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E. Timothy O’Brien, Xiao-ou Ren, Yanhong Wang; Localization of Myocilin to the Golgi Apparatus in Schlemm’s Canal Cells. Invest. Ophthalmol. Vis. Sci. 2000;41(12):3842-3849.
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purpose. Biochemical and genetic evidence suggests that overexpression of or
mutations in myocilin within the cells of the aqueous humor outflow
pathway play a significant role in the development of steroid-induced
and several other open-angle glaucomas. As a baseline to understanding
the normal and pathologic function of myocilin, we determined the
subcellular localization of myocilin in steroid-treated human
Schlemm’s canal endothelial (SC) cells.
methods. SC cells were grown to confluence, treated with dexamethasone for 10
days, and then stained using antibodies against myocilin, tubulin, orβ
-COP (a specific golgi protein) or vital stains for endoplasmic
reticulum (ER) and golgi. Brefeldin A (BFA) and nocodazol (NZ) were
used to disrupt the golgi or microtubules.
results. The authors found that myocilin staining was (a) always centered around
the centrosome, (b) very similar to the pattern seen with NBD-ceramide,
(c) was disrupted in characteristic ways by BFA and NZ and (d) showed
extensive colocalization with β-COP.
conclusions. Results indicate that myocilin is localized to the golgi in SC cells.
Such localization is consistent with myocilin being processed for
secretion but is also consistent with sequence analysis and other data
that suggest that myocilin or myocilin mutations might be targeted to
the cytoplasmic face of the golgi, and under some circumstances play a
role in or interfere with golgi or vesicle function. How such
interference could eventually lead to open angle glaucoma is
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