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Rapid Generation of Amyloid from Native Proteins In vitro
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Amyloid Evolvability and Cancer.

Yoshiki Takamatsu1, Gilbert Ho2, Makoto Hashimoto1

  • 1Tokyo Metropolitan Institute of Medical Science, 2-1-6 Kamikitazawa, Setagaya-ku, Tokyo, Japan.

Trends in Cancer
|May 11, 2020
PubMed
Summary

p53 and gamma-synuclein proteins can form amyloid-like fibrils, similar to those seen in neurodegenerative diseases. This fibril formation may represent an epigenetic mechanism driving cancer progression, including drug resistance and metastasis.

Keywords:
amyloidogenic proteins (APs)cancerevolvabilityneurodegenerative diseasesp53stressγ-synuclein (γS)

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Area of Science:

  • Molecular biology
  • Cancer research
  • Neurodegenerative diseases

Background:

  • p53 and gamma-synuclein are key regulators in cancer.
  • These proteins can form amyloid-like fibrils, a characteristic of neurodegenerative diseases.

Purpose of the Study:

  • To investigate the role of amyloid fibril formation by p53 and gamma-synuclein in cancer.
  • To propose fibril formation as a mechanism of acquired epigenetic inheritance in cancer.

Main Methods:

  • Analysis of p53 and gamma-synuclein protein structures and aggregation.
  • Investigation of the link between fibril formation and cancer hallmarks.

Main Results:

  • p53 and gamma-synuclein exhibit amyloidogenic properties.
  • Fibril formation is proposed as a potential mechanism for cancer evolvability.

Conclusions:

  • Amyloid fibril formation by p53 and gamma-synuclein may contribute to cancer proliferation, drug resistance, and metastasis.
  • This process represents a form of acquired epigenetic inheritance in cancer pathogenesis.