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Title: Human pregnancy zone protein and alpha 2-macroglobulin. High-affinity binding of complexes to the same receptor on fibroblasts and characterization by monoclonal antibodies
Authors: Van Leuven, Freddy ×
Cassiman, Jean-Jacques
Van den Berghe, Herman #
Issue Date: Jan-1987
Series Title: Journal of Biological Chemistry vol:261 issue:35 pages:16622-5
Abstract: Pregnancy zone protein (PZP) was isolated from late pregnancy serum and examined for binding to normal skin fibroblasts in culture. A high-affinity binding site on these cells is demonstrated for PZP reacted with methylamine. Experiments with alpha 2-macroglobulin (alpha 2M) and PZP, both modified by methylamine, showed this receptor to be identical to the previously characterized receptor for alpha 2M-proteinase complexes (Van Leuven, F., Cassiman, J.J., and Van den Berghe, H. (1979) J. Biol. Chem. 254, 5155-5160). With available monoclonal antibodies directed toward alpha 2M and prepared toward PZP, only a limited cross-reaction was observed. We obtained a monoclonal antibody which defines a neo-antigenic site on PZP-methylamine, completely analogous to the monoclonal antibody F2B2, which was previously shown to define a neo-antigenic site on alpha 2M complexes (Marynen, P., Van Leuven, F., Cassiman, J.J., and Van den Berghe, H. (1981) J. Immunol. 127, 1782-1786). These results provide evidence for the homologous function of alpha 2M and PZP as proteinase scavengers. The need for an extra proteinase inhibitor of the alpha 2M-type in pregnancy is discussed. The monoclonal antibodies now available will prove helpful in quantitation and eventually isolation of proteinase complexes of alpha 2M and PZP.
ISSN: 0021-9258
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Associated Laboratories - miscellaneous (-)
Human Mutations and Polymorphisms Section (-)
Clinical Genetics Section (-)
Forensic Biomedical Sciences
Department of Human Genetics - miscellaneous
× corresponding author
# (joint) last author

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