Ocular Amyloid, Condensates, and Aggregates – Higher-Order Protein Assemblies Participate in Both Retinal Degeneration and Function

Michael H. Hayes, Da Nae R. Woodard, John D. Hulleman

Research output: Chapter in Book/Report/Conference proceedingChapter


The formation of higher-order protein assemblies (commonly called protein aggregates) has long been associated with disease states, particularly in neurodegenerative disorders. Within the eye, protein aggregation has also been implicated in various retinal degenerative diseases ranging from retinitis pigmentosa (RP) to Malattia Leventinese/Doyne Honeycomb Retinal Dystrophy (ML/DHRD) to age-related macular degeneration (AMD). Yet, many essential cellular processes including transcription, translation, and the formation of non-membrane bound organelles require the formation of functional, non-pathologic protein aggregates to maintain cellular homeostasis. Thus, functional protein aggregates, also called condensates, likely play essential roles in maintaining normal retina function. However, currently, there is a critical gap in our knowledge: What proteins form higher-order assemblies under normal conditions within the retina and what function do these structures serve? Herein, we present data suggesting that protein aggregation is identifiable in multiple retinal layers of normal, healthy murine retina, and briefly discuss the potential contributions of aggregated proteins to normal retinal function, with a focus on the photoreceptor inner and outer segment.

Original languageEnglish (US)
Title of host publicationAdvances in Experimental Medicine and Biology
Number of pages5
StatePublished - 2023
Externally publishedYes

Publication series

NameAdvances in Experimental Medicine and Biology
ISSN (Print)0065-2598
ISSN (Electronic)2214-8019

Bibliographical note

Funding Information:
Acknowledgments This work was funded by the Roger and Dorothy Hirl Endowed Research Fund and the NEI Core Grant for Vision Research (P30-EY030413).

Publisher Copyright:
© 2023, The Author(s), under exclusive license to Springer Nature Switzerland AG.


  • Amyloid
  • Condensate
  • Higher-order assembly
  • Protein aggregation
  • Retinal degeneration
  • Thioflavin T

PubMed: MeSH publication types

  • Journal Article


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