1 results match your criteria: "University of Texas Houston Medical School (E.M.). astraub@pitt.edu.[Affiliation]"
Cytochrome b5 Reductase 3 Modulates Soluble Guanylate Cyclase Redox State and cGMP Signaling.
Circ Res
July 2017
From the Heart, Lung, Blood and Vascular Medicine Institute (M.M.R., A.T.N., M.P.M., S.A.H., C.S.-W., N.T.C., N.C.-M., K.C.W., M.T.G., A.C.S.), Division of Pulmonary, Allergy and Critical Care Medicine (C.S.-W., M.T.G.), Department of Pharmacology and Chemical Biology (S.J., C.J.B., F.J.S., A.C.S.), and Division of Renal-Electrolyte (C.J.B.), University of Pittsburgh, PA; Department of Physiology and Pharmacology, West Virginia University School of Medicine, Morgantown (E.E.K.); and Department of Internal Medicine, Division of Cardiology, University of Texas Houston Medical School (E.M.).
Rationale: Soluble guanylate cyclase (sGC) heme iron, in its oxidized state (Fe), is desensitized to NO and limits cGMP production needed for downstream activation of protein kinase G-dependent signaling and blood vessel dilation.
Objective: Although reactive oxygen species are known to oxidize the sGC heme iron, the basic mechanism(s) governing sGC heme iron recycling to its NO-sensitive, reduced state remain poorly understood.
Methods And Results: Oxidant challenge studies show that vascular smooth muscle cells have an intrinsic ability to reduce oxidized sGC heme iron and form protein-protein complexes between cytochrome b5 reductase 3, also known as methemoglobin reductase, and oxidized sGC.