The red cell chemokine receptor is distinct from the Fy6 epitope

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Abstract
Previous studies established an association between the red cell chemokine receptor and Fy6 of the Duffy glycoprotein. The relationship between Duffy system antigens and interleukin 8 binding by red cells was examined. Interleukin 8 adsorption was measured by using red cells from owl, squirrel, and rhesus monkeys, and human red cells before and after saturation with anti-Fya (anti-Fy1), anti-Fyb (anti-Fy2), or anti-Fy6. The effect of cell saturation with interleukin 8 on Duffy system antigen expression and the effect of enzyme treatment on interleukin 8 adsorption were also examined. Fy:1,-2,6 or Fy:-1,2,6 (owl monkey, squirrel monkey, human) red cells adsorbed interleukin 8 over a wide range of concentrations (125-1000 pg/mL). Human Fy:-1,-2,-6 red cells bound minimal interleukin 8. Human red cells saturated with corresponding antibodies displayed decreased interleukin 8 binding. Saturation of human cells with interleukin 8 failed to interfere with Duffy system antigen expression. Rhesus monkey cells lacking Fy1, Fy2, and Fy6 were able to adsorb interleukin 8 in a manner similar to Fy:1,-2,6 or Fy:-1,2,6 primate cells. Ficin treatment eliminated both Duffy system antigen expression and interleukin 8 adsorption from red cells. The Duffy glycoprotein binds interleukin 8. Although previous studies suggested that interleukin 8 bound either directly to or close to the Fy6 epitope, the ability of Fy:-1,-2,-6 rhesus monkey cells to adsorb interleukin 8 suggests that the interleukin 8 receptor is distinct from Fy6, Fy1, and Fy2.