Abstract
α-FOETOPROTEIN (AFP), an embryo-specific glycoprotein, is primarily known as a tumour-associated embryonic antigen. Although much is known about the occurrence of AFP in ontogeny and levels of AFP in different diseases, such as hepatocellular carcinoma and other tumours1–4, little work has been done on its functional significance. Results from our laboratory have shown that AFP exerts an immunosuppressive effect on antibody synthesis when administered in vivo5 and that it is a non-cytotoxic suppressor of both the primary and secondary antibody response to sheep red blood cells (SRBC) in vitro6. In addition, we found that AFP suppresses certain T-cell-dependent functions in mice such as allogeneic and mitogeninduced lymphocyte transformation7. A recent report8 suggests that bovine foetuin is immunosuppressive for mitogen and allogeneic reactions. Bovine foetuin and AFP have, however, been shown to be different proteins9. Moreover, in view of the relatively large amounts of foetuin used to obtain suppression (10,000-fold higher than those required for suppression in our studies using AFP), it is possible that the foetuin preparations were contaminated with suppressive amounts of bovine AFP.
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DATTWYLER, R., MURGITA, R. & TOMASI, T. Binding of α-foetoprotein to murine T cells. Nature 256, 656–657 (1975). https://doi.org/10.1038/256656a0
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DOI: https://doi.org/10.1038/256656a0
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