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A Regulator of Secretory Vesicle Size, Kelch-Like Protein 12, Facilitates the Secretion of Apolipoprotein B100 and Very-Low-Density Lipoproteins—Brief Report
Author(s) -
Chutikarn Butkinaree,
Liang Guo,
Bhama Ramkhelawon,
Amarylis Wanschel,
Jeffrey L. Brodsky,
Kathryn J. Moore,
Edward A. Fisher
Publication year - 2013
Publication title -
arteriosclerosis thrombosis and vascular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.007
H-Index - 270
eISSN - 1524-4636
pISSN - 1079-5642
DOI - 10.1161/atvbaha.113.302728
Subject(s) - very low density lipoprotein , apolipoprotein b , endoplasmic reticulum , secretion , microbiology and biotechnology , golgi apparatus , lipoprotein , gene knockdown , microsomal triglyceride transfer protein , chemistry , unfolded protein response , biology , biochemistry , cholesterol , apoptosis
One of the major risk factors for atherosclerosis is the plasma level of low-density lipoprotein (LDL), which is a product of very-low-density lipoprotein (VLDL). Hepatic apolipoprotein B100 (apoB100) is the essential component that provides structural stability to VLDL particles. Newly translated apoB100 is partially lipidated in the endoplasmic reticulum (ER), forming nascent apoB100-VLDL particles. These particles are further modified to form fully mature VLDLs in the Golgi apparatus. Therefore, the transport of nascent VLDL from the ER to the Golgi represents a critical step during VLDL maturation and secretion and in regulating serum LDL cholesterol levels. Our previous studies showed that apoB100 exits the ER in coat complex II vesicles (COPII), but the cohort of related factors that control trafficking is poorly defined.

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