Induction of heme oxygenase is a rapid, protective response in rhabdomyolysis in the rat.

Karl A. Nath, G Balla, Gregory M. Vercellotti, József Balla, Harry S. Jacob, Michael D. Levitt, Mark E. Rosenberg

Journal of Clinical Investigation · 1992 · 693 citations · 21 references

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TL;DR

Extracellular myoglobin and hemoglobin release can cause tissue toxicity and are implicated in renal failure during rhabdomyolysis. In a glycerol‑induced rhabdomyolysis model, kidneys upregulate heme oxygenase and ferritin synthesis in response to excess heme proteins. Pre‑infusion of hemoglobin activates heme oxygenase/ferritin, preventing kidney failure and reducing mortality from 100 % to 14 %, whereas inhibition worsens dysfunction, demonstrating a rapid protective antioxidant response and suggesting a therapeutic strategy for high‑risk rhabdomyolysis patients.

Abstract

Heme proteins such as myoglobin or hemoglobin, when released into the extracellular space, can instigate tissue toxicity. Myoglobin is directly implicated in the pathogenesis of renal failure in rhabdomyolysis. In the glycerol model of this syndrome, we demonstrate that the kidney responds to such inordinate amounts of heme proteins by inducing the heme-degradative enzyme, heme oxygenase, as well as increasing the synthesis of ferritin, the major cellular repository for iron. Prior recruitment of this response with a single preinfusion of hemoglobin prevents kidney failure and drastically reduces mortality (from 100% to 14%). Conversely, ablating this response with a competitive inhibitor of heme oxygenase exacerbates kidney dysfunction. We provide the first in vivo evidence that induction of heme oxygenase coupled to ferritin synthesis is a rapid, protective antioxidant response. Our findings suggest a therapeutic strategy for populations at a high risk for rhabdomyolysis.

References

21