scholarly journals S-sulfhydration as a cellular redox regulation

2016 ◽  
Vol 36 (2) ◽  
Author(s):  
Małgorzata Iciek ◽  
Danuta Kowalczyk-Pachel ◽  
Anna Bilska-Wilkosz ◽  
Inga Kwiecień ◽  
Magdalena Górny ◽  
...  
Keyword(s):  
Protein Function ◽  
Redox Regulation ◽  
Biological Significance ◽  
Redox Signaling ◽  
Sulfur Species ◽  
Cellular Redox ◽  
Reactive Sulfur Species

This review is focused on formation and biological significance of hydropersulfides, i.e. S-sulfhydration process. Biogenesis and properties of reactive sulfur species and their role in redox signaling are presented. The effect of S-sulfhydration on protein function is discussed.

scholarly journals Redox signaling regulated by electrophiles and reactive sulfur species

2016 ◽  
Vol 58 (2) ◽  
pp. 91-98 ◽  
Author(s):  
Motohiro Nishida ◽  
Yoshito Kumagai ◽  
Hideshi Ihara ◽  
Shigemoto Fujii ◽  
Hozumi Motohashi ◽  
...  
Keyword(s):  
Redox Signaling ◽  
Sulfur Species ◽  
Reactive Sulfur Species

scholarly journals Spatial and temporal alterations in protein structure by EGF regulate cryptic cysteine oxidation

2019 ◽  
Author(s):  
Jessica B Behring ◽  
Sjoerd van der Post ◽  
Arshag D Mooradian ◽  
Matthew J Egan ◽  
Maxwell I Zimmerman ◽  
...  
Keyword(s):  
Tyrosine Kinases ◽  
Redox Regulation ◽  
Receptor Tyrosine Kinases ◽  
Redox Signaling ◽  
Signaling Networks ◽  
Cysteine Oxidation ◽  
Time Resolved ◽  
Cellular Redox ◽  
Redox Biology ◽  
Stimulation Of

AbstractStimulation of receptor tyrosine kinases (RTK) such as EGF locally increase reactive oxygen species (ROS) levels at the plasma membrane that oxidize cysteines in proteins to enhance downstream signaling. Spatial confinement of ROS is an important regulatory mechanism to redox signaling, but it remains unknown why stimulation of different receptor tyrosine kinases (RTKs) at the plasma membrane target distinct sets of downstream proteins. To uncover additional mechanisms specifying which cysteines are redox regulated by EGF stimulation, we performed time-resolved quantification of the oxidation of 4,200 cysteine sites subsequent to EGF stimulation in A431 cells. EGF induces three distinct spatiotemporal patterns of cysteine oxidation in functionally organized protein networks, consistent with the spatial confinement model. Unexpectedly, protein crystal structure analysis and molecular dynamic simulation indicate widespread redox regulation of cryptic cysteines that are only solvent exposed upon changes in protein conformation. Phosphorylation and increased flux of nucleotide substrates serve as two distinct modes by which EGF specifies which cryptic cysteines become solvent exposed and redox regulated. Since proteins structurally regulated by different RTKs or cellular perturbations are largely unique, solvent exposure and redox regulation of cryptic cysteines is an important mechanism contextually delineating redox signaling networks.Significance StatementCellular redox processes are interconnected, but are not in equilibrium. Thus, understanding the redox biology of cells requires a systems-level, rather than reductionist, approach. Factors specifying which cysteines are redox regulated by a stimulus remain poorly characterized but are critical to understanding the fundamental properties of redox signaling networks. Here, we show that EGF stimulation induces oxidation of specific cysteines in 3 distinct spatiotemporal patterns. Redox regulated proteins include many proteins in the EGF pathway as well as many cysteines with known functional importance. Many redox regulated cysteines are cryptic and solvent exposed by changes in protein structure that were induced by EGF treatment. The novel finding that cryptic cysteines are redox regulated has important implications for how redox signaling networks are specified and regulated to minimize crosstalk. In addition, this time-resolved dataset of the redox kinetics of 4,200 cysteine sites is an important resource for others and is an important technological achievement towards systems-level understanding of cellular redox biology.

scholarly journals Redox Regulation of Lipid Mobilization in Adipose Tissues

Antioxidants ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1090
Author(s):  
Ursula Abou-Rjeileh ◽  
G. Andres Contreras
Keyword(s):  
Adipose Tissue ◽  
Energy Metabolism ◽  
Redox Regulation ◽  
Cellular Metabolism ◽  
Antioxidant Response ◽  
Redox Signaling ◽  
Nitrogen Species ◽  
Adipose Tissues ◽  
Lipid Mobilization ◽  
Cellular Processes

Lipid mobilization in adipose tissues, which includes lipogenesis and lipolysis, is a paramount process in regulating systemic energy metabolism. Reactive oxygen and nitrogen species (ROS and RNS) are byproducts of cellular metabolism that exert signaling functions in several cellular processes, including lipolysis and lipogenesis. During lipolysis, the adipose tissue generates ROS and RNS and thus requires a robust antioxidant response to maintain tight regulation of redox signaling. This review will discuss the production of ROS and RNS within the adipose tissue, their role in regulating lipolysis and lipogenesis, and the implications of antioxidants on lipid mobilization.

scholarly journals Metabolism of hydrogen sulfide (H2S) and Production of Reactive Sulfur Species (RSS) by superoxide dismutase

Redox Biology ◽  
2018 ◽  
Vol 15 ◽  
pp. 74-85 ◽  
Author(s):  
Kenneth R. Olson ◽  
Yan Gao ◽  
Faihaan Arif ◽  
Kanika Arora ◽  
Shivali Patel ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Hydrogen Sulfide ◽  
Sulfur Species ◽  
Reactive Sulfur Species

scholarly journals Cell type-specific differences in redox regulation and proliferation after low UVA doses

2018 ◽  
Author(s):  
Sylwia Ciesielska ◽  
Patryk Bil ◽  
Karolina Gajda ◽  
Aleksandra Poterala-Hejmo ◽  
Dorota Hudy ◽  
...  
Keyword(s):  
Reactive Oxygen Species ◽  
Redox Regulation ◽  
Cellular Proliferation ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Cell Type ◽  
Redox Systems ◽  
Human Colon Cancer ◽  
Cellular Redox ◽  
Hct116 Cells

AbstractUltraviolet A (UVA) radiation is harmful for living organisms but in low doses may stimulate cell proliferation. Our aim was to examine the relationships between exposure to different low UVA doses, cellular proliferation, and changes in cellular reactive oxygen species levels. In human colon cancer (HCT116) and melanoma (Me45) cells exposed to UVA doses comparable to environmental, the highest doses (30-50 kJ/m2) reduced clonogenic potential but some lower doses (1 and 10 kJ/m2) induced proliferation. This effect was cell type and dose specific. In both cell lines the levels of reactive oxygen species and nitric oxide fluctuated with dynamics which were influenced differently by UVA; in Me45 cells decreased proliferation accompanied the changes in the dynamics of H2O2 while in HCT116 cells those of superoxide. Genes coding for proteins engaged in redox systems were expressed differently in each cell line; transcripts for thioredoxin, peroxiredoxin and glutathione peroxidase showed higher expression in HCT116 cells whereas those for glutathione transferases and copper chaperone were more abundant in Me45 cells. We conclude that these two cell types utilize different pathways for regulating their redox status. Many mechanisms engaged in maintaining cellular redox balance have been described. Here we show that the different cellular responses to a stimulus such as a specific dose of UVA may be consequences of the use of different redox control pathways. Assays of superoxide and hydrogen peroxide level changes after exposure to UVA may clarify mechanisms of cellular redox regulation and help in understanding responses to stressing factors.

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