H2S-Mediated Protein S-Sulfhydration: A Prediction for Its Formation and Regulation

Ju, Youngjun; Fu, Ming; Stokes, Eric; Wu, Lingyun; Yang, Guangdong

doi:10.3390/molecules22081334

Cited by 51 publications

(31 citation statements)

References 72 publications

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“…[ 14 ] It regulates the functions of various enzymes in cells, mainly by the modification of cysteine residues to form protein persulfides called S‐sulfhydration. [ 15 ] Previous studies have revealed that high concentration of exogenous H 2 S may induce the specific inhibition of cancer cells via cellular cycle arrest, miRNA regulation, mitochondrial damage, or uncontrolled intracellular acidification owing to the differences in metabolism and signaling pathway between cancer and normal cells. [ 16 ] More importantly, the recent exploration uncovered that H 2 S can regulate CAT activity in some types of plant cells and bacteria, and this effect can be highly varied depending on cell types.…”

Section: Figurementioning

confidence: 99%

FeS@BSA Nanoclusters to Enable H₂S‐Amplified ROS‐Based Therapy with MRI Guidance

et al. 2020

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Therapeutic systems to induce reactive oxygen species (ROS) have received tremendous success in the research of tumor theranostics, but suffered daunting challenges in limited efficacy originating from low presence of reactants and reaction kinetics within cancer cells. Here, ferrous sulfide‐embedded bovine serum albumin (FeS@BSA) nanoclusters, in an amorphous nature, are designed and synthesized via a self‐assembly approach. In acidic conditions, the nanoclusters degrade and simultaneously release H2S gas and Fe2+ ions. The in vitro study using Huh7 cancer cells reveals that Fe2+ released from FeS@BSA nanoclusters induces the toxic hydroxyl radical (·OH) effectively via the Fenton reaction. More interestingly, H2S gas released intracellularly presents the specific suppression effect to catalase activity of cancer cells, resulting in the promoted presence of H2O2 that facilitates the Fenton reaction of Fe2+ and consequently promotes ROS induction within the cells remarkably. After intravenous administration, the nanoclusters accumulate in the tumors of mice via the enhanced permeability and retention effect and present strong magnetic resonance imaging (MRI) signals. The findings confirm this therapeutic system can enable superior anti‐tumor performance with MRI guidance and negligible side effects. This study, therefore, offers an alternative gas‐amplified ROS‐based therapeutic platform for synergetic tumor treatment.

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Section: Figurementioning

confidence: 99%

FeS@BSA Nanoclusters to Enable H₂S‐Amplified ROS‐Based Therapy with MRI Guidance

et al. 2020

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“…To our knowledge, no information exists on the presence of H 2 S in plant or animal peroxisomes. However, proteomic studies of animals and plants have identified catalase as a potential target of persulfidation (Mustafa et al ; Aroca et al ), which is a post‐translational modification (PTM) mediated by H 2 S that modulates the function of target proteins (Iciek et al ; Ju et al ). Thus, this study mainly aims to evaluate the presence of H 2 S in plant peroxisomes and its potential biochemical implications.…”

Section: Introductionmentioning

confidence: 99%

Hydrogen sulfide: A novel component in Arabidopsis peroxisomes which triggers catalase inhibition

Corpas

Barroso

González‐Gordo

et al. 2019

JIPB

126

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Plant peroxisomes have the capacity to generate different reactive oxygen and nitrogen species (ROS and RNS), such as H 2 O 2 , superoxide radical (O 2 Á À ), nitric oxide and peroxynitrite (ONOO -). These organelles have an active nitrooxidative metabolism which can be exacerbated by adverse stress conditions. Hydrogen sulfide (H 2 S) is a new signaling gasotransmitter which can mediate the posttranslational modification (PTM) persulfidation. We used Arabidopsis thaliana transgenic seedlings expressing cyan fluorescent protein (CFP) fused to a canonical peroxisome targeting signal 1 (PTS1) to visualize peroxisomes in living cells, as well as a specific fluorescent probe which showed that peroxisomes contain H 2 S. H 2 S was also detected in chloroplasts under glyphosate-induced oxidative stress conditions. Peroxisomal enzyme activities, including catalase, photorespiratory H 2 O 2 -generating glycolate oxidase (GOX) and hydroxypyruvate reductase (HPR), were assayed in vitro with a H 2 S donor. In line with the persulfidation of this enzyme, catalase activity declined significantly in the presence of the H 2 S donor. To corroborate the inhibitory effect of H 2 S on catalase activity, we also assayed pure catalase from bovine liver and pepper fruit-enriched samples, in which catalase activity was inhibited. Taken together, these data provide evidence of the presence of H 2 S in plant peroxisomes which appears to regulate catalase activity and, consequently, the peroxisomal H 2 O 2 metabolism. . In plant systems, several enzymes are capable of generating H 2 S, which is part of the cysteine (Cys) metabolism. These enzymes, including L-and D-cysteine desulfhydrase (L-DES/D-DES), sulfite reductase (SiR), cyano alanine synthase (CAS) and cysteine synthase (CS) (Li et al. 2013; Calderwood and Kopriva 2014; Hancock and Whiteman 2014), are present in different subcellular compartments, such as cytosol, chloroplasts

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“…It is also well-known that -SH groups of some proteins can undergo reversible polysulfidation that influences their catalytic activity. S-nitrosylation and polysulfidation have similar mechanisms and occurred at acid-base motif [97]. Aside from S-nitrosylation of CaMKII at Cys6, it was recently reported that CaMKII is sensitive to inhibition by RSS through polysulfidation at Cys6, being competitive with ATP [98,99].…”

Section: Discussionmentioning

confidence: 99%

Coordination between Calcium/Calmodulin-Dependent Protein Kinase II and Neuronal Nitric Oxide Synthase in Neurons

Araki

Osuka

Takata

et al. 2020

IJMS

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Ca2+/calmodulin (CaM)-dependent protein kinase II (CaMKII) is highly abundant in the brain and exhibits broad substrate specificity, thereby it is thought to participate in the regulation of neuronal death and survival. Nitric oxide (NO), produced by neuronal NO synthase (nNOS), is an important neurotransmitter and plays a role in neuronal activity including learning and memory processes. However, high levels of NO can contribute to excitotoxicity following a stroke and neurodegenerative disease. Aside from NO, nNOS also generates superoxide which is involved in both cell injury and signaling. CaMKII is known to activate and translocate from the cytoplasm to the post-synaptic density in response to neuronal activation where nNOS is predominantly located. Phosphorylation of nNOS at Ser847 by CaMKII decreases NO generation and increases superoxide generation. Conversely, NO-induced S-nitrosylation of CaMKII at Cys6 is a prominent determinant of the CaMKII inhibition in ATP competitive fashion. Thus, the “cross-talk” between CaMKII and NO/superoxide may represent important signal transduction pathways in brain. In this review, we introduce the molecular mechanism of and pathophysiological role of mutual regulation between CaMKII and nNOS in neurons.

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H2S-Mediated Protein S-Sulfhydration: A Prediction for Its Formation and Regulation

Cited by 51 publications

References 72 publications

FeS@BSA Nanoclusters to Enable H₂S‐Amplified ROS‐Based Therapy with MRI Guidance

FeS@BSA Nanoclusters to Enable H₂S‐Amplified ROS‐Based Therapy with MRI Guidance

Hydrogen sulfide: A novel component in Arabidopsis peroxisomes which triggers catalase inhibition

Coordination between Calcium/Calmodulin-Dependent Protein Kinase II and Neuronal Nitric Oxide Synthase in Neurons

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H2S-Mediated Protein S-Sulfhydration: A Prediction for Its Formation and Regulation

Cited by 51 publications

References 72 publications

FeS@BSA Nanoclusters to Enable H2S‐Amplified ROS‐Based Therapy with MRI Guidance

FeS@BSA Nanoclusters to Enable H2S‐Amplified ROS‐Based Therapy with MRI Guidance

Hydrogen sulfide: A novel component in Arabidopsis peroxisomes which triggers catalase inhibition

Coordination between Calcium/Calmodulin-Dependent Protein Kinase II and Neuronal Nitric Oxide Synthase in Neurons

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FeS@BSA Nanoclusters to Enable H₂S‐Amplified ROS‐Based Therapy with MRI Guidance

FeS@BSA Nanoclusters to Enable H₂S‐Amplified ROS‐Based Therapy with MRI Guidance