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Research Article Free access | 10.1172/JCI115596

NH2-terminal globular domain of human platelet glycoprotein Ib alpha has a methionine 145/threonine145 amino acid polymorphism, which is associated with the HPA-2 (Ko) alloantigens.

R W Kuijpers, N M Faber, H T Cuypers, W H Ouwehand, and A E von dem Borne

Central Laboratory, The Netherlands Red Cross Blood Transfusion Service, Amsterdam.

Find articles by Kuijpers, R. in: JCI | PubMed | Google Scholar

Central Laboratory, The Netherlands Red Cross Blood Transfusion Service, Amsterdam.

Find articles by Faber, N. in: JCI | PubMed | Google Scholar

Central Laboratory, The Netherlands Red Cross Blood Transfusion Service, Amsterdam.

Find articles by Cuypers, H. in: JCI | PubMed | Google Scholar

Central Laboratory, The Netherlands Red Cross Blood Transfusion Service, Amsterdam.

Find articles by Ouwehand, W. in: JCI | PubMed | Google Scholar

Central Laboratory, The Netherlands Red Cross Blood Transfusion Service, Amsterdam.

Find articles by von dem Borne, A. in: JCI | PubMed | Google Scholar

Published February 1, 1992 - More info

Published in Volume 89, Issue 2 on February 1, 1992
J Clin Invest. 1992;89(2):381–384. https://doi.org/10.1172/JCI115596.
© 1992 The American Society for Clinical Investigation
Published February 1, 1992 - Version history
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Abstract

The glycoprotein (GP) Ib/IX complex, a prominent platelet GP complex, is the primary receptor for vWF. Previously, we have established that an antigenic polymorphism of platelets, the HPA-2 or Ko alloantigen system, is located on the 45-kD amino-terminal globular domain of GPIb alpha. With the polymerase chain reaction, we have amplified two segments of the GPIb alpha gene coding for the first 382 amino acids of two HPA-2a and two HPA-2b homozygous individuals. Nucleotide sequence analysis revealed as the only difference a C-T polymorphism at position 434 of the coding region for the mature protein. This base change results in a substitution of threonine (ACG) in HPA-2a (Kob) to methionine (ATG) in HPA-2b (Koa) at amino acid position 145. The C-T polymorphism is reflected in a difference in restriction enzyme recognition, resulting in an Aha 2-site in the HPA-2b allele and a SfaN1 site in the HPA-2a allele. Restriction fragment length polymorphism analysis of the amplified DNA of 3 HPA-2(a-,b+), 2 HPA-2(a+,b+), and 11 HPA-2(a+,b-) donors showed that these restriction sites were associated with the HPA-2 alleles. DNA-typing for the HPA-2 alloantigen system on genomic DNA obtained from a small number of cells may be applied for determining the genotype of a fetus from an immunized mother or of severely thrombocytopenic patients.

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