Rd. Baynes, TRANSFERRIN REDUCES THE PRODUCTION OF SOLUBLE TRANSFERRIN RECEPTOR, Proceedings of the Society for Experimental Biology and Medicine, 209(3), 1995, pp. 286-294
The effect of homologous diferric transferrin from which contaminating
transferrin receptor had been removed by monoclonal antibody affinity
chromatography on soluble transferrin receptor concentrations was stu
died in K562 cells and HL60 cells in culture. Diferric transferrin in
K562 cells caused a dose-dependent decrease in cellular receptor expre
ssion, a dose-dependent increase in cellular ferritin content, and a r
eduction in soluble receptor concentration which was of greater propor
tional magnitude than the reduction in cell receptor content. In HL60
cells, while there was a dose-dependent Increase in cellular ferritin,
cellular receptor content was relatively unaffected, while there was
a consistent reduction in soluble receptor concentration. In both cell
s, the inhibitory effect of diferric transferrin on soluble receptor c
oncentration was evident as early as 3 hr into the incubation. Apotran
sferrin, by contrast, did not reduce soluble receptor concentration. W
hile elemental iron was capable of producing similar changes in cellul
ar receptor and ferritin content, It had no inhibitory effect on propo
rtional soluble receptor content. Studies employing other proteins, in
cluding human and bovine serum albumin, human lactoferrin, and rat fer
ritin, had no inhibitory effect on soluble receptors concentration, th
us confirming the specificity of the findings. Control studies exclude
d an assay artifact as the explanation for the current findings. Prior
contrary reports appear completely explained by the combination of so
luble transferrin receptor contaminating the transferrin employed for
study and a systematic difference in the assays employed between free
and transferrin-bound receptor.