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

@article{Nauseef1995CalreticulinFA,
  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},
  year={1995},
  volume={270 9},
  pages={4741-7}
}
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

Citations

Publications citing this paper.
Showing 1-10 of 68 extracted citations

Differential Modulation of SERCA2 Isoforms by Calreticulin

The Journal of cell biology • 1998
View 4 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…