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Deyrick Osmond Dean, Michael Tytell; Hsp25 and -90 Immunoreactivity in the Normal Rat Eye. Invest. Ophthalmol. Vis. Sci. 2001;42(12):3031-3040.
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purpose. The distributions of heat shock protein (Hsp)25 and -90 in various
regions of the rat eye are described to provide a basis for
understanding their roles in normal, damaged, and diseased ocular
tissues. This work complements the earlier examination of Hsp70 and
Hsc70 (the constitutive form).
methods. Eyes of adult male Sprague-Dawley rats were fixed in methacarn and
embedded in paraffin. Sagittal sections (10 μm) through the optic
nerve were stained with hematoxylin and eosin, or incubated with
anti-Hsp90, anti-Hsp25, or control IgG. Bound antibody was visualized
using an avidin-biotin–horseradish peroxidase detection system.
results. Hsp90 immunoreactivity was abundant in the retina, whereas only low
levels of Hsp25 were detected there. In the optic nerve, the relative
difference in immunoreactivity for the two Hsps was reversed, with
Hsp25 being considerably greater than Hsp90. Both Hsps were detected at
low levels in the retinal pigment epithelium (RPE), except for that
portion within 250 μm of the optic disc, where Hsp25 and -90
immunoreactivities were increased. Similar to the optic nerve, the
corneal epithelium showed greater staining for Hsp25 than for Hsp90,
and basal cells contained the highest levels of immunoreactivity for
both Hsps. In the ciliary body and iris, Hsp25 and -90 were abundant
and similarly distributed in the epithelial and stromal layers.
conclusions. Each of the ocular tissues had distinctive patterns of Hsp25 and -90
immunostaining. These results suggest that the various structures of
the eye have unique requirements for the particular chaperoning and
supportive functions of these two Hsp
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