VLDL binds APOC1 and APOC4

Stable Identifier
R-HSA-8866321
Type
Reaction [binding]
Species
Homo sapiens
Compartment
extracellular region
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VLDL binds APOC1 and APOC4
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Newly formed very low-density lipoprotein (VLDL) released from the liver can acquire lipoproteins in the circulation. Apolipoprotein C-I (APOC1) is a 6.6 kDa apolipoprotein that is synthesised mainly in the liver but also in other tissues. It is a constituent of triglyceride-rich lipoproteins (around 10% of the protein of VLDLs and 2% of HDLs) that slow the circulatory clearance of triglyceride-rich lipoproteins by a variety of mechanisms. As well as binding and inhibiting triglyceride-rich lipoprotein uptake by the very low-density lipoprotein receptor (VLDLR), it can also binds free fatty acids (FAs) in the circulation, reducing their uptake by cells (Shachter 2001, Hansen et al. 2011). A minor constituent of VLDL is apolipoprotein IV (APO4) (Kotite et al. 2003).

Literature References
PubMed ID Title Journal Year
11353333 Apolipoproteins C-I and C-III as important modulators of lipoprotein metabolism

Shachter, NS

Curr. Opin. Lipidol. 2001
12700345 Human apoC-IV: isolation, characterization, and immunochemical quantification in plasma and plasma lipoproteins

Kotite, L, Zhang, LH, Yu, Z, Burlingame, AL, Havel, RJ

J. Lipid Res. 2003
21776394 The apolipoprotein C-I content of very-low-density lipoproteins is associated with fasting triglycerides, postprandial lipemia, and carotid atherosclerosis

Hansen, JB, Fernández, JA, Notø, AT, Deguchi, H, Björkegren, J, Mathiesen, EB

J Lipids 2011
Participants
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Output
Participant Of
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Orthologous Events
VLDL binds APOC1 and APOC4 (Canis familiaris)
VLDL binds APOC1 and APOC4 (Mus musculus)
VLDL binds APOC1 and APOC4 (Rattus norvegicus)
Authored
Jassal, B  (2016-03-30)
Reviewed
D'Eustachio, P  (2016-04-05)
Created
Jassal, B  (2016-03-30)