TY - JOUR
T1 - Cross-linking of the carcinoembryonic antigen-like glycoproteins CD66 and CD67 induces neutrophil aggregation
AU - Kuijpers, T. W.
AU - van der Schoot, C. E.
AU - Hoogerwerf, M.
AU - Roos, D.
PY - 1993
Y1 - 1993
N2 - The carcinoembryonic Ag (CEA)-like glycoproteins present on human granulocytes have been designated non-specific cross-reacting Ag (NCA). We have recently demonstrated that granulocyte-specific CD66 and CD67 mAb recognize the three originally described NCA. CD66 binds to NCA-160 and NCA-90, whereas CD67 only recognizes NCA-95. As we have shown previously, NCA-160 and NCA-90 present sialylated Lewis-X oligosaccharide Ag (SLex) in a functional way, i.e., these Ag function as (one of many possible) molecules involved in neutrophil binding to the adhesion molecule E-selectin expressed on activated endothelial cells. In this study, we found that a polyclonal anti-CEA antiserum, either as intact Ig or as F(ab')2 fragments, induced neutrophil aggregation. This aggregation response was blocked by CD18 mAb. Neutrophils from a patient severely affected by paroxysmal nocturnal hemoglobinuria completely lacked expression of NCA-95 and NCA-90. The patient's neutrophils repeatedly showed no aggregation on addition of the anti-CEA antiserum. Thus, the presence of the phosphatidylinositol-linked NCA-95/90 seems to be essential for NCA-induced neutrophil activation. Our data indicate that NCA molecules on neutrophils may function via binding to E-selection or an as yet unknown ligand (as mimicked here by an antiserum) and subsequently induce CD18-dependent adhesive properties
AB - The carcinoembryonic Ag (CEA)-like glycoproteins present on human granulocytes have been designated non-specific cross-reacting Ag (NCA). We have recently demonstrated that granulocyte-specific CD66 and CD67 mAb recognize the three originally described NCA. CD66 binds to NCA-160 and NCA-90, whereas CD67 only recognizes NCA-95. As we have shown previously, NCA-160 and NCA-90 present sialylated Lewis-X oligosaccharide Ag (SLex) in a functional way, i.e., these Ag function as (one of many possible) molecules involved in neutrophil binding to the adhesion molecule E-selectin expressed on activated endothelial cells. In this study, we found that a polyclonal anti-CEA antiserum, either as intact Ig or as F(ab')2 fragments, induced neutrophil aggregation. This aggregation response was blocked by CD18 mAb. Neutrophils from a patient severely affected by paroxysmal nocturnal hemoglobinuria completely lacked expression of NCA-95 and NCA-90. The patient's neutrophils repeatedly showed no aggregation on addition of the anti-CEA antiserum. Thus, the presence of the phosphatidylinositol-linked NCA-95/90 seems to be essential for NCA-induced neutrophil activation. Our data indicate that NCA molecules on neutrophils may function via binding to E-selection or an as yet unknown ligand (as mimicked here by an antiserum) and subsequently induce CD18-dependent adhesive properties
M3 - Article
C2 - 8104998
SN - 0022-1767
VL - 151
SP - 4934
EP - 4940
JO - Journal of immunology (Baltimore, Md.
JF - Journal of immunology (Baltimore, Md.
IS - 9
ER -