Involvement of phosphorylation of myosin phosphatase by ROCK in trabecular meshwork and ciliary muscle contraction
Involvement of phosphorylation of myosin phosphatase by ROCK in trabecular meshwork and ciliary muscle contraction
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DOI：
10.1006/bbrc.2001.5751
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发表时间：
2001-10-26
影响因子：
3.1
通讯作者：
Shearer, TR
中科院分区：
文献类型：
--
作者：
Fukiage, C;Mizutani, K;Shearer, TR
平滑肌收缩的控制是维持正常眼内压的重要因素。然而，引起眼睛中磷酸化/去磷酸化方案控制变化的具体因素尚未明确。本实验的目的是（i）确定ROCK（Rho相关卷曲螺旋形成激酶）在猴和兔眼组织中的定位，以及（ii）测量卡巴胆碱诱导的小梁网或睫状肌收缩期间ROCK底物的磷酸化。我们发现ROCK I和II的mRNA在兔和猴的大多数眼组织中表达。ROCK I和H蛋白存在于除透镜外的所有研究眼组织中。当小梁网或睫状肌与卡巴胆碱孵育以诱导收缩时，肌球蛋白磷酸酶的肌球蛋白结合亚基（MBS）的磷酸化在1 min内开始，并持续至少1 h。这种磷酸化与小梁网或睫状肌的收缩密切相关。这些结果提示ROCK可能通过磷酸化肌球蛋白磷酸酶的MES来调节小梁网或睫状肌的收缩。(C)北京：科学出版社.
The control of smooth muscle contraction is an important factor in maintaining normal intraoculer pressure. However, the specific factors causing changes in control by phosphorylation/dephosphorylation schemes in the eye are not well-defined. The purposes of this experiment were to (i) determine the localization of ROCK (Rho-associated, coiled coil-forming kinase) in monkey and rabbit eye tissues and (ii) measure phosphorylation of ROCK substrate during trabecular meshwork or ciliary muscle contraction induced by carbachol. We found that mRNAs for both ROCK I and II were expressed in most eye tissues from rabbit and monkey. Proteins for ROCK I and H were present in all eye tissues studied except lens. When trabecular meshwork or ciliary muscle were incubated with carbachol to induce contraction, phosphorylation of the myosin-binding subunit (MBS) of myosin phosphatase, a substrate for ROCK started within 1 min and continued for at least I h. This phosphorylation was well correlated with contraction of trabecular meshwork or ciliary muscle. These results suggested that ROCK might regulate contraction of trabecular meshwork or ciliary muscle through phosphorylation of MES of myosin phosphatase. (C) 2001 Academic Press.