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Redox regulation of cGMP-dependent protein kinase Iα in the cardiovascular system.

Prysyazhna O, Eaton P - Front Pharmacol (2015)

Bottom Line: This regulatory role for oxidants is achieved in part by them inducing oxidative post-translational modifications of proteins which may alter their function or interactions.Such mechanisms allow changes in cell oxidant levels to be coupled to regulated alterations in enzymatic function (i.e., signal transduction), which enables "redox signaling." In this review we focus on the role of cGMP-dependent protein kinase (PKG) Ia disulfide dimerisation, an oxidative modification that is induced by oxidants that directly activates the enzyme, discussing how this impacts on the cardiovascular system.Additionally, how this oxidative activation of PKG may coordinate with or differ from classical activation of this kinase by cGMP is also considered.

View Article: PubMed Central - PubMed

Affiliation: Cardiovascular Division, King's College London, The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital , London, UK.

ABSTRACT
Elevated levels of oxidants in biological systems have been historically referred to as "oxidative stress," a choice of words that perhaps conveys an imbalanced view of reactive oxygen species in cells and tissues. The term stress suggests a harmful role, whereas a contemporary view is that oxidants are also crucial for the maintenance of homeostasis or adaptive signaling that can actually limit injury. This regulatory role for oxidants is achieved in part by them inducing oxidative post-translational modifications of proteins which may alter their function or interactions. Such mechanisms allow changes in cell oxidant levels to be coupled to regulated alterations in enzymatic function (i.e., signal transduction), which enables "redox signaling." In this review we focus on the role of cGMP-dependent protein kinase (PKG) Ia disulfide dimerisation, an oxidative modification that is induced by oxidants that directly activates the enzyme, discussing how this impacts on the cardiovascular system. Additionally, how this oxidative activation of PKG may coordinate with or differ from classical activation of this kinase by cGMP is also considered.

No MeSH data available.


Related in: MedlinePlus

PKG Iα contains three functional domains—an N-terminal leucine zipper, a regulatory and a catalytic. There are three pairs of cysteines, which may form disulfide bridges: C117-C195, C312-C518, and C42-C42.
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Figure 1: PKG Iα contains three functional domains—an N-terminal leucine zipper, a regulatory and a catalytic. There are three pairs of cysteines, which may form disulfide bridges: C117-C195, C312-C518, and C42-C42.

Mentions: PKG is a member of the serine/threonine kinase family. Mammals have two PKG genes, prkg1 and prkg2, that encode PKG type I and type II, respectively. PKG I and PKG II are homodimers of two identical subunits (≈75 or ≈85 kDa, respectively) and have similar domain architecture. PKG contains three functional domains (Francis et al., 2010; Figure 1).


Redox regulation of cGMP-dependent protein kinase Iα in the cardiovascular system.

Prysyazhna O, Eaton P - Front Pharmacol (2015)

PKG Iα contains three functional domains—an N-terminal leucine zipper, a regulatory and a catalytic. There are three pairs of cysteines, which may form disulfide bridges: C117-C195, C312-C518, and C42-C42.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4505079&req=5

Figure 1: PKG Iα contains three functional domains—an N-terminal leucine zipper, a regulatory and a catalytic. There are three pairs of cysteines, which may form disulfide bridges: C117-C195, C312-C518, and C42-C42.
Mentions: PKG is a member of the serine/threonine kinase family. Mammals have two PKG genes, prkg1 and prkg2, that encode PKG type I and type II, respectively. PKG I and PKG II are homodimers of two identical subunits (≈75 or ≈85 kDa, respectively) and have similar domain architecture. PKG contains three functional domains (Francis et al., 2010; Figure 1).

Bottom Line: This regulatory role for oxidants is achieved in part by them inducing oxidative post-translational modifications of proteins which may alter their function or interactions.Such mechanisms allow changes in cell oxidant levels to be coupled to regulated alterations in enzymatic function (i.e., signal transduction), which enables "redox signaling." In this review we focus on the role of cGMP-dependent protein kinase (PKG) Ia disulfide dimerisation, an oxidative modification that is induced by oxidants that directly activates the enzyme, discussing how this impacts on the cardiovascular system.Additionally, how this oxidative activation of PKG may coordinate with or differ from classical activation of this kinase by cGMP is also considered.

View Article: PubMed Central - PubMed

Affiliation: Cardiovascular Division, King's College London, The British Heart Foundation Centre of Excellence, The Rayne Institute, St Thomas' Hospital , London, UK.

ABSTRACT
Elevated levels of oxidants in biological systems have been historically referred to as "oxidative stress," a choice of words that perhaps conveys an imbalanced view of reactive oxygen species in cells and tissues. The term stress suggests a harmful role, whereas a contemporary view is that oxidants are also crucial for the maintenance of homeostasis or adaptive signaling that can actually limit injury. This regulatory role for oxidants is achieved in part by them inducing oxidative post-translational modifications of proteins which may alter their function or interactions. Such mechanisms allow changes in cell oxidant levels to be coupled to regulated alterations in enzymatic function (i.e., signal transduction), which enables "redox signaling." In this review we focus on the role of cGMP-dependent protein kinase (PKG) Ia disulfide dimerisation, an oxidative modification that is induced by oxidants that directly activates the enzyme, discussing how this impacts on the cardiovascular system. Additionally, how this oxidative activation of PKG may coordinate with or differ from classical activation of this kinase by cGMP is also considered.

No MeSH data available.


Related in: MedlinePlus