Disease relevance of APOM

• Leptin inhibits apolipoprotein M transcription and secretion in human hepatoma cell line, HepG2 cells [1].
• Here, we constructed G3A and G7A mutations into the F proteins of SV5 (W3A and WR isolates), Newcastle disease virus (NDV), and human parainfluenza virus type 3 (HPIV3) [2].
• Effects of ischemia-reperfusion injury on apolipoprotein m expression in the liver [3].

Psychiatry related information on APOM

• Exclusion of CYP46 and APOM as candidate genes for Alzheimer's disease in a French population [4].

High impact information on APOM

• Regulation of apolipoprotein M gene expression by MODY3 gene hepatocyte nuclear factor-1alpha: haploinsufficiency is associated with reduced serum apolipoprotein M levels [5].
• ApoM-containing HDL (HDL(apoM+)) contained significantly more free cholesterol than HDL lacking apoM (HDL(apoM-)) (5.9 +/- 0.7% vs. 3.2 +/- 0.5%; P < 0.005) and was heterogeneous in size with both small and large particles [6].
• Proposed lipocalin fold for apolipoprotein M based on bioinformatics and site-directed mutagenesis [7].
• With this background, we tested the potential association of the CYP46, APOM and APOF genes with the risk of developing AD [4].
• We also searched for polymorphisms within the APOM and APOF by dHPLC [4].

Biological context of APOM

• Single nucleotide polymorphisms in the proximal promoter region of apolipoprotein M gene (apoM) confer the susceptibility to development of type 2 diabetes in Han Chinese [8].
• Down-regulation of apolipoprotein M expression is mediated by phosphatidylinositol 3-kinase in HepG2 cells [9].

Anatomical context of APOM

• Recent studies have demonstrated that apolipoprotein M (apoM) is important for the formation of prebeta-high-density lipoprotein (HDL) and cholesterol (CHO) efflux in macrophages to HDL [8].

Associations of APOM with chemical compounds

• Correlation of apolipoprotein M with leptin and cholesterol in normal and obese subjects [10].

Analytical, diagnostic and therapeutic context of APOM

• Specific tissue expression and cellular localization of human apolipoprotein M as determined by in situ hybridization [11].
• We treated LDL proteins with N-glycosidase or neuraminidase, studied mobility shifts of Apo M by two-dimensional gel electrophoresis, and different isoforms were then identified with mass spectrometry [12].

References