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Glycoprotein Ib

GPIbbeta
Platelet glycoprotein Ib (GPIb) is a heterodimeric transmembrane protein consisting of a disulfide-linked 140 kD alpha chain and 22 kD beta chain. It is part of the GPIb-V-IX system that constitutes the receptor for von Willebrand factor (VWF), and mediates platelet adhesion in the arterial circulation. GPIb alpha chain provides the VWF binding site, and GPIb beta contributes to surface expression of the receptor and participates in transmembrane signaling through phosphorylation of its intracellular domain. Mutations in the GPIb beta subunit have been associated with Bernard-Soulier syndrome, velocardiofacial syndrome and giant platelet disorder. The 206 amino acid precursor of GPIb beta is synthesized from a 1.0 kb mRNA expressed in plateletes and megakaryocytes. A 411 amino acid protein arising from a longer, unspliced transcript in endothelial cells has been described; however, the authenticity of this product has been questioned. Yet another less abundant GPIb beta mRNA species of 3.5 kb, expressed in nonhematopoietic tissues such as endothelium, brain and heart, was shown to result from inefficient usage of a non-consensus polyA signal in the neighboring upstream gene (SEPT5, septin 5). In the absence of polyadenylation from its own imperfect site, the SEPT5 gene produces read-through transcripts that use the consensus polyA signal of this gene. [provided by RefSeq, Dec 2010] (from NCBI)
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Papers on GPIbbeta
Novel mutation in the glycoprotein Ibβ in a patient with Bernard-Soulier syndrome: possibility of distant parental consanguinity.
GeneRIF
Muwakkit et al., Beirut, Lebanon. In Blood Coagul Fibrinolysis, 2012
A 14-month-old boy with Bernard-Soulier syndrome was found to be homozygous for a nonsense mutation (c.423C > A) in the glycoprotein Ib-beta.
Quaternary organization of GPIb-IX complex and insights into Bernard-Soulier syndrome revealed by the structures of GPIbβ and a GPIbβ/GPIX chimera.
GeneRIF
Emsley et al., Nottingham, United Kingdom. In Blood, 2011
GPIbbeta missense mutations from Bernard-Soulier syndrome were examined for changes to GPIb-IX complex surface expression. Mutations A108P and P74R were found to maintain normal secretion/folding of GPIbbeta(E) but were unable to support GPIX surface expression
Delineating the roles of the GPIIb/IIIa and GP-Ib-IX-V platelet receptors in mediating platelet adhesion to adsorbed fibrinogen and albumin.
GeneRIF
Latour et al., Cleveland, United States. In Biomaterials, 2011
GPIIb/IIIa is the primary receptor set involved in platelet adhesion to adsorbed fibrinogen and serum albumin irrespective of their degree of adsorption-induced unfolding, while the GPIb-IX-V receptor complex plays an insignificant role.
Molecular basis of Bernard-Soulier syndrome in 27 patients from India.
GeneRIF
Srivastava et al., Vellore, India. In J Thromb Haemost, 2011
Report glycoprotein Ib/IX complex mutations found in Bernard-Soulier syndrome in Indian patients.
Platelet glycoprotein Ib beta/IX mediates glycoprotein Ib alpha localization to membrane lipid domain critical for von Willebrand factor interaction at high shear.
GeneRIF
Peng et al., Shanghai, China. In J Biol Chem, 2011
GP Ibbeta/GP IX mediates the disulfide-linked GP Ibalpha localization to the GEMs, which is critical for vWf interaction at high shear
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