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Bone marrow and tissue expression of gpIIb/IIIa, LFA‐1, Mac‐1 and gp150,95 glycoproteins
Author(s) -
Soligo Davide,
Cattoretti Giorgio,
Colombi Mariangela,
Polli Nicoletta,
Capsoni Franco,
Rilke Franco,
Deliliers Giorgio Lambertenghi
Publication year - 1989
Publication title -
european journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.904
H-Index - 84
eISSN - 1600-0609
pISSN - 0902-4441
DOI - 10.1111/j.1600-0609.1989.tb01207.x
Subject(s) - glycoprotein , bone marrow , platelet , platelet membrane glycoprotein , microbiology and biotechnology , chemistry , cancer research , pathology , medicine , immunology , biology
Monoclonal antibodies (MAbs) against platelet glycoprotein gpIIb/IIIa and the leucocyte adhesion molecules LFA‐1, Mac‐1, and gp 150,95 α chain (CD11a,b,c) and β chain (CD18) have been tested in normal and leukaemic bone marrows, in different human tissues, and in a patient with leucocyte adhesion deficiency (LAD). The effect of these MAbs on platelet aggregation was also tested. GpIIb/IIIa showed widespread distribution, while reactivity of CD11/18 antibodies was limited to haematopoietic cells. Platelets and megakaryocytes were reactive with one CD11a (25.5.2), and with no CD11b/c or CD18 MAbs. GpIIb/IIIa was present on the platelets of the patient with LAD, whereas 25.5.2, (CD11a) bound to his platelets but not to his leucocytes. These data indicate that LFA‐1, Mac‐1, and gp150,95 are not present on human platelets, but they suggest the existence of crossreacting epitopes on gpIIb/IIIa, which is consistent with the hypothesis that these molecules belong to a supergene family of adhesion molecules.