anti-Glycoprotein Ib (Platelet), beta Polypeptide (GP1BB) Antibodies

Human Glycoprotein Ib (Platelet), beta Polypeptide (GP1BB) interaction partners

1. loss of CD34 and expression of CD42b define cells capable of factor V endocytosis and trafficking to proplatelet extensions during differentiation of megakaryocytes ex vivo from progenitor cells isolated from umbilical cord blood

2. Rare variants in GP1BB are responsible for autosomal dominant macrothrombocytopenia.

3. miR-10a and miR10b regulate the expression of human platelet GP1BA and GP1bb for normal megakaryopoiesis.

4. Data show that localization of the GP Ib-IX complex to the lipid domain is mediated by GP Ibbeta and GP IX transmembrane domains.

5. Low levels of CD9 coincidental with a novel nonsense mutation in glycoprotein Ibbeta in a patient with Bernard-Soulier syndrome.

6. genetic association study in population in western India: Data suggest novel mutations in platelet glycoprotein Ib (GP1BA, GP1BB) and GP9 are associated with Bernard-Soulier syndrome in subjects studies; of 12 mutations identified, ten were novel.

7. a suspicion of 22q11.2 deletion is warranted in pediatric BSS patients with a mutation in the GPIbbeta gene, even without remarkable symptoms.

8. 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.

9. 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

10. A novel variant of Bernard Soulier syndrome is described in which Ser23 of GPIbbeta is substituted by a Stop codon causing a premature termination of translation.

11. 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.

12. Report glycoprotein Ib/IX complex mutations found in Bernard-Soulier syndrome in Indian patients.

13. 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.

14. GP Ibbeta/GP IX mediates the disulfide-linked GP Ibalpha localization to the GEMs, which is critical for vWf interaction at high shear

15. Identify TRAF4 as a novel binding partner for GPIb-IX-V and GPVI in human platelets.

16. -induced activation of GpIb-V-IX triggers platelet procoagulant activity and anchorage of a star-like fibrin network.

17. putative convex surface of the LRR domain in GPIX is sufficient, in the context of full-length subunit, to mediate its association with GPIbbeta

18. Lateral clustering of platelet GP Ib-IX complexes leads to up-regulation of the adhesive function of integrin alpha IIbbeta 3

19. Role of GPIbbeta in modulating vWF mediated platelet adhesion.

20. A GP1BB missense mutation suppresses GPIb/IX complex expression and is found to cause Bernard-Soulier Syndrome in the homozygous form and giant platelets in the heterozygous form.

Mouse (Murine) Glycoprotein Ib (Platelet), beta Polypeptide (GP1BB) interaction partners

1. These results indicate that Reelin 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

2. GPIbbeta has a repressor function in thrombus formation

3. These data indicate an important role for the platelet adhesion receptor GPIb-IX in endotoxin-induced thrombosis and thrombocytopenia.

4. Data show that the surface-bound VWF appears as a large, linear structure on the surface of 50% of the PT-VWD platelets.

5. Role of GPIbbeta in modulating vWF mediated platelet adhesion.