Functional and molecular characterization by the CB04 monoclonal antibody of a cell surface structure exerting C3-complement receptor activity.
CB04 monoclonal antibody which reacts with an epitope of a surface molecule expressed on human monocytes has been elicited using peripheral blood lymphocytes as immunizer. The characterization of the monoclonal antibody examined at the phenotypic, molecular, and functional levels indicates that the CB04 antibody defines a structure present on monocytes, tissue macrophages, B cells, polymorphonucleates, and erythrocytes. The molecular weight (220 kD), the tissue distribution in health and disease conditions, and the involvement in relevant biological processes indicate that the CB04 structure is the receptor for the C3b fragment of the complement. The binding of the antibody to the cell surface induces inhibition of the C3bi receptorial function.
Malavasi
F
F
Funaro
A
A
Bellone
G
G
Caligaris-Cappio
F
F
Berti
E
E
Tetta
C
C
Dellabona
P
P
DeMaria
S
S
Campogrande
M
M
Cappa
A P
AP
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000941:Antigens / Q000032:analysis; D011232:Chemical Precipitation; D000939:Epitopes / Q000032:analysis; D006801:Humans; D016177:Macrophage-1 Antigen; D051379:Mice; D008807:Mice, Inbred BALB C; D009000:Monocytes / Q000276:immunology*; D011951:Receptors, Complement / Q000032:analysis* / Q000276:immunology
D000911:Antibodies, Monoclonal; D000941:Antigens; D000939:Epitopes; D016177:Macrophage-1 Antigen; D011951:Receptors, Complement