Pflügers Archiv

, Volume 451, Issue 4, pp 511–517

The molecular basis of neutral aminoacidurias


  • Angelika Bröer
    • School of Biochemistry and Molecular BiologyAustralian National University
  • Juleen A. Cavanaugh
    • Medical Genetics Research Unit, ANU Medical SchoolThe Canberra Hospital
  • John E. J. Rasko
    • Gene and Stem Cell Therapy, Centenary Institute of Cancer Medicine and Cell BiologyUniversity of Sydney and Sydney Cancer Centre, Royal Prince Alfred Hospital
    • School of Biochemistry and Molecular BiologyAustralian National University
Invited Review

DOI: 10.1007/s00424-005-1481-8

Cite this article as:
Bröer, A., Cavanaugh, J.A., Rasko, J.E.J. et al. Pflugers Arch - Eur J Physiol (2006) 451: 511. doi:10.1007/s00424-005-1481-8


Recent success in the molecular cloning and identification of apical neutral amino acid transporters has shed a new light on inherited neutral amino acidurias, such as Hartnup disorder and Iminoglycinuria. Hartnup disorder is caused by mutations in the neutral amino acid transporter B0 AT1 (SLC6A19). The transporter is found in kidney and intestine, where it is involved in the resorption of all neutral amino acids. The molecular defect underlying Iminoglycinuria has not yet been identified. However, two transporters, the proton amino acid transporter PAT1 (SLC36A1) and the IMINO transporter (SLC6A20) appear to play key roles in the resorption of glycine and proline. A model is presented, involving all three transporters that can explain the phenotypic variability of iminoglycinuria.


IminoglycinuriaHartnup disorderSLC6A19SLC6A20SLC36A1 neurotransmitter transporterProton amino acid transporter

Copyright information

© Springer-Verlag 2005