While the signaling roles of NO have been studied extensively over the past three decades, researchers have yet to understand how this short-lived molecule travels from blood to signaling targets in the blood vessel wall.
To conduct their studies, the research team decided to investigate heme, best known for its role in oxygen delivery in the blood, but also a common signaling target for NO. They mixed ferric heme with NO and the antioxidant glutathione to see how they would react in a laboratory setting. "My laboratory has worked for more than two decades trying to understand how NO can diffuse in blood and in cells without being destroyed by reactions with other radicals and heme bound proteins like hemoglobin and myoglobin," said study lead and corresponding author Mark T. Gladwin, MD, UMSOM Dean and Vice President for Medical Affairs, University of Maryland, Baltimore, and the John Z. and Akiko K. Bowers Distinguished Professor.
Dr. Gladwin and his longtime collaborator and co-senior author Dany Kim-Shapiro, Ph.D., Professor and Chair of the Department of Physics at WFU, have worked together for more than two decades to understand how NO is transported in red blood cells and regulates blood flow. Uncovering NO-ferroheme as a biological"middleman" represents an important step towards understanding the nuanced signaling mechanisms of NO both under healthy conditions and in myriad disease states.
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