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Dietary heme iron is an important nutritional source of iron in carnivores and omnivores that is more readily absorbed than non-heme iron derived from vegetables and grain. Most heme is absorbed in the proximal intestine, with absorptive capacity decreasing distally. We utilized a subtractive hybridization approach to isolate a heme transporter from duodenum by taking advantage of the intestinal gradient for heme absorption. Here we show a membrane protein named HCP 1 (heme carrier protein 1), with homology to bacterial metal-tetracycline transporters, mediates heme uptake by cells in a temperature-dependent and saturable manner. HCP 1 mRNA was highly expressed in duodenum and regulated by hypoxia. HCP 1 protein was iron regulated and localized to the brush-border membrane of duodenal enterocytes in iron deficiency. Our data indicate that HCP 1 is the long-sought intestinal heme transporter.

Original publication

DOI

10.1016/j.cell.2005.06.025

Type

Journal article

Journal

Cell

Publication Date

09/2005

Volume

122

Pages

789 - 801

Addresses

Department of Life Sciences, Nutritional Sciences Research Division, Franklin-Wilkins Building, Kings College London, 150 Stamford Street, London SE1 9NN, UK.

Keywords

Duodenum, Oocytes, Hela Cells, CHO Cells, Epithelial Cells, Animals, Xenopus, Zebrafish, Rabbits, Humans, Mice, Rats, Iron, Heme, Bacterial Proteins, Transferrin, Carrier Proteins, Membrane Transport Proteins, RNA, Messenger, Cloning, Molecular, Sequence Alignment, Amino Acid Sequence, Intestinal Absorption, Molecular Sequence Data, Cricetinae, Proton-Coupled Folate Transporter, Hypoxia