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Investigation of the Mechanism of Hydrogen Sulfide Activation of Protein Kinase C
Author(s) -
Stahelin Robert V,
Gunasekaran Christopher
Publication year - 2011
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.25.1_supplement.939.9
Subject(s) - protein kinase c , microbiology and biotechnology , signal transduction , protein kinase a , mitochondrion , hydrogen sulfide , chemistry , kinase , biochemistry , enzyme , gene isoform , biology , gene , sulfur , organic chemistry
Hydrogen Sulfide (H2S) 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, H2S 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 H2S 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 H2S in the localization of certain isoforms of Protein Kinase C to the cellular membrane (epsilon and eta). In particular, PKC epsilon 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 H2S induced translocation of PKC isoforms to the cellular membrane. The molecular basis of PKC recruitment to cellular membranes by H2S signaling will be presented.