Abstract:
:Heme and iron are essential to almost all forms of life. The strict maintenance of heme and iron homeostasis is essential to prevent cellular toxicity and the existence of systemic and intracellular regulation is fundamental. Cytosolic heme can be catabolized and detoxified by heme oxygenases (HOs). Interestingly, free heme detoxification through HOs results in the production of free ferrous iron, which can be potentially hazardous for cells. Recently, the intracellular iron chaperone, poly (rC)-binding protein 2 (PCBP2), has been identified, which can be involved in accepting iron after heme catabolism as well as intracellular iron transport. In fact, HO1, NADPH-cytochrome P450 reductase, and PCBP2 form a functional unit that integrates the catabolism of heme with the binding and transport of iron by PCBP2. In this review, we provide an overview of our understanding of the iron chaperones and discuss the mechanism how iron chaperones bind iron released during the process of heme degradation.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Yanatori I,Richardson DR,Toyokuni S,Kishi Fdoi
10.1016/j.abb.2019.108071subject
Has Abstractpub_date
2019-09-15 00:00:00pages
108071eissn
0003-9861issn
1096-0384pii
S0003-9861(19)30282-6journal_volume
672pub_type
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pub_type: 杂志文章
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pub_type: 杂志文章,评审
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pub_type: 杂志文章,评审
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更新日期:2005-12-15 00:00:00
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