nant lipoproteins generated in both the intestine and liver from the blood. However, Helen Hobbs and colleagues show that mice lacking an adaptor protein (ARH) that associates with the receptor for bad cholesterol (LDL) are better at clearing remnant lipoproteins than mice lacking the LDL receptor (LDLR) itself. This indicates that the LDLR is important for remnant lipoprotein clearance under certain circumstances, but whether clearance is mediated directly or indirectly was not determined. Similarly, humans with a mutation in the gene encoding ARH (who suffer from autosomal recessive hypercholesterolemia) are able to clear remnant lipoproteins from the blood, whereas individuals with mutations in their genes encoding the LDLR (who suffer from familial hypercholesterolemia) are not.
In an accompanying commentary, Robert Mahley and Yadong Huang from the Gladstone Institute of Cardiovascular Disease discuss how these complex studies enhance our understanding of lipid clearance from the body and suggest that heparan sulfate proteoglycans might be "responsible for remnant [lipoprotein] uptake by hepatocytes in the presence of defective LDLR internalization."
TITLE: Liver heparan sulfate proteoglycans mediate clearance of triglyceride-rich lipoproteins independently of LDL receptor family members
AUTHOR CONTACT:
Jeffrey D. Esko
University of California, San Diego, La Jolla, California, USA.
Phone: (858) 822-1100; Fax: (858) 534-5611; E-mail: jesko@ucsd.edu.
Joseph R. Bishop
University of California, San Diego, La Jolla, California, USA.
Phone: (858) 822-1041; Fax: (858) 534-5611; E-mail: bishopr@ucsd.edu.
View the PDF of this article at: https://www.the-jci.org/article.php?id=29154
RELATED MANUSCRIPT
TITLE: Disruption of LD
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Contact: Brooke Grindlinger
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Journal of Clinical Investigation
2-Jan-2007
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