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Studies on alpha-synuclein and islet amyloid polypeptide interaction.

Ye Wang1, Joakim Bergström2, Martin Ingelsson2,3,4

  • 1Departments of Medical Cell Biology, Uppsala University, Uppsala, Sweden.

Frontiers in Molecular Biosciences
|February 16, 2023
PubMed
Summary

Alpha-synuclein (aSyn) and islet amyloid polypeptide (IAPP) coexist in pancreatic cells. While aSyn fibrils can seed IAPP amyloid formation in vitro, their direct interaction

Keywords:
BiFCalpha-synucleinamyloidcross-seedingislet amyloid polypeptide

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Area of Science:

  • Biochemistry and Molecular Biology
  • Endocrinology and Metabolism
  • Neurodegenerative Diseases

Background:

  • Parkinson's disease and type 2 diabetes share pathogenic mechanisms involving local amyloid depositions.
  • Alpha-synuclein (aSyn) forms Lewy bodies in Parkinson's disease, while islet amyloid polypeptide (IAPP) forms amyloid in type 2 diabetes.
  • Investigating potential interactions between aSyn and IAPP is crucial for understanding shared pathobiology.

Purpose of the Study:

  • To investigate the interaction and co-localization of alpha-synuclein (aSyn) and islet amyloid polypeptide (IAPP) in human pancreatic tissues.
  • To assess the functional consequences of aSyn and IAPP interactions on beta-cell function and viability.
  • To determine the cross-seeding potential between aSyn and IAPP fibrils in vitro.

Main Methods:

  • Utilized antibody-based detection, proximity ligation assay (PLA), and immuno-transmission electron microscopy (immuno-TEM) for co-localization studies.
  • Employed bimolecular fluorescence complementation (BiFC) to study interactions in HEK 293 cells.
  • Conducted Thioflavin T assays for cross-seeding experiments and siRNA for aSyn knockdown.

Main Results:

  • Demonstrated intracellular co-localization of aSyn with IAPP in human pancreatic islets, with aSyn present in secretory granules.
  • Showed that preformed aSyn fibrils could seed IAPP fibril formation in vitro, but not vice versa.
  • Found that aSyn knockdown or overexpression did not significantly affect beta-cell function or viability.

Conclusions:

  • aSyn and IAPP are found in proximity within pancreatic beta-cells.
  • aSyn fibrils exhibit cross-seeding potential with IAPP in vitro.
  • The pathogenic significance of aSyn-IAPP interaction in type 2 diabetes remains an open question.