In this study, we identify FDX1 as a mammalian CcO assembly factor. Our findings showing reduced oxygen consumption, decreased abundance of CcO, reduced levels of heme a/a 3, and COX15-based partial rescue of COX1 in FDX1 null cells support the role of FDX1 in CcO biogenesis via heme a/a 3 biosynthesis (Figs. 1, 2, and 5). Our results are in ...

上游是通过crispr-cas9 功能缺失筛选找到了上游调节因子fdx1及lias，证明了铜死亡跟fdx1和蛋白脂酰化有关系。 然后提出了铜离子能结合脂酰化蛋白形成寡聚体，进而影响TCA循环。

在大鼠心肌细胞系中使用基于 CRISPR-Cas9 的功能丧失研究，我们证明了 FDX1 在线粒体呼吸和能量产生中的基本需求。我们将线粒体呼吸减少归因于细胞色素 c 氧化酶 （CcO） 丰度和组装的特异性降低，CcO 是一种线粒体血红素-铜氧化酶和线粒体呼吸链的末端酶。

2023年10月17日 · This finding links FDX1 function to heme a biosynthesis, and places it upstream of COX15 in CcO biogenesis like its ancestral yeast homolog. Taken together, our work has identified FDX1 as a critical CcO biogenesis factor in mammalian cells.

FDX1 Is Essential for ES-Mediated Rescue of Mitochondrial Respiration in Cu-Depleted Cells. Previous studies reported that ES treatment results in an increase in mitochondrial Cu content and that loss of FDX1 conferred resistance to ES-mediated killing (8, 11, 15). Taken together, these results suggest that FDX1 may

补充铜未能挽救 cco 生物发生，但血红素合酶 cox15 的过度表达部分挽救了 fdx1 敲除细胞中 cox1 的丰度。 这一发现将 FDX1 功能与血红素生物合成联系起来，并将其置于 CcO 生物合成中 COX15 的上游，就像其祖先酵母同源物一样。

Here, we demonstrate that copper is released from elesclomol within mitochondria via FDX1, and outside of mitochondria in an FDX1-independent manner to make copper available to mitochondrial and nonmitochondrial cuproenzymes, respectively.

Up-regulation of FDX1 promoted elesclomol-induced cuproptosis against glioblastoma both in vitro and in vivo. FDX1 knockdown can reverse the inhibitory effect of elesclomol on tumor cells. Conclusions: Elesclomol inhibits glioblastoma development via inducing cuproptosis, regulated by NFκB1/FDX1 axis.

4 天之前 · FDX1 expression is decreased in ccRCC and its reduced expression is associated with poor prognosis based on public databases. First, we collected the expression data of FDX1 in ccRCC and adjacent ...

人类线粒体含有两种同工型 [2Fe-2S] 铁氧还蛋白：FDX1（又名肾上腺氧还蛋白）和 FDX2，在细胞色素 P450 依赖性类固醇转化和 Fe-S 蛋白生物合成中具有已知功能。 在这里，我们表明只有 FDX2 而不是 FDX1 参与 Fe-S 蛋白的成熟。 反之亦然，FDX1 不仅对类固醇生成具有特异性，而且对血红素 a 和硫辛酰辅因子生物合成也具有特异性。 在后一种途径中，FDX1 提供电子来启动硫辛酰合酶催化的自由基链式反应。 我们还确定硫辛酸化是有毒抗肿瘤铜离子载体艾司洛醇的 …