Heme-oxygenases during erythropoiesis in K562 and human bone marrow cells

dc.creatorAlves, Liliane R.
dc.creatorCosta, Elaine S.
dc.creatorSorgine, Marcos H. F.
dc.creatorSilva, Maria Clara L Nascimento
dc.creatorTeodosio, Cristina
dc.creatorBárcena, Paloma
dc.creatorFaria Neto, Hugo C. Castro
dc.creatorBozza, Patrícia T.
dc.creatorOrfao, Alberto
dc.creatorOliveira, Pedro L.
dc.creatorMonteiro, Clarissa M. Maya
dc.date2018-11-18T13:11:33Z
dc.date2018-11-18T13:11:33Z
dc.date2011
dc.date.accessioned2023-09-26T20:12:46Z
dc.date.available2023-09-26T20:12:46Z
dc.identifierALVES, Liliane R. et al. Heme-Oxygenases during Erythropoiesis in K562 and Human Bone Marrow Cells. Plos One, v.6, n.7, e21358, 9p, July 2011.
dc.identifier1932-6203
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/30070
dc.identifier10.1371/journal.pone.0021358
dc.identifier1932-6203
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8851514
dc.descriptionIn mammalian cells, heme can be degraded by heme-oxygenases (HO). Heme-oxygenase 1 (HO-1) is known to be the heme inducible isoform, whereas heme-oxygenase 2 (HO-2) is the constitutive enzyme. Here we investigated the presence of HO during erythroid differentiation in human bone marrow erythroid precursors and K562 cells. HO-1 mRNA and protein expression levels were below limits of detection in K562 cells. Moreover, heme was unable to induce HO-1, at the protein and mRNA profiles. Surprisingly, HO-2 expression was inhibited upon incubation with heme. To evaluate the physiological relevance of these findings, we analyzed HO expression during normal erythropoiesis in human bone marrow. Erythroid precursors were characterized by lack of significant expression of HO-1 and by progressive reduction of HO-2 during differentiation. FLVCR expression, a recently described heme exporter found in erythroid precursors, was also analyzed. Interestingly, the disruption in the HO detoxification system was accompanied by a transient induction of FLVCR. It will be interesting to verify if the inhibition of HO expression, that we found, is preventing a futile cycle of concomitant heme synthesis and catabolism. We believe that a significant feature of erythropoiesis could be the replacement of heme breakdown by heme exportation, as a mechanism to prevent heme toxicity.
dc.formatapplication/pdf
dc.languageeng
dc.publisherPublic Library of Science
dc.rightsopen access
dc.subjectHeme-oxigenases
dc.subjectK562
dc.subjecteritropoiese
dc.subjectcélulas da medula óssea humana
dc.subjectHuman Bone Marrow Cells
dc.subjectHeme-Oxygenases
dc.subjectErythropoiesis
dc.subjectK562
dc.titleHeme-oxygenases during erythropoiesis in K562 and human bone marrow cells
dc.typeArticle


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