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Abstract #13763 Published in IGR 8-2
The identification of myocilin-associated proteins in the human trabecular meshwork
Fautsch MP; Vrabel AM; Johnson DHExperimental Eye Research 2006; 82: 1046-1052
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 > 1x106 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.
Dr. M.P. Fautsch, Department of Ophthalmology, Mayo Clinic College of Medicine, Rochester, MN, USA
Classification:
3.5 Molecular biology incl. SiRNA (Part of: 3 Laboratory methods)
