Endogenous S-sulfhydration of PTEN helps protect against modification by nitric oxide

Ohno, Kazuki; Okuda, Kosaku; Uehara, Takashi

doi:10.1016/j.bbrc.2014.11.066

Cited by 45 publications

(24 citation statements)

References 16 publications

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“…The CySSO 2 H (perthiosulfinic) and CySSO 3 H (perthiosulfonic) oxidation products of persulfides can be recycled back by the reduction of their S-S moieties, which does not occur in the case of the CySO3H oxidation product of unmodified (unsulfhydrated) cysteine residues on proteins. We originally proposed this protective function of sulfhydration [2], which was tested in the case of phosphatase and tensin homolog deleted on chromosome 10, PTEN [32]. …”

Section: Protein Sulfhydrationmentioning

confidence: 99%

H 2 S: A Novel Gasotransmitter that Signals by Sulfhydration

Paul

Snyder

2015

Trends in Biochemical Sciences

287

231

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Hydrogen sulfide is a member of the growing family of gasotransmitters. Once regarded as a noxious molecule predominantly present in the atmosphere, H2S is now known to be synthesized endogenously in mammals. H2S participates in a myriad of physiological processes ranging from regulation of blood pressure to neuroprotection. Its chemical nature precludes H2S from being stored in vesicles and acting on receptor proteins in the fashion of other chemical messengers. Thus, novel cellular mechanisms have evolved to mediate its effects. This article focuses on sulfhydration (or persulfidation), which appears to be the principal post-translational modification elicited by H2S.

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Section: Protein Sulfhydrationmentioning

confidence: 99%

H 2 S: A Novel Gasotransmitter that Signals by Sulfhydration

Paul

Snyder

2015

Trends in Biochemical Sciences

287

231

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“…H 2 S regulated vaso-relaxation in spontaneously hypertensive rats through the inhibition of FOXO1 and FOXO3 phosphorylation, which resulted in their nuclear translocation and their binding to target gene promotors [177]. H 2 S was also shown to function as an endogenous regulator of PTEN, the main antagonist of the PI3K-Akt axis in the insulin/IGF-1 signal pathway, by modifying PTEN activity through S-sulfhydration [178, 179]. Following incubation with H 2 S, oral keratinocyte stem cells increased their PTEN expression [180].…”

Section: Hydrogen Sulfide and Agingmentioning

confidence: 99%

The role of hydrogen sulfide in aging and age-related pathologies

Perridon

Leuvenink

Hillebrands

et al. 2016

Aging

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When humans grow older, they experience inevitable and progressive loss of physiological function, ultimately leading to death. Research on aging largely focuses on the identification of mechanisms involved in the aging process. Several proposed aging theories were recently combined as the ‘hallmarks of aging’. These hallmarks describe (patho-)physiological processes that together, when disrupted, determine the aging phenotype. Sustaining evidence shows a potential role for hydrogen sulfide (H2S) in the regulation of aging.Nowadays, H2S is acknowledged as an endogenously produced signaling molecule with various (patho-) physiological effects. H2S is involved in several diseases including pathologies related to aging. In this review, the known, assumed and hypothetical effects of hydrogen sulfide on the aging process will be discussed by reviewing its actions on the hallmarks of aging and on several age-related pathologies.

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“…Many protein sites have been reported to undergo both S-nitrosylation and S-sulfhydration (brought by H 2 S), such as Actin [93,94], GAPDH [95], Parkin [96], PTEN [97], and the p65 subunit of NF-κB [98]. If S-sulfhydration and nitrosylation may occur on the same residue [99], reactive site cysteine, they generally promote different and opposing effects.…”

Section: A Yin-yang Relationship For S-nitrosylation and S-sulfhydratmentioning

confidence: 99%

“…reported to maintain the activity of this lipid tyrosine-phosphatase, thereby preventing its S-nitrosylation [97]. PTEN structure reports disparate sites for S-nitrosylation (Cys 83 [100]), S-sulfhydration, and hydrogen peroxide-induced disulfide bond formation (Cys 71 and Cys 124 [103]).…”

Section: A Yin-yang Relationship For S-nitrosylation and S-sulfhydratmentioning

confidence: 99%

From Nitric Oxide Toward S-Nitrosylation: Expanding Roles in Gametes and Embryos

Ješeta¹,

Sedmı́ková²,

Bodart³

2017

Nitric Oxide Synthase - Simple Enzyme-Complex Roles

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Nitric oxide (NO) is a gasotransmitter involved in various aspects of reproduction. The observational data from different species, such as sea urchin, ascidians, amphibians, rodents, porcine, bovine, and human, suggest that NO might have a significant role in reproduction through several mechanisms. This proposed role might appear preserved through evolution; however, the effects of NO also depend on the species or stages considered. There has been debate over the physiological relevance of NO, though the benefits of its use in assisted reproduction are now widely recognized. Over the past years, S-nitrosylation has provided a new angle to decipher the mechanisms through which NO exerts its actions. This chapter summarizes, in a nonexhaustive manner, research that explores the role of NO in gametes and embryos.

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Endogenous S-sulfhydration of PTEN helps protect against modification by nitric oxide

Cited by 45 publications

References 16 publications

H 2 S: A Novel Gasotransmitter that Signals by Sulfhydration

H 2 S: A Novel Gasotransmitter that Signals by Sulfhydration

The role of hydrogen sulfide in aging and age-related pathologies

From Nitric Oxide Toward S-Nitrosylation: Expanding Roles in Gametes and Embryos

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