Disease relevance of Apoc2

• Furthermore, the decrease of LPL activity in the heart, along with the inhibitory effects of excess apoC-II, may contribute to the hypertriglyceridemia observed in apoC-II transgenic mice [1].
• Finally, we demonstrate that apolipoprotein C-II in human atheroma co-localizes to regions positive for markers of amyloid and macrophage accumulation [2].

High impact information on Apoc2

• Overexpression of apolipoprotein CII causes hypertriglyceridemia in transgenic mice [3].
• In the present studies, initial attempts to demonstrate cAMP-dependent activation of triglyceride lipase using the 1,000 X g supernatant fraction (S1) of mouse heart homogenate were unsuccessful, presumably due to the masking effects of high levels of lipoprotein lipase activity even when assayed at pH 7.4 and in the absence of apolipoprotein C-II [4].
• Along with plasma apoC-II concentrations, heart and skeletal muscle LPL activities were predictors of plasma TGs [1].
• These data suggest that mice with the human apoC-II transgene may have alterations in the expression/activity of endogenous LPL in the heart [1].
• LPL and its specific physiological activator, apolipoprotein C-II (apoC-II), regulate the hydrolysis of triglycerides (TGs) from circulating TG-rich lipoproteins [1].

Biological context of Apoc2

• Three cDNA clones containing the mouse apolipoprotein C2 (Apoc2) gene were isolated from a mouse liver cDNA library [5].

Anatomical context of Apoc2

• Transcripts for Apoc2 were found in fetal liver, adult liver, intestine, and peritoneal macrophages [5].

Other interactions of Apoc2

• First, we tested whether this distinction is due to additional mutation of the Apoc1 and/or Apoc2 genes in KOR-Apoe(shl) [6].

Analytical, diagnostic and therapeutic context of Apoc2

• The exon-intron structure of the mouse Apoc2 gene was determined by sequence analysis [5].

References