Protein aggregation in the aging retina.
J Neuropathol Exp Neurol. 2011-01-01; 70(1): 63-68
DOI: 10.1097/nen.0b013e31820376cc
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1. J Neuropathol Exp Neurol. 2011 Jan;70(1):63-8. doi: 10.1097/NEN.0b013e31820376cc.
Protein aggregation in the aging retina.
Leger F(1), Fernagut PO, Canron MH, Léoni S, Vital C, Tison F, Bezard E, Vital A.
Author information:
(1)Pathology, Bordeaux University Hospital, Bordeaux, France.
The age-related altered expression of neuron-related proteins as seen in other
regions of the central nervous system is expected in the aging retina. Using
immunohistochemical techniques, we characterized the distribution and aggregation
of tau, βA4-amyloid, α-synuclein, and ubiquitin in human retina obtained from 19
enucleated eyes of patients aged 49 to 87 years and correlated the findings with
the ages. Using a phosphorylation-independent antibody, tau aggregates were
observed within the cytoplasm of several photoreceptor cells, and there was a
positive correlation between age and the number of tau-positive ganglionic cells.
Tau deposits were immunonegative with a phosphorylation-dependent antibody. We
did not observe βA4-amyloid in subretinal pigment epithelium deposits or in
neuroepithelial layers. α-Synuclein and ubiquitin inclusions were found in the
inner nuclear layer, and there was colocalization of these proteins. The
proportion of patients displaying such α-synuclein and/or ubiquitin
intracytoplasmic inclusions was significantly higher with aging. The presence of
ubiquitin deposits within drusen was remarkable, but diffuse ubiquitin aggregates
between the retinal pigment epithelium and Bruch membrane were also noticed.
These results indicate that protein aggregation in the retina increases with
aging and that tau, α-synuclein, and ubiquitin should be the subjects of future
investigations.
DOI: 10.1097/NEN.0b013e31820376cc
PMID: 21157377 [Indexed for MEDLINE]