The identification of myocilin-associated proteins in the human trabecular meshwork

Michael P. Fautsch, Anne M. Vrabel, Douglas H. Johnson

Research output: Contribution to journalArticle

31 Scopus citations

Abstract

Myocilin forms high molecular weight complexes in vivo presumably due to interaction with itself and other myocilin binding proteins. To identify myocilin interacting proteins, yeast 2-hybrid analysis was performed on >1×106 human trabecular meshwork cDNA clones. Coimmunoprecipitation and Far Western analysis were also performed on cell lysates obtained from fresh human trabecular meshworks or cultured human monolayer trabecular cell lines. Among the different methods, 46 candidate myocilin-associated proteins were identified, including molecules associated with the extracellular matrix, cytoskeleton, signaling, and metabolism. The most consistent interaction was myocilin-myocilin binding. Yeast-2 hybrid and Far Western analysis also found an association between myocilin and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). None of the other candidate myocilin interacting proteins were identified in more than one method. Characterization of these potential interacting proteins may help to better understand the function of myocilin in the trabecular meshwork and aqueous outflow pathway.

Original languageEnglish (US)
Pages (from-to)1046-1052
Number of pages7
JournalExperimental Eye Research
Volume82
Issue number6 SPEC. ISS.
DOIs
StatePublished - Jun 2006

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Keywords

  • TIGR
  • myocilin
  • myocilin-associated proteins
  • trabecular meshwork

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience

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