Characterization of two monoclonal antibodies against porcine VCAIM-1

Citation
C. Richard et al., Characterization of two monoclonal antibodies against porcine VCAIM-1, HYBRIDOMA, 18(2), 1999, pp. 159-165
Citations number
33
Categorie Soggetti
Immunology
Journal title
HYBRIDOMA
ISSN journal
0272457X → ACNP
Volume
18
Issue
2
Year of publication
1999
Pages
159 - 165
Database
ISI
SICI code
0272-457X(199904)18:2<159:COTMAA>2.0.ZU;2-C
Abstract
Immunization of mice with TNF alpha-activated porcine endothelial cells led to the characterization of two monoclonal antibodies (MAbs), 5F3 and 8A7, specific for porcine VCAM-1, Upon flow cytometry, both antibodies increasin gly labeled endothelial cells according to their degree of activation. They bound a band of MW 80 kDa on Western blots of endothelial cells, which is the apparent molecular weight of porcine VCAM-1, It was determined by surfa ce plasmon resonance that the antibodies are directed to different antigeni c sites. It was also found that 5F3 competes for binding the antigen with a MAb previously characterized as binding domain 1 of porcine VCAM-1, Subseq uently, 5F3, but not 8A7, was found to inhibit the adhesion of human B lymp hocyte Ramos cells to porcine endothelial cells in vitro. These antibodies, which do not cross-react with human VCAM-1, might be useful for diagnostic or therapeutic purposes in xenotransplantation.