Glutathionyl(cysteine-374) actin forms filaments of low mechanical stability |
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| Institution: | 1. Departamento de Ingeniería, Universidad de Guanajuato, Guanajuato, C.P. 36000, Mexico;2. Centro de Investigaciones y de Estudios Avanzados del I.P.N. Unidad Querétaro, Libramiento Norponiente No. 2000 Facc. Real de Juriquilla, Querétaro, Querétaro, C.P. 76230, Mexico;3. División de Investigación y Posgrado, Facultad de Ingeniería, Universidad Autónoma de Querétaro, Cerro de las Campanas s/n C.P, 76010, Querétaro, Qro, Mexico;4. Centro de Física Aplicada y Tecnología Avanzada, UNAM, A.P1-1010, C.P. 76000, Querétaro, Qro, Mexico;1. Institute of Biochemistry I–Pathobiochemistry, Faculty of Medicine, Goethe-University Frankfurt, 60590 Frankfurt am Main, Germany;2. Department of Medicine II, University Medical Center, Johannes Gutenberg-University Mainz, 55116 Mainz, Germany;3. Fraunhofer Institute for Molecular Biology and Applied Ecology IME, Project Group Translational Medicine & Pharmacology TMP, and Goethe-University Frankfurt, 60596 Frankfurt am Main, Germany;4. Institute of Cardiovascular Physiology–Physiology I, Faculty of Medicine, Goethe-University Frankfurt, 60590 Frankfurt am Main, Germany;1. Molecular Immunology and Inflammation Branch, NIAMS, NIH, Rockville, MD 20892, USA;2. Immunoregulation Section, Autoimmunity Branch, NIAMS, NIH, Rockville, MD 20892, USA;3. Office of Science and Technology, NIAMS, NIH, Rockville, MD 20892, USA;4. Translational Gastroenterology Unit, Experimental Medicine Division, John Radcliffe Hospital, University of Oxford, UK;5. Genenetics and Pathogenesis of Allergy Section, Laboratory of Allergic Diseases, NIAID, NIH, Rockville, MD 20892, USA;6. Metaorganism Immunity Section, Laboratory of Immune System Biology, NIAID, NIH, Rockville, MD 20892, USA;1. Department of Physiology and Pharmacology, Schulich School of Medicine and Dentistry, Western University, London, ON N6A 5C1, Canada;2. Department of Molecular Genetics and Molecular Biochemistry, Center for Translational Medicine, Lewis Katz School of Medicine, Temple University, Philadelphia, PA 19140, USA;3. Department of Biochemistry and Biomedical Sciences, McMaster University, Hamilton, ON L8S 4K1, Canada;4. Department of Biochemistry, Schulich School of Medicine and Dentistry, Western University, London, ON N6A 5C1, Canada;1. Division of Cardiology, Department of Medicine, Emory University, 101 Woodruff Circle, 308a WMB, Atlanta, GA 30322, United States;2. Department of Cardiovascular Medicine, Xiangya Hospital, Central South University, Changsha, China;3. Department of Medicine and Bioregulatory Science, Graduate School of Medical Sciences, Kyushu University, Japan |
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| Abstract: | Rabbit muscle actin reacts with 2,4-dinitrophenylglutathionyldisulfide, forming a mixed disulfide in position 374. The product S-(cysteine-374)glutathionyl actin forms filaments which are easily disrupted under shearing stress. Even weak mechanical strain, as exerted, for example, during capillary viscometry or heating the solution to 37°C, leads to considerable breakage of these filaments. Because of spontaneous repair which consumes ATP, the mechanically broken filaments exhibit an approx. 6-fold enhanced steady-state ATPase activity as compared to normal F-actin. Monomers of glutathionyl actin have a reduced affinity for their bound nucleotide and a slightly increased critical concentration. Disruption of the filaments and enhanced ATPase activity are reversed by the addition of KCl or the mushroom toxin phalloidin. By the large stabilizing effects of KCl and phalloidin on glutathionyl actin filaments we propose glutathionyl actin as a tool for detecting filament-stabilizing agents and for studying the different mechanisms of filament stabilization |
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