Nitric oxide in cellular adaptation and disease

Gantner, Benjamin N.; LaFond, Katy M.; Bonini, Marcelo G.

doi:10.1016/j.redox.2020.101550

Cited by 140 publications

(79 citation statements)

References 141 publications

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“…In skeletal muscle tissues, nitric oxide levels are low under resting conditions and the production rate of this signaling molecule is greatly enhanced during repetitive muscle contractions. Crucial regulatory functions of nitric oxide in skeletal muscle include auto-regulation of blood flow, metabolic and bioenergetic integration at the level of glucose homeostasis and mitochondrial respiration, modulation of excitation–contraction coupling and contractile force generation, as well as myocyte differentiation [ 135 , 136 ]. The influence of nitric oxide on skeletal muscle function involves changes in redox-sensitive protein species, the activation of the second messenger molecule cyclic guanosine monophosphate and interactions with reactive oxygen species [ 135 ].…”

Section: Proteomic and Biochemical Characterization Of The Dystropmentioning

confidence: 99%

The Dystrophin Node as Integrator of Cytoskeletal Organization, Lateral Force Transmission, Fiber Stability and Cellular Signaling in Skeletal Muscle

et al. 2021

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The systematic bioanalytical characterization of the protein product of the DMD gene, which is defective in the pediatric disorder Duchenne muscular dystrophy, led to the discovery of the membrane cytoskeletal protein dystrophin. Its full-length muscle isoform Dp427-M is tightly linked to a sarcolemma-associated complex consisting of dystroglycans, sarcoglyans, sarcospan, dystrobrevins and syntrophins. Besides these core members of the dystrophin–glycoprotein complex, the wider dystrophin-associated network includes key proteins belonging to the intracellular cytoskeleton and microtubular assembly, the basal lamina and extracellular matrix, various plasma membrane proteins and cytosolic components. Here, we review the central role of the dystrophin complex as a master node in muscle fibers that integrates cytoskeletal organization and cellular signaling at the muscle periphery, as well as providing sarcolemmal stabilization and contractile force transmission to the extracellular region. The combination of optimized tissue extraction, subcellular fractionation, advanced protein co-purification strategies, immunoprecipitation, liquid chromatography and two-dimensional gel electrophoresis with modern mass spectrometry-based proteomics has confirmed the composition of the core dystrophin complex at the sarcolemma membrane. Importantly, these biochemical and mass spectrometric surveys have identified additional members of the wider dystrophin network including biglycan, cavin, synemin, desmoglein, tubulin, plakoglobin, cytokeratin and a variety of signaling proteins and ion channels.

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Section: Proteomic and Biochemical Characterization Of The Dystropmentioning

confidence: 99%

The Dystrophin Node as Integrator of Cytoskeletal Organization, Lateral Force Transmission, Fiber Stability and Cellular Signaling in Skeletal Muscle

et al. 2021

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“…In aerobic organisms, RONS are constantly produced by the mitochondrial oxidative phosphorylation (OXPHOS) system and by several enzymes [e.g., NADPH oxidases (NOXs) and nitric oxide synthases (NOSs); Ignarro, 1990 ; Raha and Robinson, 2000 ; Forman et al, 2002 ; Bian and Murad, 2003 ; Murphy, 2009 ; Lambeth and Neish, 2014 ; Nayernia et al, 2014 ; Di Meo et al, 2016 ; Ma et al, 2017 ; Moldogazieva et al, 2018 ; Barua et al, 2019 ; Sbodio et al, 2019 ; Gantner et al, 2020 ]. Some of the major RONS include hydrogen peroxide (H 2 O 2 ), hydroxyl radical (•OH), superoxide anion (O 2 •− ), peroxyl radical (ROO • ), singlet oxygen ( 1 O 2 ), nitic oxide or nitrogen monoxide ( • NO), nitrogen dioxide ( • NO 2 ), and peroxynitrite (ONOO − ; Commoner et al, 1954 ; McCord, 2000 ; Forman et al, 2002 ; Pham-Huy et al, 2008 ; Di Meo et al, 2016 ; Sbodio et al, 2019 ).…”

Section: Introductionmentioning

confidence: 99%

Redox Post-translational Modifications of Protein Thiols in Brain Aging and Neurodegenerative Conditions—Focus on S-Nitrosation

Finelli

2020

Front. Aging Neurosci.

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Reactive oxygen species and reactive nitrogen species (RONS) are by-products of aerobic metabolism. RONS trigger a signaling cascade that can be transduced through oxidation-reduction (redox)-based post-translational modifications (redox PTMs) of protein thiols. This redox signaling is essential for normal cellular physiology and coordinately regulates the function of redox-sensitive proteins. It plays a particularly important role in the brain, which is a major producer of RONS. Aberrant redox PTMs of protein thiols can impair protein function and are associated with several diseases. This mini review article aims to evaluate the role of redox PTMs of protein thiols, in particular S-nitrosation, in brain aging, and in neurodegenerative diseases. It also discusses the potential of using redox-based therapeutic approaches for neurodegenerative conditions.

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“…NO is widespread in mammalian and plant cells. In mammalian cells, NO is an essential biological signalling molecule playing an important role in the regulation of nervous, vascular, and immune systems [ 47 ]. In plant cells, NO is also involved in many physiological processes such as plant-microbe interactions, seed germination, root and pollen tube growth, stomatal closure, flowering, iron homeostasis, programmed cell death, and adaptive responses to biotic as well as abiotic stressors [ 48 ].…”

Section: Discussionmentioning

confidence: 99%

Genetic engineering of circularly permuted yellow fluorescent protein reveals intracellular acidification in response to nitric oxide stimuli

Deng

Zhou

et al. 2021

Redox Biology

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Intracellular pH (pHi) is a crucial parameter in cell biology; thus, a series of pH probes have been developed to determine pHi changes in living cells. However, more sensitive and non-perturbing ratiometric pH probes are needed for accurate pHi measurements. While the fluorescence of circular permutated YFP (cpYFP) is hypersensitive to pH changes due to its intrinsic properties, the single excitation peak of this protein restricts its capacity of becoming a rational type of pH sensor. Herein, we collected several cpYFP-based probes with dual excitation peaks and constructed their corresponding loss-of-function mutants to screen for a potential competent pH probe. The most sensitive probe was named NocPer. NocPer consists of cpYFP inserted into inactive-mutated GAF and AAA + , which are two regulatory domains of E. coli NorR, a nitric oxide (NO)-specific transcription factor. Fluorescence emission of NocPer peaks at 517 nm while exhibiting dual excitation peaks at 420 and 495 nm, which can be used for ratiometric imaging. This new pH sensor has a large ratio response dynamic (pH range of 7.0–11.0), which covers the physiological pH range (pH 7.0–8.0), and exhibits an approximately 3-fold higher fluorescent signal in response to a pH increase from 7.0 to 8.0 than that of pHluorin. Using NocPer, we discovered a new biological phenomenon in which NO exposure decreases the E. coli pHi, which led to the hypothesis that pathogens decrease their own pHi during infection. Further, we elucidated that the NO-induced inhibition of cytochrome c oxidase in the respiratory chain is responsible for the decline in pHi, which might represent a protective strategy of E. coli under NO stress conditions. Our results demonstrated that NocPer is a ratiometric pH probe with high sensitivity for the physiological pH range.

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Nitric oxide in cellular adaptation and disease

Cited by 140 publications

References 141 publications

The Dystrophin Node as Integrator of Cytoskeletal Organization, Lateral Force Transmission, Fiber Stability and Cellular Signaling in Skeletal Muscle

The Dystrophin Node as Integrator of Cytoskeletal Organization, Lateral Force Transmission, Fiber Stability and Cellular Signaling in Skeletal Muscle

Redox Post-translational Modifications of Protein Thiols in Brain Aging and Neurodegenerative Conditions—Focus on S-Nitrosation

Genetic engineering of circularly permuted yellow fluorescent protein reveals intracellular acidification in response to nitric oxide stimuli

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