Pressure-overload-induced subcellular relocalization/oxidation of soluble guanylyl cyclase in the heart modulates enzyme stimulation.

Abstract

Pressure overload depresses NO/heme-dependent sGC activation in the heart, consistent with enhanced oxidation.

The data reveal a novel additional mechanism for reduced NO-coupled sGC activity related to dynamic shifts in membrane microdomain localization, with Cav3-microdomains protecting sGC from heme-oxidation and facilitating NO responsiveness.

Translocation of sGC out of this domain favors sGC oxidation and contributes to depressed NO-stimulated sGC activity.

Full Text

• DOI - Circulation research (DOI)
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• Lippincott Williams & Wilkins - full-text online
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Subjects

• Animals
• Benzoic Acids
• Cardiomegaly
• Caveolin 3
• Cyclic GMP
• Disease Models, Animal
• Down-Regulation
• Enzyme Activation
• Enzyme Activators
• Guanylate Cyclase
• Heme
• Hydrocarbons, Fluorinated
• Hydrolysis
• Membrane Microdomains
• Mice
• Mice, Inbred C57BL
• Mice, Knockout
• Myocytes, Cardiac
• Nitric Oxide
• Oxidation-Reduction
• Protein Transport
• Receptors, Cytoplasmic and Nuclear
• Signal Transduction

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Authors

• Emily J Tsai
• Yuchuan Liu
• Norimichi Koitabashi
• Djahida Bedja
• Thomas Danner
• Jean-Francois Jasmin
• Michael P Lisanti
• Andreas Friebe
• Eiki Takimoto
• David A Kass

Publication date

2012-01-23

Journal

Journal topics

• Cardiovascular System

Language

Eng.

Copyright

Circulation research

Division of Cardiology, Johns Hopkins Medical Institutions, 720 Rutland Ave, Ross 858, Baltimore, MD 21205, USA. emily.tsai [at] tuhs.temple.edu

Release reference

Circ Res. 2012 Jan;110(2):295-303

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