期刊
CLINICA CHIMICA ACTA
卷 412, 期 7-8, 页码 493-498出版社
ELSEVIER
DOI: 10.1016/j.cca.2010.12.011
关键词
Hemoglobin; Haptoglobin; Redox reactions
When released from red blood cells (RBCs), hemoglobin (Hb) is extremely toxic due in large part to the redox activity of its heme center. Mature however, has provided a multitude of protective mechanisms that can detoxify free Hb effectively under physiological conditions. Chief amongst them is haptoglobin (Hp) which chaperones Hb subunits to the macrophages for safe degradation. Recent research on the interactions between Hb and Hp under oxidative conditions revealed that Hp specifically shields key amino acids on the Hb molecule, allowing the heme to consume oxidants and short-circuits the emerging and damaging radicals. Moreover, animal studies showed that the infusion of Hb complexed with Hp prevents Hb-induced systemic hypertension and tissue injury. It may prove necessary to explore these protective clearing mechanisms to counter the toxicity associated with free Hb when used as oxygen therapeutics in hemolytic anemias and in RBC storage lesions. Published by Elsevier B.V.
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