Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase.

  title={Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase.},
  author={William M Nauseef and Sara J. McCormick and Robert A. Clark},
  journal={The Journal of biological chemistry},
  volume={270 9},
Myeloperoxidase (MPO), a lysosomal heme protein found exclusively in neutrophils and monocytes, is necessary for efficient oxygen-dependent microbicidal activity. Acquisition of heme by the heme-free MPO precursor apopro-MPO appears to be a prerequisite for its subsequent proteolytic processing and advancement along the biosynthetic pathway to mature MPO. We present data indicating that calreticulin (CRT), a high capacity calcium-binding protein residing in the lumen of the endoplasmic… CONTINUE READING


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