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Human Recombinant Interleukin 2 Binds to Mouse Red Blood Cells via the Erythropoietin Receptor

  • Rita B. Moyes
  • John R. DeLoach

Abstract

Murine red blood cells (RBC) incubated with recombinant human interleukin 2 (rIL2) bound 10–20% of the added cytokine with 41.28 ± 4.64% of the population positive for bound cytokine as determined by fluorescence activated cell scanning (FACS) analysis. It has been well documented that 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 hypothesized 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 labeled 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.

Keywords

Erythropoietin Receptor CTLL Cell Residual EPOR Fluorescence Activate Cell Scanning Natural Killer Enhance Factor 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1997

Authors and Affiliations

  • Rita B. Moyes
    • 1
  • John R. DeLoach
    • 1
  1. 1.USDA-ARS-FAPRLCollege StationUSA

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