2006年4月20日 · In this article, we demonstrate that an increase in ADRP promotes the storage of triglycerides in cytosolic lipid droplets and inhibit their secretion as VLDL. Conversely, a knockdown of ADRP decreases the storage of triglycerides but channels the fatty acids mainly to …

VLDL stimulation of FAO hepatoma cells infected with Ad-HL significantly increased ADRP mRNA levels in a VLDL concentration-dependent manner (Fig. 4A). HL hydrolysis of VLDL also increased expression of angiopoietin like protein-4 (ANGPLT4) and pyruvate dehydrogenase kinase 4 (PDK4), two known PPARδ-regulated genes with important roles in ...

2006年1月1日 · Cells treated with VLDL contained three times the amount of ADRP as cells incubated without lipoproteins, whereas incubation of the cells with AcLDL increased the amount of ADRP by only 50%.

Addition of triacsin C, a potent inhibitor of acyl-CoA synthase, for 6 h decreased the amount of TG in VLDL-induced foam cells and oleic acid-treated liver cells; it decreased the amount of ADRP protein in parallel, indicating the amount of ADRP reduced during …

An increase in ADRP prevents the formation of VLDL by diverting fatty acids from the VLDL assembly pathway into cytosolic triglycerides, whereas a decrease of the protein increases the sorting of fatty acids to -oxidation and promotes the secretion of apoB-48 VLDL1.

我们还提出,脂滴有可能直接为VLDL的脂化提供脂肪来源.Cideb和ADRP有可能通过调节脂滴中的脂肪向其他脂滴或者VLDL的流动,转运来调控脂滴的大小和VLDL的脂化成熟程度.

特异性的沉默肝脏ADRP的表达能够减少肝脏脂肪（TAG）的积累，增强VLDL-TG的分泌，并且增加Golgi体中成熟的、TAG含量丰富的VLDL的积累。 过表达ADRP有相反的效果。 并且，ADRP也能调节脂滴的大小。 沉默肝脏中ADRP的表达能够使肝细胞中的脂滴变大。 这些数据表明，Cideb主要在Golgi体中发挥功能，能够促进VLDL在Golgi体中的脂化成熟。 ADRP则能够抑制VLDL在Golgi体中的脂化成熟，从而使肝脏脂肪的分泌减少。 Cideb使脂滴变大，ADRP阻碍 …

Extended further, VLDL stimulation of HL-expressing HUVECs and FAO hepatoma cells increased mRNA expression of canonical PPARδ target genes, including adipocyte differentiation related protein (ADRP), angiopoietin like protein 4 and pyruvate dehydrogenase kinase-4.

Treatment of WT macrophages with VLDL results in triglyceride accumulation and the induction of adipose differentiation-related protein (ADRP). Remarkably, disruption of the PPARδ gene in macrophages completely abolishes this transcriptional response to native VLDL.

An increase in ADRP prevents the formation of VLDL by diverting fatty acids from the VLDL assembly pathway into cytosolic triglycerides, whereas a decrease of the protein increases the sorting of fatty acids to beta-oxidation and promotes the secretion of apoB-48 VLDL1.