A variant thrombasthenic phenotype associated with compound heterozygosity of integrin beta3-subunit: (Met124Val)beta3 alters the subunit dimerization rendering a decreased number of constitutive active alphaIIbbeta3 receptors.

@article{GonzlezManchn2004AVT,
  title={A variant thrombasthenic phenotype associated with compound heterozygosity of integrin beta3-subunit: (Met124Val)beta3 alters the subunit dimerization rendering a decreased number of constitutive active alphaIIbbeta3 receptors.},
  author={Consuelo Gonz{\'a}lez-Manch{\'o}n and Nora C. Butta and Susana Larrucea and Elena Garcia Arias-Salgado and Sonia Alonso and Angela J L{\'o}pez and Roberto Parrilla},
  journal={Thrombosis and haemostasis},
  year={2004},
  volume={92 6},
  pages={1377-86}
}
We report the analysis of a variant case of thrombasthenic phenotype that is a compound heterozygote for two mutations located within the metal ion dependent adhesion site (MIDAS) of the beta3 subunit. The patient inherited a maternal allele carrying the Met124Val substitution and a paternal allele that changes Asp119 to Tyr. Phenotyping of the human platelet antigen 1 (HPA-1) showed that the platelet alphaIIbbeta3 complex in the patient was mostly accounted for by the Asp 119Tyr allele that… CONTINUE READING