Key result
10C3 monoclonal antibody targets the LPL heparin binding site without inhibiting catalytic activity.
The development of the 10C3 monoclonal antibody provides a novel immunochemical tool for investigating the metabolism of triglyceride-rich lipoproteins and the functional anatomy of lipoprotein lipase.
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10C3 provides a selective preclinical tool for LPL domain studies; leaves open translation to human triglyceride metabolism research.
A fragment of the human lipoprotein lipase (LPL) cDNA (405 bp, 5' terminal end) was cloned in an expression vector to produce a approximately 17 kDa fusion peptide and was used as antigen to produce a high titre anti-LPL monoclonal antibody (10C3 MAb). This antibody reacts with both native and denatured forms of LPL from different tissue and animal sources. Competition studies with heparin indicate that 10C3 MAb is specific for an epitope at a heparin binding site. The antibody does not inhibit LPL enzyme activity, indicating that the antigenic epitope is not situated within or in the proximity of the LPL catalytic region. With these characteristics, 10C3 MAb should prove to be a useful immunochemical tool in clinical as well as in fundamental investigations on the metabolism of triglyceride-rich lipoproteins and in studies on the functional anatomy of LPL.
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Cadelis et al. (1996) studied this question. 10C3 MAb (anti-LPL monoclonal antibody) was evaluated on Antibody specificity and effect on LPL enzyme activity. The 10C3 monoclonal antibody against human lipoprotein lipase specifically targets a heparin binding site without inhibiting the enzyme's catalytic activity.
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