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Cys97→Tyr mutation in the glycoprotein IX gene associated with Bernard‐Soulier syndrome
Author(s) -
Kunishima Shinji,
Tomiyama Yoshiaki,
Honda Shigenori,
Kurata Yoshiyuki,
Kamiya Tadashi,
Ozawa Kazuo,
Saito Hidehiko
Publication year - 1999
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1046/j.1365-2141.1999.01733.x
Subject(s) - bernard–soulier syndrome , missense mutation , von willebrand factor , platelet membrane glycoprotein , mutation , microbiology and biotechnology , mutant , transfection , platelet , glycoprotein ib , platelet glycoprotein gpib ix complex , phenotype , gene , biology , glycoprotein , genetics , immunology
Bernard‐Soulier syndrome (BSS) is an autosomal recessive bleeding disorder due to quantitative or qualitative abnormalities in the glycoprotein (GP) Ib/IX/V complex, the platelet receptor for von Willebrand factor. We describe here the genetic basis of the disorder in a patient with BSS. Flow cytometric analysis of the patient's platelets showed a greatly reduced GPIbα and completely absent GPIX surface expression. Immunoblot analysis disclosed greatly reduced GPIbα and residual amounts of GPIbβ and GPIX in the platelets. DNA sequencing analysis revealed the patient to be homozygous for a novel missense mutation in the GPIX gene that converts Cys (TGT) to Tyr (TAT) at residue 97. Transient transfection studies confirmed that mutant GPIX was not expressed on the transfected cells, showing that the mutation was responsible for the BSS phenotype observed in the patient.