SENP1 and SENP2 regulate SUMOylation of amyloid precursor protein

Takuma Maruyama, Yoichiro Abe, Takako Niikura

研究成果: Article

2 引用 (Scopus)

抄録

Amyloid β a key molecule in the pathogenesis of Alzheimer's disease (AD), is produced from amyloid precursor protein (APP) by the cleavage of secretases. APP is SUMOylated near the cleavage site of β-secretase. SUMOylation of APP reduces amyloid β production, but its regulatory system is still unclear. SUMOylation, a modification at a lysine residue of a target protein, is mediated by activating, conjugating, and ligating enzymes and is reversed by a family of sentrin/SUMO-specific proteases (SENPs). Here, we found that both SENP1 and SENP2 induced de-SUMOylation of APP. Using quantitative PCR, we also found that expression of SENP1 but not SENP2 increased in an age-dependent manner only in female mice. The results of immunoblot analyses showed that the protein expression was consistent with the PCR results. Females, compared to males, have a higher incidence of AD in humans and show more aggressive amyloid pathology in AD mouse models. Our results provide a clue to understanding the role of SUMOylation in the sex difference in AD pathogenesis.

元の言語English
記事番号e00601
ジャーナルHeliyon
4
発行部数4
DOI
出版物ステータスPublished - 2018 4 1

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Sumoylation
Amyloid beta-Protein Precursor
Alzheimer Disease
Amyloid
Amyloid Precursor Protein Secretases
SUMO-1 Protein
Polymerase Chain Reaction
Sex Characteristics
Lysine
Proteins
Peptide Hydrolases
Pathology
Incidence
Enzymes

ASJC Scopus subject areas

  • General

これを引用

SENP1 and SENP2 regulate SUMOylation of amyloid precursor protein. / Maruyama, Takuma; Abe, Yoichiro; Niikura, Takako.

:: Heliyon, 巻 4, 番号 4, e00601, 01.04.2018.

研究成果: Article

Maruyama, Takuma ; Abe, Yoichiro ; Niikura, Takako. / SENP1 and SENP2 regulate SUMOylation of amyloid precursor protein. :: Heliyon. 2018 ; 巻 4, 番号 4.
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