Protein oxidation, tyrosine nitration, and inactivation of sarcoplasmic reticulum Ca2+‐ATPase in low‐frequency stimulated rabbit muscle

FEBS Letters

Pette, Dirk¹  Ayoub, Ahmed T¹  Klebl, Bert M¹ 

[1] Fakultät für Biologie, Universität Konstanz, D-78457 Constance, Germany

关键词: Ca2+-ATPase;    Chronic low-frequency stimulation;    Inactivation;    Nitrotyrosine;    Peroxynitrite;    Protein oxidation;   

DOI  :  10.1016/S0014-5793(98)00053-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Sustained contractile activity by chronic low-frequency stimulation in rabbit fast-twitch muscle causes a partial (40–50%) inactivation of the sarcoplasmic reticulum (SR) Ca²⁺-ATPase and, with prolonged stimulation, a SERCA1a to SERCA2a transition. To investigate the underlying mechanism of the inactivation which precedes the isoform transition, we analyzed SR from 4-day stimulated muscles for Ca²⁺-ATPase activity, lipid peroxidation, SH and carbonyl groups, and nitrotyrosine. At unaltered SH group and malondialdehyde contents, carbonyl groups were elevated 50% in the SR from stimulated muscles. Immunoblotting with anti-dinitrophenyl and anti-nitrotyrosine antibodies revealed strong labeling of the Ca²⁺-ATPase, suggesting the inactivation of the enzyme to result from protein oxidation and peroxynitrite-mediated tyrosine nitration.

【 授权许可】

Unknown