Disease relevance of APOL3

• Absorption with normal adult and fetal brain homogenate did not modify the binding capacity of BF7 and GE2 for glioma cells, while the binding of CG12 antibodies was abolished [1].
• ApoLp-III from Galleria mellonella was incubated with LPS from Escherichia coli O55:B5, and analyzed by non-denaturing polyacrylamide gel electrophoresis (PAGE) [2].
• The anti-glioma Mabs BF7 and GE2 reacted preferentially with gliomas, while the anti-glioma Mab CG12 reacted with gliomas, melanomas, neuroblastomas and medulloblastomas [3].

High impact information on APOL3

• CG12_1 (apolipoprotein-L like) was specifically expressed in endothelial cells lining the normal and atherosclerotic iliac artery and aorta [4].
• ApoLp-III binds with high affinity (Kd = 1.9 X 10(-7)M) to both phosphatidylcholine- and diacylglycerol-coated polystyrene beads [5].
• ApoLp-III joins apolipoproteins E and J (clusterin, sulfated glycoprotein-2) as a group of proteins that function in both lipid transfer and cell death [6].
• In CG12, despite the presence of runs of A-T pairs, CpG presents a high twist of 43 degrees and a sugar phase at the guanine of about 180 degrees, previously observed in other ACGT-containing-oligomers [7].
• Indirect immunofluorescence and flow cytofluorometry revealed a heterogeneous distribution of surface GE 2 and CG 12 tumor-associated antigens (TAA's): three cell lines were positive (greater than 69% TAA-positive cells) and three cell lines were negative (less than 9% TAA-positive cells) [8].

Anatomical context of APOL3

• ApoLp-III is a 18 kDa protein that normally exists as a water-soluble monomeric hemolymph protein [9].
• CG12, the third monoclonal antibody, binds to the great majority of tumor cell lines of neuroectodermal origin and does not bind to any other cell lines tested [10].

Associations of APOL3 with chemical compounds

• ApoLp-III isolated from hemolymph of Lethocerus medius had a M(r) = 19,000 and an amino acid composition high in methionine, in comparison with other apoLp-IIIs [11].
• ApoLp-III degradation by protease IV was inhibited by 1 mM TLCK but not 1 mM EDTA, additionally demonstrating that digestion was catalysed by a serine protease [12].

Analytical, diagnostic and therapeutic context of APOL3

• Indirect immunofluorescence and flow cytofluorimetry revealed a heterogeneous distribution of surface GE 2 and CG 12 Tumour Associated Antigens (TAA) [13].

References