Identification of sites in apolipoprotein A-I susceptible to chymase and carboxypeptidase A digestion

@inproceedings{Usami2012IdentificationOS,
  title={Identification of sites in apolipoprotein A-I susceptible to chymase and carboxypeptidase A digestion},
  author={Yoko Usami and Yukihiro Kobayashi and Takahiro Kameda and Akari Miyazaki and Kazuyuki Matsuda and Mitsutoshi Sugano and Kenji Kawasaki and Yuriko Kurihara and Takeshi Kasama and Minoru Tozuka},
  booktitle={Bioscience reports},
  year={2012}
}
MCs (mast cells) adversely affect atherosclerosis by promoting the progression of lesions and plaque destabilization. MC chymase cleaves apoA-I (apolipoprotein A-I), the main protein component of HDL (high-density lipoprotein). We previously showed that C-terminally truncated apoA-I (cleaved at the carboxyl side of Phe(225)) is present in normal human serum using a newly developed specific mAb (monoclonal antibody). In the present study, we aimed to identify chymase-induced cleavage sites in… CONTINUE READING

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