Studies on the Reaction of Nitric Oxide with the Hypoxia-Inducible Factor Prolyl Hydroxylase Domain 2 (EGLN1)

Chowdhury, Rasheduzzaman; Flashman, Emily; Mecinović, Jasmin; Kramer, Holger; Kessler, Benedikt M.; Frapart, Yves; Boucher, Jean‐Luc; Clifton, I.J.; McDonough, Michael A.; Schofield, Christopher J.

doi:10.1016/j.jmb.2011.04.075

Cited by 58 publications

(38 citation statements)

References 68 publications

(73 reference statements)

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“…Therefore, while both hypoxia and anemia are associated with reduced O 2 delivery, the relative sparing of SaO 2 during anemia fails to trigger classical O 2 -dependent HIF-1α signaling (5). Rather, HIF-1α activation during anemia occurs because S-nitrosylation -generating SNOpVHL, SNO-PHD2, and SNO-HIF-1α -serves to activate HIF-1α under normoxic conditions (106)(107)(108)(109). In addition, GSNOR abundance has been found to decrease in rodent models of acute anemia, which could further augment SNO bioactivity and hypoxic adaptation (110).…”

Section: Figurementioning

confidence: 99%

S-nitrosylation: integrator of cardiovascular performance and oxygen delivery

Haldar

Stamler²

2013

J. Clin. Invest.

106

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Delivery of oxygen to tissues is the primary function of the cardiovascular system. NO, a gasotransmitter that signals predominantly through protein S-nitrosylation to form S-nitrosothiols (SNOs) in target proteins, operates coordinately with oxygen in mammalian cellular systems. From this perspective, SNO-based signaling may have evolved as a major transducer of the cellular oxygen-sensing machinery that underlies global cardiovascular function. Here we review mechanisms that regulate S-nitrosylation in the context of its essential role in "systems-level" control of oxygen sensing, delivery, and utilization in the cardiovascular system, and we highlight examples of aberrant S-nitrosylation that may lead to altered oxygen homeostasis in cardiovascular diseases. Thus, through a bird's-eye view of S-nitrosylation in the cardiovascular system, we provide a conceptual framework that may be broadly applicable to the functioning of other cellular systems and physiological processes and that illuminates new therapeutic promise in cardiovascular medicine.

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Section: Figurementioning

confidence: 99%

S-nitrosylation: integrator of cardiovascular performance and oxygen delivery

Haldar

Stamler²

2013

J. Clin. Invest.

106

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“…Its activity is inhibited by Co 2ϩ and Ni 2ϩ by replacing the iron at the catalytic site (28). ⅐ NO and iron chelators have also been shown to inhibit prolyl hydroxylase activity by either binding to or removing this catalytic iron (29). Previously, it has been shown that the JMJC domain-containing histone demethylase KDM3A is highly sensitive to inhibition by carcinogenic nickel ions (28,30,31).…”

mentioning

confidence: 99%

Nitric Oxide Modifies Global Histone Methylation by Inhibiting Jumonji C Domain-containing Demethylases

Hickok

Vasudevan

Antholine

et al. 2013

Journal of Biological Chemistry

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Background:The methylation status of histone tails is a balance between methylation and demethylation. Results: Nitric oxide inhibits lysine demethylase 3A and alters cellular histone methylation patterns. Conclusion: Nitric oxide can significantly modify the epigenetic landscape. Significance: These results establish nitric oxide as a physiological epigenetic regulator acting through a nonclassical cell signaling mechanism.

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“…Alternatively, oxidants like H 2 O 2 or other metals may influence PHD activity via effects on the ascorbate pool, thus, indirectly affect-ing the redox state of iron (9). Finally, PHDs have been proposed to be regulated by other gasses such as NO (10).…”

mentioning

confidence: 99%

The Skp1 Protein from Toxoplasma Is Modified by a Cytoplasmic Prolyl 4-Hydroxylase Associated with Oxygen Sensing in the Social Amoeba Dictyostelium

Brown

Wang

et al. 2012

Journal of Biological Chemistry

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Background: A cytoplasmic prolyl 4-hydroxylase of Dictyostelium contributes to O 2 sensing by modifying Skp1. Results: The corresponding protein of Toxoplasma exhibits related functions but has high affinity for O 2 . Conclusion: Hydroxylation of Skp1 is conserved in protists but may sense O 2 indirectly. Significance: The putative evolutionary precursor of animal prolyl 4-hydroxylases that modify HIF␣ potentially remodeled the proteome via degradation rather than transcriptionally.

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Studies on the Reaction of Nitric Oxide with the Hypoxia-Inducible Factor Prolyl Hydroxylase Domain 2 (EGLN1)

Cited by 58 publications

References 68 publications

S-nitrosylation: integrator of cardiovascular performance and oxygen delivery

S-nitrosylation: integrator of cardiovascular performance and oxygen delivery

Nitric Oxide Modifies Global Histone Methylation by Inhibiting Jumonji C Domain-containing Demethylases

The Skp1 Protein from Toxoplasma Is Modified by a Cytoplasmic Prolyl 4-Hydroxylase Associated with Oxygen Sensing in the Social Amoeba Dictyostelium

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