Apolipoprotein B Secretion Assay from Primary Hepatocytes
Yawei WANG,
Xin LI,
Runze HUANG,
Xiao- Chen,
Xiao Wang
Affiliations
Yawei WANG
State Key Laboratory of Membrane Biology, Peking University, Beijing, ChinaPKU-THU Joint Center for Life Sciences, Peking University, Beijing, China
Xin LI
State Key Laboratory of Membrane Biology, Peking University, Beijing, ChinaCollege of Future Technology, Institute of Molecular Medicine, Peking University, Beijing, China
Runze HUANG
State Key Laboratory of Membrane Biology, Peking University, Beijing, ChinaCollege of Future Technology, Institute of Molecular Medicine, Peking University, Beijing, China
Xiao- Chen
State Key Laboratory of Membrane Biology, Peking University, Beijing, ChinaPKU-THU Joint Center for Life Sciences, Peking University, Beijing, China, College of Future Technology, Institute of Molecular Medicine, Peking University, Beijing, China
Xiao Wang
State Key Laboratory of Membrane Biology, Peking University, Beijing, ChinaPKU-THU Joint Center for Life Sciences, Peking University, Beijing, China, College of Future Technology, Institute of Molecular Medicine, Peking University, Beijing, China
Apolipoprotein B (APOB) is the primary structural protein of atherogenic lipoproteins, which drive atherogenesis and thereby lead to deadly cardiovascular diseases (CVDs). Plasma levels of APOB-containing lipoproteins are tightly modulated by LDL receptor–mediated endocytic trafficking and cargo receptor–initiated exocytic route; the latter is much less well understood. This protocol aims to present an uncomplicated yet effective method for detecting APOB/lipoprotein secretion. We perform primary mouse hepatocyte isolation and culture coupled with well-established techniques such as immunoblotting for highly sensitive, specific, and semi-quantitative analysis of the lipoprotein secretion process. Its inherent simplicity facilitates ease of operation, rendering it a valuable tool widely utilized to explore the intricate landscape of cellular lipid metabolism and unravel the mechanistic complexities underlying lipoprotein-related diseases.
