[논문]Globin X is a six-coordinate globin that reduces nitrite to nitric oxide in fish red blood cells

Corti, Paola; Xue, Jianmin; Tejero, Jesú; s; Wajih, Nadeem; Sun, Ming; Stolz, Donna B.; Tsang, Michael; Kim-Shapiro, Daniel B.; Gladwin, Mark T.

doi:10.1073/pnas.1522670113

Globin X is a six-coordinate globin that reduces nitrite to nitric oxide in fish red blood cells 원문보기

Proceedings of the National Academy of Sciences of the United States of America, v.113 no.30, 2016년, pp.8538 - 8543

Corti, Paola (Pittsburgh Heart, Lung, Blood, and Vascular Medicine Institute, University of Pittsburgh, Pittsburgh, PA 15213) , Xue, Jianmin , Tejero, Jesús (Pittsburgh Heart, Lung, Blood, and Vascular Medicine Institute, University of Pittsburgh, Pittsburgh, PA 15213) , Wajih, Nadeem , Sun, Ming (Pittsburgh Heart, Lung, Blood, and Vascular Medicine Institute, University of Pittsburgh, Pittsburgh, PA 15213) , Stolz, Donna B. , Tsang, Michael (Department of Physics and the Translational Science Center, Wake Forest University, Winston-Salem, NC 27109) , Kim-Shapiro, Daniel B. , Gladwin, Mark T. (Department of Cell Biology, University of Pittsburgh, Pittsburgh, PA 15213)

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SignificanceHemoglobin is generally assumed to be the only globin in vertebrate RBCs. In addition to its foremost role as an oxygen carrier, mammalian hemoglobin can also operate as a nitrite reductase, producing the signaling molecule nitric oxide (NO) from nitrite. Over the last 15 yr, several novel globins have been identified with six-coordinate heme geometry and uncertain physiological functions. Here we report that a six-coordinate globin of ancient origin, named Globin X, is present in fish RBCs. We establish that Globin X is a fast nitrite reductase, and this activity can regulate NO production from fish RBCs and modulate platelet activation. Thus we provide evidence that the ancestral globins in blood were efficient nitrite reductases.The discovery of novel globins in diverse organisms has stimulated intense interest in their evolved function, beyond oxygen binding. Globin X (GbX) is a protein found in fish, amphibians, and reptiles that diverged from a common ancestor of mammalian hemoglobins and myoglobins. Like mammalian neuroglobin, GbX was first designated as a neuronal globin in fish and exhibits six-coordinate heme geometry, suggesting a role in intracellular electron transfer reactions rather than oxygen binding. Here, we report that GbX to our knowledge is the first six-coordinate globin and the first globin protein apart from hemoglobin, found in vertebrate RBCs. GbX is present in fish erythrocytes and exhibits a nitrite reduction rate up to 200-fold faster than human hemoglobin and up to 50-fold higher than neuroglobin or cytoglobin. Deoxygenated GbX reduces nitrite to form nitric oxide (NO) and potently inhibits platelet activation in vitro, to a greater extent than hemoglobin. Fish RBCs also reduce nitrite to NO and inhibit platelet activation to a greater extent than human RBCs, whereas GbX knockdown inhibits this nitrite-dependent NO signaling. The description of a novel, six-coordinate globin in RBCs with dominant electron transfer and nitrite reduction functionality provides new insights into the evolved signaling properties of ancestral heme-globins.

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Globin X is a six-coordinate globin that reduces nitrite to nitric oxide in fish red blood cells 원문보기

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