AmyCo: the amyloidoses collection

Katerina C Nastou1, Georgia I Nasi1, Paraskevi L Tsiolaki1

  • 1a Section of Cell Biology and Biophysics, Department of Biology, School of Sciences, National and Kapodistrian University of Athens , Panepistimiopolis , Athens , Greece.

Insights

Amyloid fibrils, linked to amyloidoses and other diseases, are now cataloged in AmyCo. This new database offers a comprehensive resource for understanding amyloid deposition disorders.

Area of Science:

  • Biochemistry
  • Pathology
  • Bioinformatics

Background:

  • Amyloid fibrils result from protein misfolding and aggregation, leading to amyloidoses and complications in other diseases.
  • The heterogeneity of amyloidoses necessitates better classification and understanding.
  • Amyloid deposition is a hallmark of various pathological conditions, including neurodegenerative and endocrine diseases.

Purpose of the Study:

  • To introduce AmyCo, a freely accessible database of diseases associated with amyloid deposition.
  • To classify 75 diseases into distinct categories: amyloidosis and clinical conditions with amyloidosis.
  • To provide a centralized, up-to-date repository for amyloid-related disorder information.

Main Methods:

  • Development of a comprehensive collection of amyloidoses and related clinical disorders.
  • Classification of diseases based on amyloid deposition.
  • Annotation of database entries with causative proteins, deposit components, and affected tissues.
  • Cross-referencing with established databases like ICD-10, MeSH, OMIM, PubMed, AmyPro, and UniProtKB.

Main Results:

  • AmyCo classifies 75 diseases related to amyloid deposition.
  • Each entry details the major protein component, other deposit constituents, and affected organs.
  • Database entries are extensively annotated and linked to multiple external resources.

Conclusions:

  • AmyCo represents the first comprehensive and up-to-date repository for amyloidoses and associated diseases.
  • The database facilitates research and understanding of amyloid deposition disorders.
  • The AmyCo web interface is publicly available for access and utilization.

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