ApoAI, a major protein component of HDL is considered to be a key
factor which contributes for HDL’s cardio- protective functions. ApoAI is
sensitive to myeloperoxidase mediated oxidative modifications under chronic
inflammatory conditions such as atherosclerosis. The amino acid tyrosine at
position 192 of ApoAI is considered to be one of the vulnerable sites for oxidation
which impairs HDL functions and its quality. The presence of oxidized ApoAI in
plasma may serve as a useful indicator of CVD risks in humans, but its detection
in the clinical settings requires monoclonal antibodies (mAbs) with high
specificity. In this study, we have developed mAbs against chloro- tyrosine at
position 192 of ApoAI. We designed a small synthetic peptide of 7 amino acids
length containing modified tyrosine residue (189-LAE-3-Cl-Y-HAK-195) based on antigenicity
prediction. We coupled this peptide to Keyhole Limpet Hemocyanin (KLH) for generating mAbs.
Hybridoma clones, KLH-ApoAI-F2 and KLH-ApoAI-H9, were found to be highly specific to
chloro-192Tyr containing peptide of ApoAI and not to either nitro-192Tyr containing or to chloro-166Tyr and nitro-166Tyr containing peptides of ApoAI. The utility of these mAbs for screening the
quality of HDL as an indicator of CVD risks in humans is discussed.
Keywords: Atherosclerosis, High Density Lipoprotein (HDL), Apolipoprotein AI, Oxidized Apolipoprotein AI, Chlorinated
192Tyrosine ApoAI, Myeloperoxidase.
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