以下是為大家整理的關(guān)于《英語(yǔ)科普知識(shí)：細(xì)胞如何控制離子的進(jìn)出》文章，供大家學(xué)習(xí)參考！
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A common protein plays a different role than previously1 thought in the opening and closing of channels that let ions flow in and out of our cells, researchers at Johns Hopkins report. Those channels are critical to life, as having the right concentrations of sodium2 and calcium3 ions in cells enables healthy brain communication, heart contraction4 and many other processes. The new study reveals that a form of calmodulin long thought to be dormant5 actually opens these channels wide. The finding is likely to bring new insight into disorders6 caused by faulty control of these channels, such as cardiac arrhythmias, epilepsy and Parkinson's disease, the researchers say. A report on the finding appears in the Oct. 23 issue of the journal Cell.
In the current model, explains David Yue, M.D., Ph.D. , a professor of biomedical engineering and neuroscience at the Johns Hopkins University School of Medicine, calmodulin can do little until it binds8 to calcium, which changes its shape and snaps it into action. The activated9 calmodulin can then bind7 to a specialized10 control lever inside calcium and sodium channels, which closes the channels.
The new study revises this viewpoint by devising ways to deliver surges of calcium-free calmodulin to channels. In so doing, "it can be seen that calcium-free calmodulin is in no way dormant, but instead markedly boosts the opening of calcium and sodium channels to begin with," Yue says. When calcium binds to the "resident" calcium-free calmodulin on channels, this initial enhancement dissipates. "The two forms of calmodulin are both powerful, each imposing11 opposing actions that together maintain exquisite12 control, akin13 to the 'yin-yang' balance in Chinese philosophy," Yue says. "This insight into how the calmodulin-controlled lever works could ultimately help in finding treatments for a plethora14 of conditions that stem from faulty ion channels."
小編推薦： 英文歌詞| 英文網(wǎng)名| 英語(yǔ)祝福語(yǔ)| 英文名字| 英語(yǔ)詩(shī)歌| 英語(yǔ)作文網(wǎng)
A common protein plays a different role than previously1 thought in the opening and closing of channels that let ions flow in and out of our cells, researchers at Johns Hopkins report. Those channels are critical to life, as having the right concentrations of sodium2 and calcium3 ions in cells enables healthy brain communication, heart contraction4 and many other processes. The new study reveals that a form of calmodulin long thought to be dormant5 actually opens these channels wide. The finding is likely to bring new insight into disorders6 caused by faulty control of these channels, such as cardiac arrhythmias, epilepsy and Parkinson's disease, the researchers say. A report on the finding appears in the Oct. 23 issue of the journal Cell.
In the current model, explains David Yue, M.D., Ph.D. , a professor of biomedical engineering and neuroscience at the Johns Hopkins University School of Medicine, calmodulin can do little until it binds8 to calcium, which changes its shape and snaps it into action. The activated9 calmodulin can then bind7 to a specialized10 control lever inside calcium and sodium channels, which closes the channels.
The new study revises this viewpoint by devising ways to deliver surges of calcium-free calmodulin to channels. In so doing, "it can be seen that calcium-free calmodulin is in no way dormant, but instead markedly boosts the opening of calcium and sodium channels to begin with," Yue says. When calcium binds to the "resident" calcium-free calmodulin on channels, this initial enhancement dissipates. "The two forms of calmodulin are both powerful, each imposing11 opposing actions that together maintain exquisite12 control, akin13 to the 'yin-yang' balance in Chinese philosophy," Yue says. "This insight into how the calmodulin-controlled lever works could ultimately help in finding treatments for a plethora14 of conditions that stem from faulty ion channels."