期刊
ANTIOXIDANTS & REDOX SIGNALING
卷 12, 期 2, 页码 233-248出版社
MARY ANN LIEBERT, INC
DOI: 10.1089/ars.2009.2822
关键词
-
资金
- National Heart Lung and Blood Institute: NHLBI [R01 HL67367, P01HL055552]
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL067367, P01HL055552] Funding Source: NIH RePORTER
Heme is an essential molecule in aerobic organisms. Heme consists of protoporphyrin IX and a ferrous (Fe2+) iron atom, which has high affinity for oxygen (O-2). Hemoglobin, the major oxygen-carrying protein in blood, is the most abundant heme-protein in animals and humans. Hemoglobin consists of four globin subunits (alpha(2)beta(2)), with each subunit carrying a heme group. Ferrous (Fe2+) hemoglobin is easily oxidized in circulation to ferric (Fe3+) hemoglobin, which readily releases free hemin. Hemin is hydrophobic and intercalates into cell membranes. Hydrogen peroxide can split the heme ring and release free'' redox-active iron, which catalytically amplifies the production of reactive oxygen species. These oxidants can oxidize lipids, proteins, and DNA; activate cell-signaling pathways and oxidant-sensitive, proinflammatory transcription factors; alter protein expression; perturb membrane channels; and induce apoptosis and cell death. Heme-derived oxidants induce recruitment of leukocytes, platelets, and red blood cells to the vessel wall; oxidize low-density lipoproteins; and consume nitric oxide. Heme metabolism, extracellular and intracellular defenses against heme, and cellular cytoprotective adaptations are emphasized. Sickle cell disease, an archetypal example of hemolysis, heme-induced oxidative stress, and cytoprotective adaptation, is reviewed. Antioxid. Redox Signal. 12, 233-248.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据