<P><B>Abstract</B></P> <P>The DJ-1 protein engages in diverse cellular and pathological processes, including tumorigenesis, apoptosis, sperm fertilization, and the progression of Parkinson’s disease (PD). The funct...
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https://www.riss.kr/link?id=A107520577
2018
-
SCI,SCIE,SCOPUS
학술저널
1650-1658(9쪽)
0
상세조회0
다운로드다국어 초록 (Multilingual Abstract)
<P><B>Abstract</B></P> <P>The DJ-1 protein engages in diverse cellular and pathological processes, including tumorigenesis, apoptosis, sperm fertilization, and the progression of Parkinson’s disease (PD). The funct...
<P><B>Abstract</B></P> <P>The DJ-1 protein engages in diverse cellular and pathological processes, including tumorigenesis, apoptosis, sperm fertilization, and the progression of Parkinson’s disease (PD). The functional dimeric form of DJ-1 transforms into non-functional filamentous aggregates in an inorganic phosphate (P<SUB>i</SUB>)-dependent manner in vitro. Here, we demonstrated that P<SUB>i</SUB> and reactive oxygen species (ROS) induce DJ-1 aggregation in Neuro2A and SH-SY5Y cells. Remarkably, tartrate treatment significantly reduced P<SUB>i</SUB>- and ROS-induced DJ-1 aggregation and restored P<SUB>i</SUB>- and ROS-provoked cell death using quantitative data as mean±standard deviation, and statistics. Mechanistically, tartrate prevented DJ-1 aggregation via occupying the P<SUB>i</SUB>-binding site. These findings revealed an unexpected physiological role of tartrate in the maintenance of DJ-1 function, and thus, a potential use as an inhibitor of DJ-1 aggregation.</P>
A novel core 1 O-linked glycan-specific binding lectin from the fruiting body of Hericium erinaceus