Journal info
Aims and Scope |
||
Select Journal
Journals
Bratislava Medical Journal Endocrine Regulations General Physiology and Biophysics 2024 2023 2022 2021 2020 2019 2018 2017 2016 2015 2014 2013 2012 2011 2010 2009 2008 2007 Neoplasma Acta Virologica Studia Psychologica Cardiology Letters Psychológia a patopsych. dieťaťa Kovove Materialy-Metallic Materials Slovenská hudbaWebshop Cart
Your Cart is currently empty.
Info: Your browser does not accept cookies. To put products into your cart and purchase them you need to enable cookies.
General Physiology and Biophysics Vol.28, No.2, p.195–209, 2009 |
||
Title: Oxidative injury induced by hypochlorous acid to Ca-ATPase from sarcoplasmic reticulum of skeletal muscle and protective effect of trolox | ||
Author: Miriam Strosova, Jana Karlovska, Corinne M. Spickett, Tilman Grune, Zuzana Orszagova, Lubica Horakova | ||
Abstract: Hypochlorous acid (HOCl) concentration-dependently decreased ATPase activity and SH groups of pure Ca-ATPase from sarcoplasmic reticulum (SERCA) of rabbit skeletal muscle with IC50 of 150 µmol/l and 6.6 µmol/l, respectively. This indicates that SH goups were not critical for impairment of Ca-ATPase activity. Pure Ca-ATPase activity was analysed individually with respect to both substrates, Ca2+ and ATP. Concerning dependence of ATPase activity on HOCl (150 µmol/l) as a function of free Ca2+ and ATP, Vmax of both dependences decreased significantly, while the affinities to individual substrates were not influenced, with the exception of the regulatory binding site of ATP. On increasing HOCl concentration, fluorescence of fluorescein-5-isothiocyanate (FITC) decreased, indicating binding of HOCl to nucleotide binding site of SERCA. A new fragment appeared at 75 kDa after HOCl oxidation of SR, indicating fragmentation of SERCA. Fragmentation may be associated with protein carbonyl formation. The density of protein carbonyl bands at 75 and 110 kDa increased concentration- and time-dependently. Trolox (250 µmol/l) recovered the Ca-ATPase activity decrease induced by HOCl, probably by changing conformational properties of the Ca-ATPase protein. Trolox inhibited FITC binding to SERCA. |
||
Keywords: Ca-ATPase — HOCl oxidative stress — Trolox | ||
Year: 2009, Volume: 28, Issue: 2 | Page From: 195, Page To: 209 | |
doi:10.4149/gpb_2009_02_195 |
||
|
download file |
|