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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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Methods to Study Changes in Inherent Protein Aggregation with Age in Caenorhabditis elegans
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Published on: November 26, 2017

Protein aggregation in the aging retina.

François Leger1, Pierre-Olivier Fernagut, Marie-Hélène Canron

  • 1Pathology, Bordeaux University Hospital, Bordeaux, France.

Journal of Neuropathology and Experimental Neurology
|December 16, 2010
PubMed
Summary
This summary is machine-generated.

Protein aggregation in the aging retina increases with age. Researchers found tau, alpha-synuclein, and ubiquitin aggregates in human retinal tissues, highlighting their potential role in age-related retinal changes.

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Area of Science:

  • Ophthalmology
  • Neuroscience
  • Gerontology

Background:

  • Aging is associated with altered protein expression in the central nervous system.
  • Similar age-related changes in protein expression are anticipated in the aging retina.

Purpose of the Study:

  • To investigate the distribution and aggregation of key proteins (tau, beta-amyloid, alpha-synuclein, ubiquitin) in the aging human retina.
  • To correlate protein aggregation with patient age.

Main Methods:

  • Immunohistochemical techniques were employed to analyze retinal tissues from 19 human donors (aged 49-87).
  • Specific antibodies were used to detect tau (phosphorylation-independent and dependent), beta-amyloid, alpha-synuclein, and ubiquitin.
  • Protein distribution and colocalization were examined.

Main Results:

  • Tau aggregates were found in photoreceptor cells; tau-positive ganglionic cells correlated positively with age.
  • Beta-amyloid was not detected in key retinal layers or sub-RPE deposits.
  • Alpha-synuclein and ubiquitin inclusions were observed in the inner nuclear layer, increasing with age.
  • Ubiquitin deposits were found in drusen and between the retinal pigment epithelium and Bruch membrane.

Conclusions:

  • Protein aggregation, including tau, alpha-synuclein, and ubiquitin, demonstrably increases in the human retina with aging.
  • These proteins are significant targets for future research into age-related retinal conditions.
  • The findings suggest a link between aging and the accumulation of specific proteins within the retina.