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© Research
Publication : Transfusion

A new Ser472Asn (Cab2(a+)) polymorphism localized within the αIIb “thigh” domain is involved in neonatal thrombocytopenia.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Transfusion - 01 Feb 2011

Jallu V, Dusseaux M, Kaplan C,

Link to Pubmed [PMID] – 20723174

Link to DOI – 10.1111/j.1537-2995.2010.02815.x

Transfusion 2011 Feb; 51(2): 393-400

A new platelet antigen, Cab2(a+), was identified in a case of severe neonatal alloimmune thrombocytopenia (A mutation leading to a Ser472Asn substitution. Immunologic assays with transfected CHO cells revealed the Asn472 form of αIIbβ3 responsible for the Cab2(a+) epitope but not an Ala472 form. Using these cells lines we demonstrated that both Ser472Asn and Ser472Ala substitutions produced limited structural alteration as revealed by the reactivity of a panel of anti-αIIbβ3 monoclonal antibodies (MoAbs). Activated Asn472 and Ala472 forms of αIIbβ3 supported 1) binding of soluble fibrinogen and of the ligand mimetic MoAb PAC-1, 2) ligand-induced binding site epitopes exposure (MoAbs AP-5 and D3GP3), and 3) cell aggregation. Adhesion onto adsorbed fibrinogen was conserved and was specifically inhibited by MoAb AP-2 or peptide RGDS. Finally outside-in signaling was not affected.We have characterized a new low-frequency alloantigen (<1%) resulting from the Ser472Asn substitution in αIIb and shown this polymorphism to have a limited effect, if any, on the αIIbβ3 complex functions.

https://pubmed.ncbi.nlm.nih.gov/20723174