Andrew T. McKie

TL;DR: The isolation and characterization of a novel cDNA (Ireg1) encoding a duodenal protein that is localized to the basolateral membrane of polarized epithelial cells are described and it is concluded that IREG1 represents the long-sought duodental iron export protein and is upregulated in the iron overload disease, hereditary hemochromatosis.

TL;DR: A complementary DNA, Dcytb (for duodenal cytochrome b), was isolated, which encoded a putative plasma membrane di-heme protein in mouse duodensal mucosa, and provides an important element in the iron absorption pathway.

TL;DR: 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 and is indicated to be the long-sought intestinal heme transporter.

TL;DR: Both hepcidin expression and iron absorption can be regulated before iron stores and erythropoiesis are affected, and transferrin saturation may signal such changes.