Effects of metalloporphyrins on hemoglobin formation in mouse Friend virus-transformed erythroleukemia cells. Stimulation of heme biosynthesis by cobalt protoporphyrin.
Mouse Friend virus-transformed erythroleukemia cells in culture undergo erythroid differentiation when treated with a variety of compounds including iron protoporphyrin IX, i.e. hemin. Exogenous hemin is not only incorporated into hemoglobin in these cells but also stimulates heme biosynthesis (Granick, J. L., and Sassa, S. (1978) J. Biol. Chem. 253, 5402-5406). In this study, we examined whether metalloporphyrins other than hemin can also induce differentiation, and if so, whether they can also be incorporated into hemoglobin. Among eight metalloporphyrins examined in culture of these cells, i.e. Co, Mn, Cu, Mg, Ni, Zn, Sn, and Cd protoporphyrin IX, only Co protoporphyrin (10(-4) M) was found to significantly increase the biosynthesis of heme and hemoglobin. In contrast to hemin-mediated induction of erythroid differentiation, Co protoporphyrin was not incorporated into hemoglobin in Friend cells. These data indicate that Co protoporphyrin induces the formation of heme and hemoglobin in Friend cells and that these increases are due to the enhancement of heme biosynthetic activity.
D000818:Animals; D002472:Cell Transformation, Viral; D005622:Friend murine leukemia virus / Q000235:genetics*; D006418:Heme / Q000096:biosynthesis* / Q000378:metabolism; D006419:Heme Oxygenase (Decyclizing) / Q000378:metabolism; D006454:Hemoglobins / Q000096:biosynthesis*; D007700:Kinetics; D007942:Leukemia, Experimental / Q000378:metabolism*; D051379:Mice; D011166:Porphyrins / Q000494:pharmacology*; D011524:Protoporphyrins / Q000494:pharmacology*
D006454:Hemoglobins; D011166:Porphyrins; D011524:Protoporphyrins; D006418:Heme; C007095:cobaltiprotoporphyrin; D006419:Heme Oxygenase (Decyclizing)