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Regulation of ApoB Secretion by the Low Density Lipoprotein Receptor Requires Exit from the Endoplasmic Reticulum and
 

Summary: Regulation of ApoB Secretion by the Low Density Lipoprotein
Receptor Requires Exit from the Endoplasmic Reticulum and
Interaction with ApoE or ApoB*S
Received for publication,December 22, 2007, and in revised form, February 5, 2008 Published, JBC Papers in Press,February 13, 2008, DOI 10.1074/jbc.M710457200
Daniel A. Blasiole1
, Angie T. Oler, and Alan D. Attie2
From the Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706
Apolipoprotein B (apoB) is required for the hepatic assembly
and secretion of very low density lipoprotein (VLDL). The
LDL receptor (LDLR) promotes post-translational degrada-
tion of apoB and thereby reduces VLDL particle secretion.
We investigated the trafficking pathways and ligand require-
ments for the LDLR to promote degradation of apoB. We first
tested whether the LDLR drives apoB degradation in an endo-
plasmic reticulum (ER)-associated pathway. Primary mouse
hepatocytes harboring an ethyl-nitrosourea-induced, ER-re-
tained mutant LDLR secreted comparable levels of apoB with
LDLR-null hepatocytes, despite reduced secretion from cells
expressing the wild-type LDLR. Additionally, treatment of
cells with brefeldin A inhibited LDLR-dependent degrada-

  

Source: Attie, Alan D. - Department of Biochemistry, University of Wisconsin at Madison

 

Collections: Biology and Medicine