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Investigation of the Mechanism of Hydrogen Sulfide Activation of Protein Kinase C
Author(s) -
Buck Lauren,
Stahelin Robert V
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.690.1
Subject(s) - diacylglycerol kinase , protein kinase c , microbiology and biotechnology , activator (genetics) , signal transduction , second messenger system , chemistry , biochemistry , kinase , protein kinase a , mitochondrion , biology , gene
Hydrogen Sulfide (H 2 S) has been shown to be an endogenously produced second messenger, affecting a variety of physiological and cell signaling processes. It is present at micromolar levels within the body and is produced via two key enzymes in the cysteine biosynthesis pathway: cystathione‐β synthase, and cystathione‐γ lyase. Despite its prior reputation as a noxious gas, H 2 S has been shown to have significant involvement in protection of cardiac tissue following myocardial infarction. These protective properties may be due to a role of H 2 S in control of mitochondrial oxidation, in addition to its ties to the localization and signaling of Protein Kinase C. Recent studies have indicated an involvement of H 2 S in the localization of certain isoforms of Protein Kinase C to the cellular membrane (epsilon and eta). In particular, PKC‐ε knockout has been found to be deleterious to cardiac recovery and also has probable involvement in the process of mitochondrial respiration. We are investigating the molecular basis of H 2 S induced translocation of PKC isoforms to the cellular membrane. One possibility of H 2 S involvement in PKC‐ε localization is through a diacylglycerol (DAG) synthesis response. DAG is known to be the main activator of PKC, and it is possible that H 2 S serves as a signaling molecule to initiate DAG synthesis. The molecular basis of PKC recruitment to cellular membranes by H 2 S signaling will be presented.