Impact of actin glutathionylation on the actomyosin-S1 ATPase.
Impact of actin glutathionylation on the actomyosin-S1 ATPase.
复制标题
肌动蛋白谷胱甘肽化对肌动球蛋白-S1 ATP 酶的影响。
DOI:
10.1021/bi900669m
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发表时间:
2009
期刊:
影响因子:
2.9
通讯作者:
Ogut,Ozgur
中科院分区:
文献类型:
--
作者:
Pizarro,GresinO;Ogut,Ozgur
Glutathionylation of intracellular proteins is an established physiological regulator of protein function. In multiple models, including ischemia-reperfusion of the heart, increased oxidative stress results in the glutathionylation of sarcomeric actin. We hypothesized that actin glutathionylation may play a role in the multifactorial change in cardiac muscle contractility observed during this pathophysiological state. Therefore, the functional impact of glutathionylated actin on the interaction with myosin-S1 was examined. Substituting glutathionylated F-actin for unmodified F-actin reduced the maximum actomyosin-S1 ATPase, and this was accompanied by an increase in the activation energy of the steady state ATPase. Measurement of steady state binding did not suggest a large impact of actin glutathionylation on the binding to myosin-S1. However, transient binding and dissociation kinetics determined by stopped-flow methods demonstrated that although actin glutathionylation did not significantly alter the rate constant of myosin-S1 binding, there was a significant decrease in the rate of ATP-induced myosin-S1 detachment in the presence of ADP. These results suggest that actin glutathionylation may play a limited but defined role in the alteration of contractility following oxidative stress to the myocardium, particularly through a decrease in the actomyosin ATPase activity.
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影响因子:
2.9
作者:
Furch, M;Geeves, MA;Manstein, DJ
通讯作者:
Manstein, DJ
DOI:
10.1073/pnas.82.3.658
发表时间:
1985-01-01
影响因子:
11.1
作者:
SIEMANKOWSKI, RF;WISEMAN, MO;WHITE, HD
通讯作者:
WHITE, HD
影响因子:
4.8
作者:
M. Mezgueldi;N. Tang;S. Rosenfeld;E. Ostap
通讯作者:
E. Ostap
影响因子:
4.8
作者:
G. Drewes;H. Faulstich
通讯作者:
H. Faulstich
影响因子:
7.4
作者:
Dalle-Donne, I;Giustarini, D;Milzani, A
通讯作者:
Milzani, A