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

Journal of Lipid Research

Ji-Young Cha¹  Joyce J. Repa¹  Christopher Harp¹  Xinxin Yu²  Harini Gopal²  Hongfei Ge²  Cai Li² 

[1] Department of Physiology, The University of Texas Southwestern Medical Center, Dallas, TX 75390-8854;Touchstone Center for Diabetes Research, The University of Texas Southwestern Medical Center, Dallas, TX 75390-8854;

关键词: Angptl3;    Angptl4;    LPL;    peroxisome proliferator-activated receptor;    liver X receptor;    gel filtration;   

DOI  :  

来源: DOAJ

【 摘 要 】

Angiopoietin-like protein 3 and 4 (Angptl3 and Angptl4) are two members of the angiopoietin-like family of proteins. These two closely related proteins have been reported to similarly affect lipid metabolism through their capacity to inhibit lipoprotein lipase. We undertook a series of studies to compare the structure, function, and regulation of Angptl3 and Angptl4. Previously, we reported that Angptl4 exists as variable-sized oligomers that contain intermolecular disulfide bonds. We now have evidence that although 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 the liver. Treatments with various ligands of nuclear receptors reveal that Angptl3 is a target gene of liver X receptor, while Angptl4 expression is activated by ligands of all peroxisome proliferator-activated receptors. 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 Angptl4 by sites of expression, nutritional status, and ligands of nuclear receptors may confer unique roles of each in lipoprotein metabolism.

【 授权许可】

Unknown