描述：
Angiopoietin-like 3 (ANGPTL3) is a secreted glycoprotein that is structurally related to the
angiopoietins. Mature mouse ANGPTL3 contains an N-terminal coiledcoil domain and a
C-terminal fibrinogen-like domain. ANGPTL3 is expressed in the liver from early in development
through adulthood. Full length ANGPTL3 circulates in the plasma as do the proteolytically
separated N-and C-terminal fragments containing the coiled-coil domain and fibrinogen-like
domains, respectively. ANGPTL3 is found as 70 kDa, 50 kDa, and 32 kDa species and can form
weakly associated noncovalent multimers in vitro. ANGPTL3 directly inhibits lipoprotein lipase
(LPL), an enzyme responsible for hydrolyzing circulating triglycerides. This activity requires a
putative heparinbinding motif that is N-terminal to the coiledcoil domain. Proteolytic removal
of the fibrinogenlike domain from the N-terminal fragment serves to activate ANGPTL3 and
increase its ability to inhibit LPL in vitro and function in vivo. ANGPTL3 promotes an increase in
circulating triglyceride levels without altering VLDL or HDL secretion or uptake. ANGPTL3
knockout mice are hypolipidemic and have elevated LPL activity. ANGPTL3 expression in vivo
is upregulated by LXR agonists and downregulated by insulin, leptin, and TRβ agonists.
Dysregulated ANGPTL3 expression and elevated plasma triglyceride levels are characteristic
of some strains of obese and diabetic mice. ANGPTL3 does not bind Tie-1 or Tie-2 but its
fibrinogenlike domain interacts with integrin αVβ3 to induce endothelial cell adhesion,
migration, and neovascularization. ANGPTL3, secreted by fetal liver cells, also promotes the
expansion of hematopoietic stem cells. Mature mouse ANGPTL3 shares 22% 30% amino acid
(aa) sequence identity with ANGPTL1, 2, 4, 6, and 7. It shares 77% aa sequence identity with
human ANGPTL3.
原厂资料：
Angiopoietin-like 3 (ANGPTL3) is a secreted glycoprotein that is structurally related to the
angiopoietins. Mature mouse ANGPTL3 contains an N-terminal coiledcoil domain and a
C-terminal fibrinogen-like domain. ANGPTL3 is expressed in the liver from early in development
through adulthood. Full length ANGPTL3 circulates in the plasma as do the proteolytically
separated N-and C-terminal fragments containing the coiled-coil domain and fibrinogen-like
domains, respectively. ANGPTL3 is found as 70 kDa, 50 kDa, and 32 kDa species and can form
weakly associated noncovalent multimers in vitro. ANGPTL3 directly inhibits lipoprotein lipase
(LPL), an enzyme responsible for hydrolyzing circulating triglycerides. This activity requires a
putative heparinbinding motif that is N-terminal to the coiledcoil domain. Proteolytic removal
of the fibrinogenlike domain from the N-terminal fragment serves to activate ANGPTL3 and
increase its ability to inhibit LPL in vitro and function in vivo. ANGPTL3 promotes an increase in
circulating triglyceride levels without altering VLDL or HDL secretion or uptake. ANGPTL3
knockout mice are hypolipidemic and have elevated LPL activity. ANGPTL3 expression in vivo
is upregulated by LXR agonists and downregulated by insulin, leptin, and TRβ agonists.
Dysregulated ANGPTL3 expression and elevated plasma triglyceride levels are characteristic
of some strains of obese and diabetic mice. ANGPTL3 does not bind Tie-1 or Tie-2 but its
fibrinogenlike domain interacts with integrin αVβ3 to induce endothelial cell adhesion,
migration, and neovascularization. ANGPTL3, secreted by fetal liver cells, also promotes the
expansion of hematopoietic stem cells. Mature mouse ANGPTL3 shares 22% 30% amino acid
(aa) sequence identity with ANGPTL1, 2, 4, 6, and 7. It shares 77% aa sequence identity with
human ANGPTL3.
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