Biosynthesis and intracellular post-translational processing of normal and mutant platelet glycoprotein GPIb-IX.

doi:10.1042/0264-6021:3580295

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Article

Biosynthesis and intracellular post-translational processing of normal and mutant platelet glycoprotein GPIb-IX.

The Biochemical journal - 1 Sept 2001

Ulsemer P, Strassel C, Baas M J, Salamero J, Chasserot-Golaz S, Cazenave J P, De La Salle C, Lanza F

Abstract excerpt

The multisubunit leucine-rich glycoprotein (GP) Ib-IX-V complex mediates von Willebrand factor-dependent platelet adhesion at sites of blood-vessel injury. Molecular defects of this receptor are reported to cause the Bernard-Soulier haemorrhagic disorder. To gain insight into the mechanisms controlling expression of normal and defective receptors, we performed pulse-chase metabolic studies and detailed analysis...

Topics

Animals
CHO Cells
Carbohydrate Metabolism
Cell Membrane
Cricetinae
Cytoplasm
Endoplasmic Reticulum
Glycosylation
Golgi Apparatus
Kinetics
Leucine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Microscopy, Confocal

Mutation

Platelet Glycoprotein GPIb-IX Complex

Protein Processing, Post-Translational

Protein Subunits

Protein Transport

Source

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Identifiers

PMID: 11513727
DOI: 10.1042/0264-6021:3580295
PMCID: PMC1222061

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Biosynthesis and intracellular post-translational processing of normal and mutant platelet glycoprotein GPIb-IX.PMID 11513727Read ↗

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