Rutin stimulates sarcoplasmic reticulum Ca2+-ATPase activity (SERCA1) and protects SERCA1 from peroxynitrite mediated injury

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• 作者：Jana Viskupicova ; Miriam K. Strosova…
• 关键词：Rutin ; SERCA1 ; ONOO? Structural and conformational changes ; In silico study
• 刊名：Molecular and Cellular Biochemistry
• 出版年：2015
• 出版时间：April 2015
• 年：2015
• 卷：402
• 期：1-2
• 页码：51-62
• 全文大小：1,574 KB
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• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Biochemistry
  Medical Biochemistry
  Oncology
  Cardiology
  
• 出版者：Springer Netherlands
• ISSN：1573-4919

文摘

In this study we analyzed the protective action of the flavonoid rutin on peroxynitrite (ONOO?/sup>) mediated impairment of sarcoplasmic reticulum Ca2+-ATPase (SERCA1 isoform), especially related to posttranslational and conformational changes. Rutin concentration dependently protected ONOO?/sup> induced SERCA1 activity decrease with effective concentration EC50 of 18?±?1.5?μM. Upon treatment with ONOO?/sup>, this flavonoid also prevented SERCA1 from thiol group oxidation and significantly reduced tyrosine nitration and protein carbonyl formation. In the absence of ONOO?/sup>, rutin (250 and 350?μM) stimulated SERCA1 activity at 2.1?mM [ATP] and 10?μM [Ca2+]free. According to changes in the kinetic parameters V max and K m with regard to [ATP], rutin (250?μM) increased the rate of enzyme catalysis and decreased the affinity of SERCA1 to ATP. FITC fluorescence decreased in the presence of rutin (150 and 250?μM), indicating conformational changes in the cytosolic ATP binding region of SERCA1. In silico study confirmed the binding of rutin in the cytosolic region of SERCA1, in the vicinity of the ATP binding site. Residue Glu183 localized within the conserved TGES loop was identified to play a key role in rutin-SERCA1 interaction (H-bond length of 1.7??), elucidating the ability of rutin to affect the affinity of SERCA1 to ATP. The binding of rutin in the proximity of Lys515 is likely to cause a decrease in FITC fluorescence.