Genetic and structural characterization of an amino acid dimorphism in glycoprotein Ibα involved in platelet transfusion refractoriness

M. Murata, K. Furihata, F. Ishida, S. R. Russell, J. Ware, Z. M. Ruggeri

研究成果: Article査読

85 被引用数 (Scopus)

抄録

The platelet-specific alloantigen, Siba, located within the α-subunit of the glycoprotein (GP) Ib-IX membrane receptor, has been found to be involved in the pathogenesis of platelet transfusion refractoriness. We have identified the existence of a naturally occurring threonine/methionine dimorphism at position 145 of the GPIbα sequence, and determined that the Siba antigen corresponds to the molecule containing methionine145. The diallelic codons can be detected by restriction enzyme analysis of amplified genomic DNA fragments from the GPIbα gene. Evaluation of 61 healthy blood donors showed that the allele frequencies are 89% and 11% for the threonine145 and methionine145 codons, respectively. A positive correlation exists between platelet reactivity with the anti-Siba antibody and the presence of a methionine145-encoding allele. Moreover, recombinant expression of two soluble GPIbα fragments differing only at residue 145, provided definitive evidence that the human anti-Siba antibody reacts only with the molecule containing methionine145. These results explain the structural basis of the Siba human alloantigen system and define screening methodologies useful in transfusion medicine to match donor and recipient platelets accordingly.

本文言語English
ページ(範囲)3086-3090
ページ数5
ジャーナルBlood
79
11
DOI
出版ステータスPublished - 1992
外部発表はい

ASJC Scopus subject areas

  • 生化学
  • 免疫学
  • 血液学
  • 細胞生物学

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