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668 Chapter 14: Radioimmunotherapy
Figure 1. Francis William Rogers Brambell (1901-1970), Commander of the British
Empire, Fellow of the Royal Society, Royal Medallist, Professor of Zoology, and Director of
the Agricultural Research Council Unit of Embryology, University College of North Wales,
Bangor, U.K. Photo courtesy of Dr. Michael Brambell.
IgA, and IgM. Furthermore, it was shown that Fc of IgG, but no other classes, was
both necessary and sufficient to mediate this activity. To resolve this paradox,
Brambell et al. inferred that the only thing compatible with this finding was in fact
a nonsaturable catabolic mechanism, and a saturable protection mechanism, in direct
parallel to the antenatal and neonatal transport mechanism he and colleagues had
previously established for IgG transmission. For protection from catabolism, he
inferred a "protection receptor" on the walls of the vesicles of pinocytotically active
cells that selectively rescued IgG from catabolism by lysosomes. 3
The model we suggest to account for these findings is the isolation from the
general pool in a special compartment or compartments of a part of the 7-globulin
solution. The essential point is that, of the -y-globulin so isolated, only those
molecules which attach to receptors are saved and returned to the circulation. It is
suggested that isolation is effected by pinocytosis and that the receptors are
intracellular in the walls of the vesicles.
As to the site of IgG catabolism, Brambell 4
averred "the catabolism of 7-globulin
in the manner predicted could take place in any part of the body in which pinocytosis
of plasma proteins occurs and that where this is not implicit in the hypothesis."
Waldmann and Jones 5
later inferred that the vascular endothelium was most likely
as the primary site of IgG catabolism, which is also the dominant tissue in the body
for endocytosis. Furthermore, they discovered that Brambell's receptor mediates