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Editorial
. 2011 Mar;96(3):355-9.
doi: 10.3324/haematol.2010.039883.

Bernard-Soulier syndrome

Michael C Berndt, Robert K Andrews
Editorial

Bernard-Soulier syndrome

Michael C Berndt et al. Haematologica. 2011 Mar.
No abstract available

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Figures

Figure 1.
Figure 1.
The GPIb-IX-V complex composed of GPIbα disulphide-linked to two GPIbβ subunits, and noncovalently associated with GPIX and GPV. Disulphide bonds within domains either side of leucine-rich repeat domains are depicted as solid black bars. The position of sulphated tyrosine residues (Sulfo-Tyr at 276, 278 and 279 of GPIbα), phosphorylated serine residues (Phospho-Ser) and palmitylated Cys residues of GPIbβ and GPIX are indicated. C, C-terminus; N, N-terminus; TM, transmembrane domain.
Figure 2.
Figure 2.
Mutations of (A) GPIbα, (B) GPIbβ and (C) GPIX associated with Bernard-Soulier syndrome, mapped to the mature protein structure, indicating missense mutations or short deletions (green), nonsense mutations leading to premature stop (red), or mutations causing a frameshift leading to stop (blue), based mainly on Lanza and the Bernard-Soulier syndrome registry and website (http://www.bernardsouli-er.org/) and references therein. Mutations also occur in the GPIbβ and GPIX signal sequences leading to BSS. There are no reported mutations in GPV, which is not essential for functional GPIb-IX expression.,, The N-terminal 282 residues of GPIbα constitutes the major ligand-binding domain of GPIb-IX-V, with distinct or partially overlapping interactive sites for multiple ligands: VWF, thrombospondin, P-selectin, αMβ2 (Mac-1), thrombin, Factor XI, Factor XII and HMW kininogen. *autosomal dominant inheritance. **mutations detected by Savoia et al.
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