SOFT 2004 Meeting Abstracts - Society of Forensic Toxicologists

A65
A STUDY OF CROSS-REACTIVITY OF SELECTED ANIMAL PROTEINS ON AN ENZYME­
LINKED IMMUNOASSAY FOR RECOMBINANT HUMAN ERYTHROPOIETIN
Richard Stripp' and Lillian Guia
John Jay College of Criminal Justice, The City University ofNew York, New York, NY, USA
The FDA approved recombinant human erythropoietin, otherwise known as rhuEPO, for human use in
1991. Recombinant human erythropoietin was created for patients with anemia to boost red blood cell
production, termed erythropoiesis. Alleged abuse due to availability during clinical trials has been reported
as early as 1987 in human athletes. Administration of rhuEPO to a healthy patient is similar to blood
doping or training at high altitudes. It increases the level of circulating erythrocytes, increasing the oxygen
carrying capacity of the blood to reduce fatigue in the athlete competing in endurance sports. This abuse,
not limited to human athletes, has been reported in horseracing as well. The unique characteristic of
administration ofrhuEPO to the equine athlete results in an immune reaction to the drug. This results in an
autoimmune reaction to the horse's intrinsic erythropoietin, causing severe anemia and in some cases death.
These reactions create antibodies detectable in an enzyme-linked immunoassay (ELISA). Questions have
been proposed as to the specificity of this assay to react only to the anti- rhuEPO, and not to other intrinsic
proteins in equine serum. In order to ensure the assay is detecting only the horse's antibody to rhuEPO, we
have tested the assay against various immunoglobulins and sera from equine and other sources. Reactions
from all of the 19G's and sera tested and potential cross reactivity between the ELISA rhuEPO plate and
serum proteins in animals are presented.
Keywords: rhuEPO, Blood doping, ELISA
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