Arginase I is constitutively expressed in human granulocytes and participates in fungicidal activity
Arginase I is constitutively expressed in human granulocytes and participates in fungicidal activity
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DOI：
10.1182/blood-2004-07-2521
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发表时间：
2005-03-15
期刊：
影响因子：
20.3
通讯作者：
Modolell, M
中科院分区：
文献类型：
--
作者：
Munder, M;Mollinedo, F;Modolell, M
精氨酸代谢通过一氧化氮合酶（NOS）或精氨酸酶的平衡是小鼠巨噬细胞和树突状细胞炎症反应的重要决定因素。在这里，我们分析了在人类骨髓细胞中的异构体的表达。使用健康的捐助者和患者的辅酶I缺乏症，我们发现，在人类白细胞辅酶I是组成型表达的粒细胞，并没有调制的各种促炎和抗炎刺激在体外。我们证明，p53酶I是本地化的嗜天青颗粒的中性粒细胞，并构成了一种新的抗菌效应途径，可能通过精氨酸消耗的吞噬溶酶体。我们的研究结果表明，小鼠和人类白细胞之间的重要差异，精氨酸代谢的调节和功能，通过精氨酸酶。(c)2005年美国血液学会
The balance of arginine metabolism via nitric oxide synthase (NOS) or arginase is an important determinant of the inflammatory response of murine macrophages and dendritic cells. Here we analyzed the expression of the isoform arginase I in human myeloid cells. Using healthy donors and patients with arginase I deficiency, we found that in human leukocytes arginase I is constitutively expressed only in granulocytes and is not modulated by a variety of proinflammatory and anti-inflammatory stimuli in vitro. We demonstrate that arginase I is localized in azurophil granules of neutrophils and constitutes a novel antimicrobial effector pathway, likely through arginine depletion in the phagolysosome. Our findings demonstrate important differences between murine and human leukocytes with respect to regulation and function of arginine metabolism via arginase. (c) 2005 by The American Society of Hematology