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血红素加氧酶-1回到内质网。

Heme oxygenase-1 comes back to endoplasmic reticulum.

机构信息

School of Biological Sciences, Ulsan University, Republic of Korea.

出版信息

Biochem Biophys Res Commun. 2011 Jan 7;404(1):1-5. doi: 10.1016/j.bbrc.2010.11.067. Epub 2010 Nov 19.

DOI:10.1016/j.bbrc.2010.11.067
PMID:21094129
Abstract

Originally identified as a rate-limiting enzyme for heme catabolism, heme oxygenase-1 (HO-1) has expanded its roles in anti-inflammation, anti-apoptosis and anti-proliferation for the last decade. Regulation of protein activity by location is well appreciated. Even though multiple compartmentalization of HO-1 has been documented, the functional implication of this enzyme at these subcellular organelles is only partially elucidated. In this review we discuss the endoplasmic reticulum (ER)-residing HO-1 and its cytoprotective activity against ER stress.

摘要

最初被鉴定为血红素分解代谢的限速酶,血红素加氧酶-1(HO-1)在过去十年中扩大了其在抗炎、抗细胞凋亡和抗增殖方面的作用。位置对蛋白质活性的调节已得到充分认识。尽管已经记录了 HO-1 的多种区室化,但该酶在这些亚细胞细胞器中的功能意义仅部分阐明。在这篇综述中,我们讨论了内质网(ER)驻留的 HO-1 及其对 ER 应激的细胞保护活性。

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