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Role of peroxiredoxin‐1 in regulation of PKG dimerization associated with relaxation to hydrogen peroxide in bovine pulmonary arteries
Author(s) -
Patel Dhara,
Kelly Melissa,
Kandhi Sharath,
Wolin Michael S
Publication year - 2013
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.27.1_supplement.920.8
Subject(s) - peroxiredoxin , hydrogen peroxide , phosphorylation , chemistry , peroxide , oxidative phosphorylation , biochemistry , microbiology and biotechnology , biophysics , biology , enzyme , organic chemistry , peroxidase
Previous studies from our laboratory have suggested that thiol oxidation‐elicited dimerization‐activation of the 1α form of protein kinase G (PKG1α) contributes to the relaxation of isolated endothelium removed bovine pulmonary arteries (BPA) to peroxide and responses to hypoxia. We depleted peroxiredoxin‐1 by using siRNA to determine if peroxide metabolism by peroxiredoxin‐1 plays a role in the dimerization‐activation (based on increased VASP phosphorylation) of PKG1α. Hypoxic conditions were used to minimize basal PKG dimerization. Depletion of peroxiredoxin‐1 was observed to attenuate PKG dimerization‐activation (based on decreased VASP phosphorylation). However, peroxiredoxin‐1 depletion did not inhibit PKG dimerization‐activation elicited by inhibiting glucose‐6‐phosphate dehydrogenase (G6PD) with 6‐aminonicotinamide (6‐ AN). 6‐AN promotes NADPH oxidation and a dimerization‐activation of PKG via a mechanism potentially independent of peroxide. Thus, peroxiredoxin‐1 appears to participate in the PKG‐dimerization mediated relaxation to peroxide, but, it does not seem to participate in controlling the NADPH oxidation‐ and PKG‐dimerization associated relaxation to 6‐AN.