Fractionation of erytroblasts with affinitymediated modifications of their electrical properties using counter-current distribution |
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| Authors: | Jesús Mendieta Göte Johansson |
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| Affiliation: | (1) Departments of Medicine, Biochemistry and Molecular Biology, University of Massachusetts Medical School, 01655 Worcester, MA, USA;(2) Center for Study of Disorders of Iron and Porphyrin Metabolism, University of Massachusetts Medical School, 01655 Worcester, MA, USA;(3) Division of Digestive Disease and Nutrition, University of Massachusetts Medical Center, 01655 Worcester, MA, USA |
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| Abstract: | Enterally administered, heme is a good source of iron in humans and other animals, but the metabolism of heme by enterocytes has not been fully characterized. Caco-2 cells in culture provide a useful model for studying cells that resemble small intestinal epithelium, both morphologically and functionally. In this paper we show that heme oxygenase, the rate-controlling enzyme of heme catabolism, is present in abundance in Caco-2 cells, and that levels of its mRNA and activity can be increased by exposure of the cells to heme or metal ions (cadmium, cobalt). Caco-2 cells also contain biliverdin reductase activity which, in the basal state, is similar to that of heme oxygenase (approximately 40 pmole of product per mg protein per minute); however, when heme oxygenase is induced, biliverdin reductase may become rate-limiting for bilirubin production.Abbreviations BVR biliverdin reductase - DMEM Dulbecco's modified Eagles medium - DMSO dimethyl sulfoxide - HO heme oxygenase - 1xSSC a solution of 0.015 M sodium citrate/0.15 sodium chloride |
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| Keywords: | biliverdin reductase Caco-2 cells heme heme oxygenase intestinal cells |
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