Inefficient membrane targeting, translocation, and proteolytic processing by signal peptidase of a mutant preproparathyroid hormone protein.

@article{Karaplis1995InefficientMT,
  title={Inefficient membrane targeting, translocation, and proteolytic processing by signal peptidase of a mutant preproparathyroid hormone protein.},
  author={Andrew C Karaplis and Soe K. Lim and Hiroko Baba and Andrew O. Arnold and Henry M. Kronenberg},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 4},
  pages={1629-35}
}
A preproparathyroid hormone allele from a patient with familial isolated hypoparathyroidism was shown to have a single point mutation in the hydrophobic core of the signal sequence. This mutation, changing a cysteine to an arginine codon at the -8 position of the signal peptide, was associated with deleterious effects on the processing of preproparathyroid hormone to proparathyroid hormone in vitro. To examine the biochemical consequence(s) of this mutation, proteins produced by cell-free… CONTINUE READING

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