Xanthine oxidase activates pro-matrix metalloproteinase-2 in cultured rat vascular smooth muscle cells through non-free radical mechanisms.
Xanthine oxidase activates pro-matrix metalloproteinase-2 in cultured rat vascular smooth muscle cells through non-free radical mechanisms.
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黄嘌呤氧化酶通过非自由基机制激活培养的大鼠血管平滑肌细胞中的前基质金属蛋白酶-2。
DOI：
10.1016/j.abb.2004.03.029
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发表时间：
2004
影响因子：
3.9
通讯作者：
Liu,KeJian
中科院分区：
文献类型：
--
作者：
Liu,Wenlan;Rosenberg,GaryA;Shi,Honglian;Furuichi,Takamitsu;Timmins,GrahamS;Cunningham,LeeA;Liu,KeJian
Reactive oxygen species (ROS) have been implicated in the regulation of matrix metalloproteinases (MMPs). The xanthine/xanthine oxidase (X/XO) reaction has been widely used as a source of exogenous ROS in studying MMPs, but commercial XO has also been known to be contaminated by proteolytic activity, and MMPs are protease sensitive substrate. We have investigated the activation of proMMP-2 by X/XO in cultured vascular smooth muscle cells (SMCs). SMCs were incubated with X/XO (unpurified or purified) or XO alone for 24h. X/XO activated proMMP-2 in a dose-dependent manner. A similar profile was observed using XO. Purified XO produced lower amounts of active MMP-2 compared to unpurified XO. EPR study showed that X/XO, not XO itself, produced superoxide anion, which was completely scavenged by SOD. However, X/XO-induced proMMP-2 activation could not be inhibited by combination of SOD and catalase. Incubation with XO either in cell-free conditioned media or in cells resulted in similar amounts of active MMP-2, suggesting that membrane-type-MMPs were not involved in proMMP-2 activation. This was further confirmed by the lack of inhibitory effect of hydroxamate MMP inhibitor, BB1101. Aprotinin blocked unpurified XO-induced proMMP-2 activation in a dose-dependent manner, demonstrating the proteolytic activity contained in XO is essential. We conclude that proteolytic activity contained in XO, rather the ROS derived from X/XO, is responsible for proMMP-2 activation in cultured SMCs. The results also suggest that caution needs to be taken when interpreting the reported results on activation of MMPs where X/XO had been used as an “authentic” source of superoxide anion.
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超氧化物、黄嘌呤氧化酶和血小板反应：氧化剂影响血小板机制的进一步研究
影响因子：
6.7
作者：
P. Levine;Danielle Sladdin;N. Krinsky
通讯作者：
N. Krinsky
影响因子：
20.1
作者：
GALIS, ZS;MUSZYNSKI, M;LIBBY, P
通讯作者：
LIBBY, P
通过血清蛋白组分抑制商业黄嘌呤氧化酶制剂中的蛋白水解污染物。
DOI：
--
发表时间：
1985
期刊：
Journal of Free Radicals in Biology & Medicine
影响因子：
--
作者：
R. Greenwald;S. Moak;S. Carsons;S. Rush
通讯作者：
S. Rush
商业黄嘌呤氧化酶中蛋白酶活性的细胞效应。
影响因子：
4.1
作者：
A. Ager;J. Gordon
通讯作者：
J. Gordon
商业黄嘌呤氧化酶制剂中蛋白酶活性对内皮细胞的刺激。
影响因子：
7.5
作者：
A. Ager;D. Wenham;J. Gordon
通讯作者：
J. Gordon