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Cited by 106Barrier Structure and Function StudiesAmino Acid Enzymes and MetabolismDrug Transport and Resistance Mechanisms

The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.

Na+-dependent transport of large neutral amino acids occurs at the abluminal membrane of the blood-brain barrier

O'Kane, Robyn L., Hawkins, Richard A.·2003·American Journal of Physiology-Endocrinology and Metabolism
DOI 10.1152/ajpendo.00193.2003
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Abstract

Several Na+-dependent carriers of amino acids exist on the abluminal membrane of the blood-brain barrier (BBB). These Na+-dependent carriers are in a position to transfer amino acids from the extracellular fluid of brain to the endothelial cells and thence to the circulation. To date, carriers have been found that may remove nonessential, nitrogen-rich, or acidic (excitatory) amino acids, all of which may be detrimental to brain function. We describe here Na+-dependent transport of large neutral amino acids across the abluminal membrane of the BBB that cannot be ascribed to currently known systems. Fresh brains, from cows killed for food, were used. Microvessels were isolated, and contaminating fragments of basement membranes, astrocyte fragments, and pericytes were removed. Abluminal-enriched membrane fractions from these microvessels were prepared. Transport was Na+ dependent, voltage sensitive, and inhibited by 2-aminobicyclo-(2,2,1)-heptane-2-carboxylic acid, a particular inhibitor of the facilitative large neutral amino acid transporter 1 (LAT1) system. The carrier has a high affinity for leucine (Km 21 +/- 7 microM) and is inhibited by other neutral amino acids, including glutamine, histidine, methionine, phenylalanine, serine, threonine, tryptophan, and tyrosine. Other established neutral amino acids may enter the brain by way of LAT1-type facilitative transport. The presence of a Na+-dependent carrier on the abluminal membrane capable of removing large neutral amino a…

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Crossref · 10.1152/ajpendo.00193.2003

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Metadata

Authors
O'Kane, R. L., & Hawkins, R. A.
Affiliations
  • Department of Physiology and Biophysics, Finch University of Health Sciences/The Chicago Medical School, North Chicago, Illinois 60064
  • Rosalind Franklin University of Medicine and Science (US)
ORCID
Hawkins, Richard A.
Venue
American Journal of Physiology-Endocrinology and Metabolism
Publisher
American Physiological Society
Published
2003-12
Volume
285
Issue
6
Pages
E1167-E1173
ISSN
  • 0193-1849 (ISSN-L)
  • 1522-1555
DOI
10.1152/ajpendo.00193.2003
OpenAlex
W2141267676
Cited by
105
References
55
Citations by year
2026: 1 · 2025: 5 · 2024: 5 · 2023: 1 · 2022: 3 · 2021: 8 · 2020: 6 · 2019: 3 · 2018: 3 · 2017: 4 · 2016: 10 · 2015: 6 · 2014: 5 · 2013: 1 · 2012: 3
FWCI
3.43
Type
journal article
Language
en
Open access
closed
Locations
  • American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute of Neurological Disorders and Stroke (R01NS041405, NS-041405)
Topics
  • Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
  • Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
Keywords
blood-brain barrier, Na+-dependent amino acid transport, large neutral amino acids, LAT1, amino acid transporters, leucine, essential amino acids, excitatory amino acids, endothelial cells
MeSH terms
Amino Acids, Essential, Animals, Biological Transport, Active, Blood-Brain Barrier, Capillary Permeability, Cattle, Cell Membrane, Cell Membrane Permeability, Cells, Cultured, Endothelium, Vascular, Sodium, Extracellular Fluid

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