Choline and Ethanolamine Plasmalogens Prevent Lead-Induced Cytotoxicity and Lipid Oxidation in HepG2 Cells

Yue Wu; Zhen Chen; Wageh S. Darwish; Koh Terada; Hitoshi Chiba; Shu-Ping Hui

doi:10.1021/acs.jafc.9b02485

Choline and Ethanolamine Plasmalogens Prevent Lead-Induced Cytotoxicity and Lipid Oxidation in HepG2 Cells

Journal of Agricultural and Food Chemistry ◽

10.1021/acs.jafc.9b02485 ◽

2019 ◽

Vol 67 (27) ◽

pp. 7716-7725 ◽

Cited By ~ 9

Author(s):

Yue Wu ◽

Zhen Chen ◽

Wageh S. Darwish ◽

Koh Terada ◽

Hitoshi Chiba ◽

...

Keyword(s):

Lipid Oxidation ◽

Hepg2 Cells ◽

Ethanolamine Plasmalogens

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Phytochemical constituents of Opuntia ficus-indica var. saboten Makino and their hepatoprotective effects against tert-butylhydroperoxide-induced cytotoxicity in human HepG2 cells

Planta Medica ◽

10.1055/s-0028-1084357 ◽

2008 ◽

Vol 74 (09) ◽

Author(s):

YS Lee ◽

HJ Kim ◽

SY Jung ◽

C Jin

Keyword(s):

Hepg2 Cells ◽

Opuntia Ficus Indica ◽

Tert Butylhydroperoxide ◽

Phytochemical Constituents ◽

Hepatoprotective Effects

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Linalool Effect on HepG2 cells: Structure Function Relation

Planta Medica ◽

10.1055/s-0031-1282506 ◽

2011 ◽

Vol 77 (12) ◽

Author(s):

J Usta ◽

K Racha ◽

K Boushra ◽

S Shatha ◽

B Yolla ◽

...

Keyword(s):

Structure Function ◽

Hepg2 Cells ◽

Function Relation

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Transcriptome analysis in HepG2 cells revealed multiple activity mechanisms of a Tibetan polyherbal formula

Zeitschrift für Phytotherapie ◽

10.1055/s-0032-1313243 ◽

2012 ◽

Vol 33 (S 01) ◽

Author(s):

K Becker ◽

A Klein ◽

OA Wrulich ◽

P Gruber ◽

D Fuchs ◽

...

Keyword(s):

Transcriptome Analysis ◽

Hepg2 Cells

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Impact of soluble Endoglin on TGF-β1 mediated immediate early responses in HepG2 cells

Zeitschrift für Gastroenterologie ◽

10.1055/s-0033-1360867 ◽

2014 ◽

Vol 52 (01) ◽

Author(s):

M Neß ◽

SK Meurer ◽

E Borkham-Kamphorst ◽

R Weiskirchen

Keyword(s):

Hepg2 Cells ◽

Immediate Early ◽

Soluble Endoglin ◽

Tgf Β1

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The Effects of Vitamin K1 and Warfarin on Prothrombin Expression in Human Hepatoblastoma (HepG2) Cells

Thrombosis and Haemostasis ◽

10.1055/s-0038-1656315 ◽

1992 ◽

Vol 68 (01) ◽

pp. 040-047 ◽

Cited By ~ 3

Author(s):

C Scott Jamison ◽

Bryan F Burkey ◽

Sandra J Friezner Degen

Keyword(s):

Total Protein ◽

Hepg2 Cells ◽

Enzyme Linked Immunosorbent Assay ◽

Response Analysis ◽

Secreted Protein ◽

Mrna Levels ◽

Vitamin K1 ◽

Maximal Increase ◽

Protein Levels ◽

Warfarin Treatment

SummaryCultures of human hepatoblastoma (HepG2) cells were treated with vitamin K1 or warfarin and prothrombin antigen and mRNA levels were determined. With 3 and 6 h of 10 µg vitamin K1 treatment secreted prothrombin antigen levels, relative to total secreted protein levels, were increased 1.5-fold and 2.1-fold, respectively, over ethanol-treated control levels as determined by an enzyme-linked immunosorbent assay. Dose-response analysis with 3 h of 25 µg/ml vitamin K1 treatment demonstrated a maximal increase of 2.0-fold in secreted prothrombin antigen levels, relative to total secreted protein levels, over ethanol-treated control levels. Pulse-chase analysis with 35S-methionine and immunoprecipitation of 35S-labelled prothrombin demonstrated that, with vitamin K1 treatment (25 µg/ml, 3 h), the rate of prothrombin secretion increased approximately 2-fold and the total amount (intra- and extracellular) of prothrombin synthesized increased approximately 50% over ethanol-treated control levels. Warfarin treatment (1, 5, or 10 µg/ml, 24 h) resulted in decreases in secreted prothrombin antigen levels, relative to total protein levels to approximately 85%, 87% or 81% of ethanol-treated control levels. Analysis of total RNA isolated from these cultures by Northern and solution hybridization techniques demonstrated that prothrombin mRNA was approximately 2.1 kb and that neither vitamin K1 nor warfarin treatment affected the quantity of prothrombin mRNA (ranging from 240–350 prothrombin mRNA molecules per cell). These results demonstrate that vitamin K1 and warfarin, in addition to effects on γ-carboxylation, affect prothrombin synthesis post-transcriptionally, perhaps influencing translation, post-translational processing and/or secretion mechanisms.

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