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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




Journal article



Publication Date





789 - 801


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