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A more recent version of this article appeared on July 1, 2005

Papers In Press, published online ahead of print May 1, 2005
J. Lipid Res., doi:10.1194/jlr.M500005-JLR200
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Submitted on January 6, 2005
Revised on April 19, 2005
Accepted on April 21, 2005

Differential regulation and properties of angiopoietin-like proteins 3 and -4

Hongfei Ge, Ji-Young Cha, Harini Gopal, Christopher Harp, Xinxin Yu, Joyce J. Repa, and Cai Li

Metabolic Disorders, Merck Research Laboratories, Rahway, NJ 07065

Corresponding Author: cai_li{at}merck.com

Angiopoietin-like protein 3 and –4 (Angptl3 and –4) are two members of the angiopoietin-like family of proteins. These two closely related proteins have been reported to similarly affect lipid metabolism by their capacity to inhibit lipoprotein lipase. We undertook a series of studies to compare the structure, function, and regulation of Angptl3 and –4. Previously, we reported that Angptl4 exists as variable sized oligomers that contain intermolecular disulfide bonds. We now present evidence that while there are no intermolecular disulfide bonds evident in Angptl3, higher molecular weight forms do exist. In addition, Angptl4 exhibits a widespread distribution of tissue expression, while Angptl3 is exclusively expressed in liver. Treatments with various ligands of nuclear receptors reveal that Angptl3 is a target gene of liver X receptor (LXR), while Angptl4 expression is activated by ligands of all peroxisome proliferator-activated receptors (PPARs). Expression of Angptl4 in adipose tissue and liver is induced by fasting, while Angptl3 expression is not appreciably affected by nutritional status. We suggest that the differential regulation of Angptl3 and –4 by sites of expression, nutritional status, and ligands of nuclear receptors may confer unique roles of each in lipoprotein metabolism.


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