ArticleBiophysical journal1995
H2O2-treated actin: assembly and polymer interactions with cross-linking proteins.
Article in Biophysical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 96 citations in OpenAlex.
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- Oxidative stress induced by DMSA-IONPs impairs breast cancer cell migration and paracrine cell communication.Journal of nanobiotechnology · 2026Article
- Axonal mitochondria regulate gentle touch response through control of axonal actin dynamics.bioRxiv : the preprint server for biology · 2024Article
- Gastrodin improves osteoblast function and adhesion to titanium surface in a high glucose environment.Biochemistry and biophysics reports · 2024Article
- The structure of the human LACTB filament reveals the mechanisms of assembly and membrane binding.PLoS biology · 2022Article
- Mechanism and Prospect of Gastrodin in Osteoporosis, Bone Regeneration, and Osseointegration.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Renoprotective Effect of Liraglutide Is Mediated via the Inhibition of TGF-Beta 1 in an LLC-PK1 Cell Model of Diabetic Nephropathy.Current issues in molecular biology · 2022Article
- Reactive Oxygen Species: Modulators of Phenotypic Switch of Vascular Smooth Muscle Cells.International journal of molecular sciences · 2020Review
- Redox Regulation of the Actin Cytoskeleton in Cell Migration and Adhesion: On the Way to a Spatiotemporal View.Frontiers in cell and developmental biology · 2020Review
- Oxidative hotspots on actin promote skeletal muscle weakness in rheumatoid arthritis.JCI insight · 2019Article
- Endothelial Nanomechanics in the Context of Endothelial (Dys)function and Inflammation.Antioxidants & redox signaling · 2019Review
- NOX4 (NADPH Oxidase 4) and Poldip2 (Polymerase δ-Interacting Protein 2) Induce Filamentous Actin Oxidation and Promote Its Interaction With Vinculin During Integrin-Mediated Cell Adhesion.Arteriosclerosis, thrombosis, and vascular biology · 2018Article
- Oxidant production and SOD1 protein expression in single skeletal myofibers from Down syndrome mice.Redox biology · 2017Article
- Actin filaments-A target for redox regulation.Cytoskeleton (Hoboken, N.J.) · 2016Review
- The Neuro-Immune Pathophysiology of Central and Peripheral Fatigue in Systemic Immune-Inflammatory and Neuro-Immune Diseases.Molecular neurobiology · 2016Review
- Article
- Proteomic Identification of Oxidized Proteins in Entamoeba histolytica by Resin-Assisted Capture: Insights into the Role of Arginase in Resistance to Oxidative Stress.PLoS neglected tropical diseases · 2016Article
- The role of Nox-mediated oxidation in the regulation of cytoskeletal dynamics.Current pharmaceutical design · 2015Review
- The role of reactive oxygen species in microvascular remodeling.International journal of molecular sciences · 2014Review
- Acidic priming enhances metastatic potential of cancer cells.Pflugers Archiv : European journal of physiology · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During inflammation, hydrogen peroxide, produced by polymorphonuclear leukocytes, provokes cell death mainly by disarranging filamentous (polymerized) actin (F-actin). To show the molecular mechanism(s) by which hydrogen peroxide could alter actin dynamics, we analyzed the ability of H2O2-treated actin samples to polymerize as well as the suitability of actin polymers (from oxidized monomers) to interact with cross-linking proteins. H2O2-treated monomeric (globular) actin (G-actin) shows an altered time course of polymerization. The increase in the lag phase and the lowering in both the polymerization rate and the polymerization extent have been evidenced. Furthermore, steady-state actin polymers, from oxidized monomers, are more fragmented than control polymers. This seems to be ascribable to the enhanced fragility of oxidized filaments rather than to the increase in the nucleation activity, which markedly falls. These facts; along with the unsuitability of actin polymers from oxidized monomers to interact with both filamin and alpha-actinin, suggest that hydrogen peroxide influences actin dynamics mainly by changing the F-actin structure. H2O2, via the oxidation of actin thiols (in particular, the sulfhydryl group of Cys-374), likely alters the actin C-terminus, influencing both subunit/subunit interactions and the spatial structure of the binding sites for cross-linking proteins in F-actin. We suggest that most of the effects of hydrogen peroxide on actin could be explained in the light of the "structural connectivity," demonstrated previously in actin.
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