부산대학교 도서관

Heme (iron protoporphyrin IX) is a major toxic component of hemoglobin released from red cell turnover especially during intravascular hemolysis such as in sickle cell disease, malaria and paroxysmal nocturnal hemoglobinuria. Heme oxygenase 1 (HO-1) is an enzyme that degrades heme, primarily generated by damaged or senescent red blood cells, releasing iron from protoporphyrin and generating equimolar amounts of biliverdin and carbon monoxide. The HO-1 heme catabolic pathway provides an important defense from oxidant and inflammatory consequences of exposure to free heme. HO-1 induction occurs as a transcriptional response to heme through the NRF2 oxidant-sensing transcription factor. Placental Growth Factor (PGF) is an angiogenic growth factor secreted by proliferating erythroblasts during normal development, which we previously have found is also activated by heme, secondarily regulating expression of the vasoconstrictor endothelin-1 that promotes pulmonary hypertension. We assessed the transcriptional response of HO-1 and PGF in different organs in C57BL/6J wild type (WT) and Nrf2 null mice following acute exposure to heme.