Identification of domains in apoA-I susceptible to proteolysis by mast cell chymase. Implications for HDL function.

@article{Lee2000IdentificationOD,
  title={Identification of domains in apoA-I susceptible to proteolysis by mast cell chymase. Implications for HDL function.},
  author={Miriam Lee and Patrizia Uboldi and D. Lo Giudice and Alberico L. Catapano and Petri T. Kovanen},
  journal={Journal of lipid research},
  year={2000},
  volume={41 6},
  pages={975-84}
}
When stimulated, rat serosal mast cells degranulate and secrete a cytoplasmic neutral protease, chymase. We studied the fragmentation of apolipoprotein (apo) A-I during proteolysis of HDL(3) by chymase, and examined how chymase-dependent proteolysis interfered with the binding of eight murine monoclonal antibodies (Mabs) against functional domains of apoA-I. Size exclusion chromatography of HDL(3) revealed that proteolysis for up to 24 h did not alter the integrity of the alpha-migrating HDL… CONTINUE READING