Article
Competition between normal [674C] and mutant [674R] subunits: role of the molecular chaperone BiP in the processing of GPIIb-IIIa complexes.
Blood - 1 May 2001
Arias-Salgado E G, Butta N, González-Manchón C, Larrucea S, Ayuso M S, Parrilla R
Abstract excerpt
This work aimed at investigating the function of the [C674R] mutation in GPIIb that disrupts the intramolecular 674 to 687 disulfide bridge. Individuals heterozygous for this mutation show a platelet GPIIb-IIIa content approximately 30% of normal controls, which is less than expected from one normal functioning allele. Coexpression of normal [674C]GPIIb and mutant [674R]GPIIb with normal GPIIIa produced a...
Topics
- Animals
- CHO Cells
- Carrier Proteins
- Cricetinae
- Endoplasmic Reticulum Chaperone BiP
- Heat-Shock Proteins
- Humans
- Molecular Chaperones
- Mutation
- Platelet Activation
- Platelet Glycoprotein GPIIb-IIIa Complex
- Signal Transduction
- Structure-Activity Relationship