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Platelet glycoprotein Ib (GPIb) is a heterodimeric transmembrane protein consisting of a disulfide-linked 140 kD alpha chain and 22 kD beta chain. Zusätzlich bieten wir Ihnen GP1BB Antikörper (36) und GP1BB Kits (9) und viele weitere Produktgruppen zu diesem Protein an.
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Rare variants in GP1BB are responsible for autosomal dominant macrothrombocytopenia.
miR (zeige MLXIP Proteine)-10a and miR10b regulate the expression of human platelet GP1BA (zeige GP1BA Proteine) and GP1bb for normal megakaryopoiesis.
Data show that localization of the GP Ib-IX complex to the lipid domain is mediated by GP Ibbeta and GP IX (zeige GP9 Proteine) transmembrane domains.
Low levels of CD9 (zeige CD9 Proteine) coincidental with a novel nonsense mutation in glycoprotein Ibbeta in a patient with Bernard-Soulier syndrome.
genetic association study in population in western India: Data suggest novel mutations in platelet glycoprotein Ib (GP1BA (zeige GP1BA Proteine), GP1BB) and GP9 (zeige GP9 Proteine) are associated with Bernard-Soulier syndrome in subjects studies; of 12 mutations identified, ten were novel.
a suspicion of 22q11.2 deletion is warranted in pediatric BSS (zeige GP1BA Proteine) patients with a mutation in the GPIbbeta gene, even without remarkable symptoms.
Studies indicate that platelets from Bernard-Soulier syndrome (BSS) are defective in glycoprotein (GP)Ib-IX-V, a platelet-specific adhesion-signaling complex, composed of GPIbalpha disulfide linked to GPIbbeta, and noncovalently associated with GPIX and GPV.
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 (zeige GP9 Proteine) surface expression
GPIIb/IIIa is the primary receptor set involved in platelet adhesion to adsorbed fibrinogen and serum albumin (zeige ALB Proteine) irrespective of their degree of adsorption-induced unfolding, while the GPIb-IX-V receptor complex plays an insignificant role.
GP Ibbeta/GP IX (zeige GP9 Proteine) mediates the disulfide-linked GP Ibalpha localization to the GEMs, which is critical for vWf (zeige VWF Proteine) interaction at high shear
These results indicate that Reelin (zeige RELN Proteine) is an important regulator of GPIb-mediated platelet activation and may represent a new therapeutic target for the prevention and treatment of cardio- and cerebrovascular diseases
Data show that the surface-bound VWF (zeige VWF Proteine) appears as a large, linear structure on the surface of 50% of the PT-VWD (zeige VWF Proteine) platelets.
Role of GPIbbeta in modulating vWF (zeige VWF Proteine) mediated platelet adhesion.
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.
glycoprotein Ib (platelet), beta polypeptide
, GP-Ib beta
, antigen CD42b-beta
, nuclear localization signal deleted in velocardiofacial syndrome
, platelet glycoprotein Ib beta chain
, glycoprotein Ib, beta polypeptide