Involvement of phosphorylation of myosin phosphatase by ROCK in trabecular meshwork and ciliary muscle contraction

Chiho Fukiage, Kanako Mizutani, Yoko Kawamoto, Mitsuyoshi Azuma, Thomas R. Shearer

Research output: Contribution to journalArticle

26 Scopus citations

Abstract

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 II 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 1 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 MBS of myosin phosphatase.

Original languageEnglish (US)
Pages (from-to)296-300
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume288
Issue number2
DOIs
StatePublished - Oct 26 2001

Keywords

  • Ciliary muscle contraction
  • Myosin phosphatase
  • Phosphorylation
  • Rho-associated protein kinase
  • Trabecular meshwork contraction

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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