Cellular and Molecular Life Sciences CMLS

, Volume 57, Issue 5, pp 754–778

Structure and function of eukaryotic peptide transporters

  • D. Meredith*
  • C. A. R. Boyd

DOI: 10.1007/s000180050040

Cite this article as:
Meredith*, D. & Boyd, C. CMLS, Cell. Mol. Life Sci. (2000) 57: 754. doi:10.1007/s000180050040

Abstract.

The cotransport of protons and peptides is now recognised as a major route by which dietary nitrogen is absorbed from the intestine, and filtered protein reabsorbed in the kidney. Recently, molecular biology has had a very substantial impact on the study of peptide transport, and here we review the molecular and functional information available within the framework of physiology. To this end we consider not only the mammalian peptide transporters and their tissue distribution and regulation but also those from other species (including Caenorhabditis elegans) which make up the proton-dependent oligopeptide transport superfamily. In addition, understanding the binding requirements for transported substrates may allow future design and targeted tissue delivery of peptide and peptidomimetic drugs. Finally, we aim to highlight some of the less well understood areas of peptide transport, in the hope that it will stimulate further research into this challenging yet exciting topic.

Key words. PepT1; PepT2; epithelia; β-lactam antibiotics; PTR2; oligopeptide transport; apical membrane; basolateral membrane. 

Copyright information

© Birkhäuser Verlag Basel, 2000

Authors and Affiliations

  • D. Meredith*
    • 1
  • C. A. R. Boyd
    • 2
  1. 1.Department of Biochemistry, University of Bristol, School of Medical Sciences, University Walk, Bristol BS8 1TD (United Kingdom) Fax 44 117 928 8274, e-mail: david.meredith@bristol.ac.ukGB
  2. 2.Department of Human Anatomy and Genetics, University of Oxford, South Parks Road, Oxford, OX1 3QX (United Kingdom), Fax 44 1865 272420, e-mail: richard.boyd@human-anatomy.ox.ac.uk GB

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