Amyloid Evolvability and Cancer

Yoshiki Takamatsu; Gilbert Ho; Makoto Hashimoto

doi:10.1016/j.trecan.2020.04.001

Amyloid Evolvability and Cancer

Trends Cancer. 2020 Aug;6(8):624-627. doi: 10.1016/j.trecan.2020.04.001. Epub 2020 May 5.

Authors

Yoshiki Takamatsu¹, Gilbert Ho², Makoto Hashimoto³

Affiliations

¹ Tokyo Metropolitan Institute of Medical Science, 2-1-6 Kamikitazawa, Setagaya-ku, Tokyo, Japan.
² Pacific Center for Neurological Disease (PCND) Neuroscience Research Institute, Poway, CA, USA.
³ Tokyo Metropolitan Institute of Medical Science, 2-1-6 Kamikitazawa, Setagaya-ku, Tokyo, Japan. Electronic address: hashimoto-mk@igakuken.or.jp.

PMID: 32386876
DOI: 10.1016/j.trecan.2020.04.001

Abstract

p53 and γ-synuclein are two major regulators of cancer pathogenesis that have the propensity to form amyloid-like fibrils reminiscent of those in neurodegenerative diseases. Here we propose that fibril formation by these amyloidogenic molecules reflects evolvability, an acquired epigenetic inheritance that may be involved in cancer proliferation, drug resistance, and metastasis.

Keywords: amyloidogenic proteins (APs); cancer; evolvability; neurodegenerative diseases; p53; stress; γ-synuclein (γS).

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amyloid / genetics*
Amyloid / metabolism
Carcinogenesis / genetics
Carcinogenesis / pathology
Cell Proliferation / genetics
Drug Resistance, Neoplasm / genetics
Epigenesis, Genetic
Genetic Predisposition to Disease
Humans
Mutation, Missense
Neoplasm Proteins / genetics
Neoplasm Proteins / metabolism*
Neoplasms / genetics
Neoplasms / pathology*
Tumor Suppressor Protein p53 / genetics
Tumor Suppressor Protein p53 / metabolism*
gamma-Synuclein / genetics
gamma-Synuclein / metabolism*

Substances

Amyloid
Neoplasm Proteins
SNCG protein, human
TP53 protein, human
Tumor Suppressor Protein p53
gamma-Synuclein