Binding of human recombinant interleukin 2 to murine erythrocytes is erythropoietin receptor mediated Academic Article uri icon

abstract

  • Murine red blood cells (RBC) incubated with recombinant human interleukin 2 (rIL2) bound 10%-20% of the added cytokine with 41% ± 5% of the population positive for bound cytokine as determined by fluorescence activated cell scanning (FACS) analysis. Since a high degree of homology exists between the erythropoietin receptor (EPOR) and the IL2βR chain (based both on amino acid sequence and hydrophobicity alignment), we hypothesised that the rIL2 was binding to residual EPOR on murine RBC. Upon bioassay, it was found that reticulocytes (RET), which express a higher percentage of EPOR than normal RBC, bound 400% more rIL2 as compared to normal RBC. FACS analysis using fluorescently labelled rIL2 revealed a log higher fluorescence intensity on RET compared to RBC. Therefore, the population of immature or young RBC in circulation which are expressing residual EPOR are binding rIL2 due to cross-reactivity between the EPOR and IL2βR. © 1996 Springer-Verlag London Limited.

author list (cited authors)

  • Moyes, R. B., & DeLoach, J. R.

citation count

  • 1

publication date

  • September 1996