Inhibition of ADP‐ribosylation suppresses aberrant accumulation of lipidated apolipoprotein B in the endoplasmic reticulum
Copyright policy )Inhibition of ADP‐ribosylation suppresses aberrant accumulation of lipidated apolipoprotein B in the endoplasmic reticulum
ApoB‐crescent, an endoplasmic reticulum (ER)‐lipid droplet amalgamation structure, is a useful marker to indicate aberrant lipidated apolipoprotein B accumulation in the hepatocyte ER. Blockade of the ER‐to‐Golgi transport by either vesicle transport inhibitors or dominant‐negative Arf1 caused a significant increase in ApoB‐crescents. However, a low concentration of Brefeldin A induced the same result without affecting protein secretion, suggesting ADP‐ribosylation as an additional mechanism. ADP‐ribosylation inhibitors not only suppressed the increase of ApoB‐crescents, but also rapidly dissolved existing ApoB‐crescents. These results implicate the involvement of ADP‐ribosylation in the ApoB‐crescent formation and maintenance process at the ER.
- State University of New York at Potsdam United States
- State University of New York United States
- Tokai National Higher Education and Research System Japan
- SUNY Upstate Medical University United States
- Nagoya University Japan
Adenosine Diphosphate Ribose, Brefeldin A, Lipoylation, Lipid droplet, Hep G2 Cells, Endoplasmic Reticulum, Lipid Metabolism, 3-Iodobenzylguanidine, Protein Transport, ER, ApoB-crescent, Humans, Carrier Proteins, Protein Processing, Post-Translational, ADP-ribosylation, Apolipoproteins B
Adenosine Diphosphate Ribose, Brefeldin A, Lipoylation, Lipid droplet, Hep G2 Cells, Endoplasmic Reticulum, Lipid Metabolism, 3-Iodobenzylguanidine, Protein Transport, ER, ApoB-crescent, Humans, Carrier Proteins, Protein Processing, Post-Translational, ADP-ribosylation, Apolipoproteins B
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