Hemoglobin. A biologic fenton reagent.

Sadrzadeh, S.M. Hossein; Graf, Ernst; Panter, S. Scott; Hallaway, Philip E.; Eaton, John W.

doi:10.1016/s0021-9258(17)42604-4

Cited by 529 publications

(77 citation statements)

References 13 publications

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“…The Fenton catalytic performance of the RBC@Hb@GOx NPs was evaluated [ 45 , 46 ]. The RBC@Hb@GOx NPs were incubated with glucose solution (10 mM) to start cascade Fenton-type reactions (Figs.…”

Section: Resultsmentioning

confidence: 99%

Self-Assembly Protein Superstructures as a Powerful Chemodynamic Therapy Nanoagent for Glioblastoma Treatment

et al. 2020

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Glioblastoma (GBM) remains a formidable challenge in oncology. Chemodynamic therapy (CDT) that triggers tumor cell death by reactive oxygen species (ROS) could open up a new door for GBM treatment. Herein, we report a novel CDT nanoagent. Hemoglobin (Hb) and glucose oxidase (GOx) were employed as powerful CDT catalysts. Instead of encapsulating the proteins in drug delivery nanocarriers, we formulate multimeric superstructures as self-delivery entities by crosslinking techniques. Red blood cell (RBC) membranes are camouflaged on the protein superstructures to promote the delivery across blood–brain barrier. The as-prepared RBC@Hb@GOx nanoparticles (NPs) offer superior biocompatibility, simplified structure, and high accumulation at the tumor site. We successfully demonstrated that the NPs could efficiently produce toxic ROS to kill U87MG cancer cells in vitro and inhibit the growth of GBM tumor in vivo, suggesting that the new CDT nanoagent holds great promise for treating GBM.

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Section: Resultsmentioning

confidence: 99%

Self-Assembly Protein Superstructures as a Powerful Chemodynamic Therapy Nanoagent for Glioblastoma Treatment

et al. 2020

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“…During this three-step process bilirubin is formed, and ferrous iron is directed to safe storage in ferritin, preventing the generation of reactive oxygen species via the Fenton reaction. 82 Each of the degradation products of heme / HO-1 (bilirubin, CO and Fe-ferritin) are well-known to display antioxidant and antiapoptotic properties. 83,84 Figure 5.…”

Section: Heme Oxygenase-1 (Ho-1)mentioning

confidence: 99%

Enzyme-activated probes in optical imaging: a focus on atherosclerosis

et al. 2021

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“…Sci. 2021, 22, 6668 2 of 20 only in pathological states but also in physiological conditions [1][2][3][4]. Importantly, Hb undergoing a natural auto-oxidation in red blood cells (RBCs) generates reactive oxygen species (ROS) and hydrogen peroxide (H 2 O 2 ) [5][6][7].…”

Section: Introductionmentioning

confidence: 99%

“…The ferrous form of the heme group has been described to react with nitric-oxide, reducing its vasodilator effect and leading to vasoconstriction, hypertension and MetHb formation [21]. Hb also facilitates hydroxyl-radical generation from activated oxygen species via the Fenton reaction [22]. Furthermore, Hb reacts with plaque lipids in the atheroma, leading to Hb oxidation and formation of MetHb and FerrylHb species [10].…”

Section: Introductionmentioning

confidence: 99%

Ferryl Hemoglobin and Heme Induce A1-Microglobulin in Hemorrhaged Atherosclerotic Lesions with Inhibitory Function against Hemoglobin and Lipid Oxidation

Pethő

Gáll

Hendrik

et al. 2021

IJMS

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Infiltration of red blood cells into atheromatous plaques and oxidation of hemoglobin (Hb) and lipoproteins are implicated in the pathogenesis of atherosclerosis. α1-microglobulin (A1M) is a radical-scavenging and heme-binding protein. In this work, we examined the origin and role of A1M in human atherosclerotic lesions. Using immunohistochemistry, we observed a significant A1M immunoreactivity in atheromas and hemorrhaged plaques of carotid arteries in smooth muscle cells (SMCs) and macrophages. The most prominent expression was detected in macrophages of organized hemorrhage. To reveal a possible inducer of A1M expression in ruptured lesions, we exposed aortic endothelial cells (ECs), SMCs and macrophages to heme, Oxy- and FerrylHb. Both heme and FerrylHb, but not OxyHb, upregulated A1M mRNA expression in all cell types. Importantly, only FerrylHb induced A1M protein secretion in aortic ECs, SMCs and macrophages. To assess the possible function of A1M in ruptured lesions, we analyzed Hb oxidation and heme-catalyzed lipid peroxidation in the presence of A1M. We showed that recombinant A1M markedly inhibited Hb oxidation and heme-driven oxidative modification of low-density lipoproteins as well plaque lipids derived from atheromas. These results demonstrate the presence of A1M in atherosclerotic plaques and suggest its induction by heme and FerrylHb in the resident cells.

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Hemoglobin. A biologic fenton reagent.

Cited by 529 publications

References 13 publications

Self-Assembly Protein Superstructures as a Powerful Chemodynamic Therapy Nanoagent for Glioblastoma Treatment

Self-Assembly Protein Superstructures as a Powerful Chemodynamic Therapy Nanoagent for Glioblastoma Treatment

Enzyme-activated probes in optical imaging: a focus on atherosclerosis

Ferryl Hemoglobin and Heme Induce A1-Microglobulin in Hemorrhaged Atherosclerotic Lesions with Inhibitory Function against Hemoglobin and Lipid Oxidation

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