Journal
BIOCHEMICAL PHARMACOLOGY
Volume 86, Issue 9, Pages 1311-1319Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bcp.2013.08.064
Keywords
cAMP; Isolated mitochondria; Phosphodiesterase
Categories
Funding
- Shriners Burns Hospitals
- American Diabetes Association [7-12-BS-184]
- University of Texas
- American Heart Association
- EU (ESF)
- Greek national funds through the Operational Program Education and Lifelong Learning of the National Strategic Reference Framework-Research Funding Program: Aristeia [1436]
- EU [CT-2011-285950-SEE-DRUG]
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Although hydrogen sulfide (H2S) is generally known as a mitochondrial poison, recent studies show that lower concentrations of H2S play a physiological role in the stimulation of mitochondrial electron transport and cellular bioenergetics. This effect involves electron donation at Complex II. Other lines of recent studies demonstrated that one of the biological actions of H2S involves inhibition of CAMP and cGMP phosphodiesterases (PDEs). Given the emerging functional role of the mitochondrial isoform of CAMP PDE (PDE2A) in the regulation of mitochondrial function the current study investigated whether CAMP-dependent mechanisms participate in the stimulatory effect of NaHS on mitochondrial function. In isolated rat liver mitochondria, partial digestion studies localized PDE2A into the mitochondrial matrix. NaHS exerted a concentration-dependent inhibitory effect on recombinant PDE2A enzyme in vitro. Moreover, NaHS induced an elevation of CAMP levels when added to isolated mitochondria and stimulated the mitochondrial electron transport. The latter effect was inhibited by Rp-cAMP, an inhibitor of the cAMP-dependent protein kinase (PKA). The current findings suggest that the direct electron donating effect of NaHS is amplified by an intramitochondrial CAMP system, which may involve the inhibition of PDE2A and subsequent, cAMP-mediated stimulation of PICA. (C) 2013 Elsevier Inc. All rights reserved.
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