Cross-linking of the ninth consensus repeat domain of P-selectin (GMP-140, CD62P) with a monoclonal antibody enhanced leukocyte adhesive activity.
P-selectin (GMP-140, CD62P) is a member of the selectin family of cell adhesion molecules expressed on the cell surface of platelets and endothelial cells, which mediates leukocyte adhesion via carbohydrate ligands. We now report that a monoclonal antibody (mAb), recognizing the ninth consensus repeat domain of the human P-selectin molecule, enhanced the adhesion activity of neutrophils to platelets, whereas the monovalent Fab fragment of the mAb did not exert this effect. The enhancement by the mAb was thought to result from cross-linking of the P-selectin molecules. The results indicated that cross-linking adjacent to the transmembrane domain of P-selectin enhanced the cell adhesion activity.
Yokota
S
S
Sumitomo Pharmaceuticals Research Center, Osaka, Japan.
Nunn
M F
MF
Morooka
S
S
D000911:Antibodies, Monoclonal / Q000276:immunology; D001792:Blood Platelets / Q000737:chemistry / Q000166:cytology*; D002448:Cell Adhesion; D002478:Cells, Cultured; D003432:Cross-Linking Reagents; D018604:Epitope Mapping; D018922:HL-60 Cells; D006801:Humans; D009504:Neutrophils / Q000166:cytology*; D019007:P-Selectin / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism; D011940:Receptor Aggregation
D000911:Antibodies, Monoclonal; D003432:Cross-Linking Reagents; D019007:P-Selectin