Open AccessIdentification of Proton‐Coupled High‐Affinity Human Intestinal Folate Transporter Mutated in Human Hereditary Familial Folate Malabsorption
Author(s) -
Wolf George
Publication year - 2007
Publication title -
nutrition reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.958
H-Index - 150
eISSN - 1753-4887
pISSN - 0029-6643
DOI - 10.1111/j.1753-4887.2007.tb00281.x
Subject(s) - transporter , brush border , biology , malabsorption , biochemistry , exon , solute carrier family , gene , membrane transport protein , mutation , atp binding cassette transporter , genetics , microbiology and biotechnology , endocrinology , membrane , vesicle
The human folate transporter of the small intestine has been identified and characterized. It functions optimally at the lowpH (6.0–6.2) characteristic of the micro environment of the duodenal brush border membrane, where dietary folates are mainly absorbed. The transporter, named PCFT/HCP1, is a protein of approximately 50 kDa and functions as a reversible, electrogenic, proton‐coupled high‐affinity folate transporter (PCFT). It shows high specificity for fo‐lates and anti‐folates. This protein was previously identified as an intestinal heme carrier protein HCP1. Patients suffering from hereditary familial folate malabsorption were found to be homozygous for a mutation of the PCFT/HCP1 gene due to loss of a particular exon coding for 28 amino acids.