Detachment of cell surface-bound anticarcinoembryonic antigen immune complexes by phospholipase C.


Autoria(s): Matzku S.; Mach J.P.; Buchegger F.; Moldenhauer G.; Stadler M.; Kalthoff H.
Data(s)

1991

Resumo

CEA as well as normal cross-reacting antigens (NCA) are fixed to the cell membrane via phosphatidylinositol (PI). To find out whether these antigens are internalized after antibody contact, acid pH desorption was compared to phospholipase C (PLC)-mediated cleavage of the antigen anchor. With the former procedure, marked differences in the desorbability of individual MAbs were noted, while PLC was able to cleave off surface-bound immune complexes irrespective of the MAb involved. From this it is concluded that internalization of MAb complexes of CEA/NCA, if occurring at all, is a low efficiency process.

Identificador

http://serval.unil.ch/?id=serval:BIB_1AA93CDDF8F2

isbn:1010-4283 (Print)

pmid:1962149

doi:10.1159/000217715

isiid:A1991GU28000005

Idioma(s)

en

Fonte

Tumour Biology, vol. 12, no. 5, pp. 272-278

Palavras-Chave #Antibodies, Monoclonal/immunology; Antigen-Antibody Complex/metabolism; Carcinoembryonic Antigen/immunology; Cell Line; Cell Membrane/immunology; Humans; Hydrogen-Ion Concentration; Phosphatidylinositols/metabolism; Tumor Cells, Cultured; Type C Phospholipases/metabolism
Tipo

info:eu-repo/semantics/article

article