulo, CEP 05403-000, Brazil,
E-mail:rb.psu.rocni@odnirual.ocsicnarf
Address correspondence to:, Prof. Francisco R.M. Laurindo, Vascular Biology Laboratory, Heart Institute (InCor), University of São Paulo School of Medicine, Av Eneas C Aguiar, 44-Annex 2, 9th floor, São Paulo, CEP 05403-000, Brazil,
E-mail:rb.psu.rocni@odnirual.ocsicnarf
Received 2013 Sep 6; Revised 2013 Dec 17; Accepted 2014 Jan 5.
Copyright 2014, Mary Ann Liebert, Inc.

Abstract

Significance: Understanding isoform- and context-specific subcellular Nox reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidase compartmentalization allows relevant functional inferences. This review addresses the interplay between Nox NADPH oxidases and the endoplasmic reticulum (ER), an increasingly evident player in redox pathophysiology given its role in redox protein folding and stress responses. Recent Advances: Catalytic/regulatory transmembrane subunits are synthesized in the ER and their processing includes folding, N-glycosylation, heme insertion, p22phox heterodimerization, as shown for phagocyte Nox2. Dual oxidase (Duox) maturation also involves the regulation by ER-resident Duoxa2. The ER is the activation site for some isoforms, typically Nox4, but potentially other isoforms. Such location influences redox/Nox-mediated calcium signaling regulation via ER targets, such as sarcoendoplasmic reticulum calcium ATPase (SERCA). Growing evidence suggests that Noxes are integral signaling elements of the unfolded protein response during ER stress, with Nox4 playing a dual prosurvival/proapoptotic role in this setting, whereas Nox2 enhances proapoptotic signaling. ER chaperones such as protein disulfide isomerase (PDI) closely interact with Noxes. PDI supports growth factor-dependent Nox1 activation and mRNA expression, as well as migration in smooth muscle cells, and PDI overexpression induces acute spontaneous Nox activation. Critical Issues: Mechanisms of PDI effects include possible support of complex formation and RhoGTPase activation. In phagocytes, PDI supports phagocytosis, Nox activation, and redox-dependent interactions with p47phox. Together, the results implicate PDI as possible Nox organizer. Future Directions: We propose that convergence between Noxes and ER may have evolutive roots given ER-related functional contexts, which paved Nox evolution, namely calcium signaling and pathogen killing. Overall, the interplay between Noxes and the ER may provide relevant insights in Nox-related (patho)physiology. Antioxid. Redox Signal. 20, 2755–2775.

Abstract

Abbreviations Used

Aktprotein kinase B
AngIIangiotensin II
c-AblAbelson murine leukemia viral oncogene homolog
CAMKIIcalcium/calmodulin-dependent protein kinase II
CHOPCCAT/enhancer binding protein homologous protein
cyscysteine
DCF2′,7′-dichlorofluorescein
Duoxdual oxidase
EGFepidermal growth factor
ERendoplasmic reticulum
ERADER-associated degradation
Ero-1ER oxidoreductin 1
Erp46endoplasmic reticulum protein 46
FADflavin adenine dinucleotide
GFPgreen fluorescent protein
Grpglucose-regulated protein
GTPaseguanosine triphosphate hidrolase enzyme
HAEChuman aortic endothelial cell
Hsp90heat shock protein 90
HUVEChuman umbilical vein endothelial cell
IFimmunofluorescence
JNKc-Jun N-terminal kinases
KOknockout
LPSlipopolysaccharide
NADPHreduced nicotinamide adenine dinucleotide phosphate
NOnitric oxide
PDIprotein disulfide isomerase
PMAphorbol myristate acetate
PTP-1Bprotein-tyrosine phosphatase-1B
ROSreactive oxygen species
SERCAsarcoendoplasmic reticulum calcium ATPase
STAT5signal transducer and activator of transcription 5
Tgtransgenic
TGF-βtransforming growth factor beta
TIRFtotal internal reflection fluorescence
UPRunfolded protein response
VEGFvascular endothelial growth factor
VSMCvascular smooth muscle cells
Abbreviations Used

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