Hemopexin decreases spontaneous chemiluminescence of cold preserved liver after reperfusion.

Hemopexin is a plasma protein with exceptionally high affinity for heme. During liver transplantation heme is released via lysis of transfused blood. This heme may catalyze peroxidative reactions that contribute to "reperfusion" injury of the organ. Using a rat liver model of cold storage and reperfusion we tested the potential anti-oxidant effects of hemopexin. After 3 h of cold storage rat liver was reperfused with warm oxygenated buffer. Spontaneous liver chemiluminescence, which is a parameter of oxyradical production, was measured during reperfusion and expressed as an index of free radical production (IFRP). Chemiluminescence reached a maximum within 5 min of reperfusion and decreased to baseline within 30 min. Addition of hemopexin to the perfusate (5 microM) significantly decreased the IFRP. By contrast, the control proteins albumin and gamma-globulin (10 microM) had a smaller non-significant effect. The data suggest that heme could be complexed by hemopexin during reperfusion, thus inhibiting heme mediated cellular injury.