An Iron-Regulated Ferric Reductase Associated with the Absorption of Dietary Iron

  • Andrew T. McKie
    Department of Molecular Medicine, Guy's, King's and St. Thomas' School of Medicine, King's College London, Rayne Institute, Denmark Hill Campus, 123 Coldharbour Lane, London SE5 9NU, UK.
  • Dalna Barrow
    Department of Molecular Medicine, Guy's, King's and St. Thomas' School of Medicine, King's College London, Rayne Institute, Denmark Hill Campus, 123 Coldharbour Lane, London SE5 9NU, UK.
  • Gladys O. Latunde-Dada
    Department of Molecular Medicine, Guy's, King's and St. Thomas' School of Medicine, King's College London, Rayne Institute, Denmark Hill Campus, 123 Coldharbour Lane, London SE5 9NU, UK.
  • Andreas Rolfs
    Membrane Biology Program, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.
  • Giamal Sager
    Department of Clinical Biochemistry,
  • Elida Mudaly
    Department of Clinical Biochemistry,
  • Melitta Mudaly
    Department of Clinical Biochemistry,
  • Christopher Richardson
    Department of Pharmacy, King's College London, Franklin-Wilkins Building, Waterloo Campus, 150 Stamford Street, London SE1 8WA, UK.
  • David Barlow
    Department of Pharmacy, King's College London, Franklin-Wilkins Building, Waterloo Campus, 150 Stamford Street, London SE1 8WA, UK.
  • Adrian Bomford
    Institute of Liver Studies, Guy's, King's and St. Thomas' School of Medicine, King's College London, Denmark Hill Campus, Bessemer Road, London SE5 9PJ, UK.
  • Timothy J. Peters
    Department of Clinical Biochemistry,
  • Kishor B. Raja
    Department of Clinical Biochemistry,
  • Sima Shirali
    Department of Clinical Biochemistry,
  • Matthias A. Hediger
    Membrane Biology Program, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.
  • Farzin Farzaneh
    Department of Molecular Medicine, Guy's, King's and St. Thomas' School of Medicine, King's College London, Rayne Institute, Denmark Hill Campus, 123 Coldharbour Lane, London SE5 9NU, UK.
  • Robert J. Simpson
    Department of Clinical Biochemistry,

抄録

<jats:p> The ability of intestinal mucosa to absorb dietary ferric iron is attributed to the presence of a brush-border membrane reductase activity that displays adaptive responses to iron status. We have isolated a complementary DNA, Dcytb (for duodenal cytochrome b), which encoded a putative plasma membrane di-heme protein in mouse duodenal mucosa. Dcytb shared between 45 and 50% similarity to the cytochrome b561 family of plasma membrane reductases, was highly expressed in the brush-border membrane of duodenal enterocytes, and induced ferric reductase activity when expressed in <jats:italic>Xenopus</jats:italic> oocytes and cultured cells. Duodenal expression levels of Dcytb messenger RNA and protein were regulated by changes in physiological modulators of iron absorption. Thus, Dcytb provides an important element in the iron absorption pathway. </jats:p>

収録刊行物

  • Science

    Science 291 (5509), 1755-1759, 2001-03-02

    American Association for the Advancement of Science (AAAS)

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