Article
Inefficient membrane targeting, translocation, and proteolytic processing by signal peptidase of a mutant preproparathyroid hormone protein.
The Journal of biological chemistry - 27 Jan 1995
Karaplis A C, Lim S K, Baba H, Arnold A, Kronenberg H M
Abstract excerpt
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...
Topics
- Alleles
- Amino Acid Sequence
- Animals
- Cell Membrane
- Endopeptidases
- Glycosylation
- Humans
- Hypoparathyroidism
- Membrane Proteins
- Molecular Sequence Data
- Parathyroid Hormone