Effects of PRELI in Oxidative-Stressed HepG2 Cells.
Protein of relevant evolutionary and lymphoid interest (PRELI) is known for preventing apoptosis by mediating intramitochondrial transport of phosphatidic acid. However, the role of PRELI remains unclear. This study has demonstrated functions of PRELI through PRELI-knockdown in hepatocellular carcinoma (HepG2) cells exposed to oxidative stress by hydrogen peroxide. Results show that PRELI has three functions in HepG2 cells with regard to oxidative stress. First, PRELI affects expressional regulation of SOD-1 and caspase-3 genes in HepG2 cells. PRELI knockdown HepG2 cells have shown up-regulation of caspase-3 and down-regulation of SOD-1. Second, PRELI suppresses mitochondrial apoptosis in HepG2 cells. Fluorescence intensity related to mitochondrial apoptosis in PRELI-knockdown HepG2 cells increased more than two-fold compared to normal HepG2 cells. Third, PRELI suppresses senescence of HepG2 cells with oxidative stress. PRELI knockdown HepG2 cells showed higher levels of senescence than normal HepG2 cells. These results suggest that PRELI is a crucial protein in the suppression of apoptosis in HepG2 cells in response to oxidative stress.
School of Life Sciences and Biotechnology, Korea University, South Korea.
Bo Yong
BY
Kim
Department of Clinical Laboratory Sciences, College of Health Science, Korea University, South Korea.
Min Ho
MH
Cho
Department of Clinical Laboratory Sciences, College of Health Science, Korea University, South Korea.
Kyung Joo
KJ
Kim
Department of Clinical Laboratory Sciences, College of Health Science, Korea University, South Korea.
Kyung Jin
KJ
Cho
Department of Clinical Laboratory Sciences, College of Health Science, Korea University, South Korea.
Suhng Wook
SW
Kim
Department of Biomedical Laboratory Science, College of Health Science, Jungwon University, Chungbuk, South Korea.
Hyun Sook
HS
Kim
Department of Biomedical Laboratory Science, College of Health Science, Cheongju University, Chungbuk, South Korea.
Woon-Won
WW
Jung
Department of Laboratory Medicine, Kangwon National University School of Medicine, Chuncheon, Kangwondo, South Korea.
Boo Hyung
BH
Lee
School of Life Sciences and Biotechnology, Korea University, South Korea.
Bong Hee
BH
Lee
Department of Clinical Laboratory Sciences, College of Health Science, Korea University, South Korea seunggwan@korea.ac.kr.
Seung Gwan
SG
Lee
D048868:Adaptor Proteins, Signal Transducing / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D017209:Apoptosis / Q000187:drug effects / Q000235:genetics; D002277:Carcinoma / Q000473:pathology; D053148:Caspase 3 / Q000235:genetics / Q000378:metabolism; D045744:Cell Line, Tumor; D015972:Gene Expression Regulation, Neoplastic / Q000187:drug effects / Q000235:genetics / Q000502:physiology*; D049452:Green Fluorescent Proteins / Q000235:genetics / Q000378:metabolism; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D018384:Oxidative Stress / Q000187:drug effects* / Q000502:physiology*; D034741:RNA, Small Interfering / Q000235:genetics / Q000378:metabolism; D017382:Reactive Oxygen Species / Q000378:metabolism; D013482:Superoxide Dismutase / Q000235:genetics / Q000378:metabolism; D000072105:Superoxide Dismutase-1; D014162:Transfection; D001616:beta-Galactosidase / Q000378:metabolism
C493340:APBB1IP protein, human; D048868:Adaptor Proteins, Signal Transducing; D008565:Membrane Proteins; D034741:RNA, Small Interfering; D017382:Reactive Oxygen Species; C000606290:SOD1 protein, human; D049452:Green Fluorescent Proteins; D006861:Hydrogen Peroxide; D013482:Superoxide Dismutase; D000072105:Superoxide Dismutase-1; D001616:beta-Galactosidase; D053148:Caspase 3
HepG2 cell; PRELI; oxidative stress; reactive oxygen species; shRNA; transfection