Cited by 192Amino Acid Enzymes and MetabolismBarrier Structure and Function StudiesIon Transport and Channel Regulation

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Glutamine transport by the blood-brain barrier: a possible mechanism for nitrogen removal

Lee, Wha-Joon, Hawkins, Richard A., Viña, Juan R., Peterson, Darryl R.·1998·American Journal of Physiology-Cell Physiology

DOI 10.1152/ajpcell.1998.274.4.c1101

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Abstract

Glutamine and glutamate transport activities were measured in isolated luminal and abluminal plasma membrane vesicles derived from bovine brain endothelial cells. Facilitative systems for glutamine and glutamate were almost exclusively located in luminal-enriched membranes. The facilitative glutamine carrier was neither sensitive to 2-aminobicyclo(2,2,1)heptane-2-carboxylic acid inhibition nor did it participate in accelerated amino acid exchange; it therefore appeared to be distinct from the neutral amino acid transport system L1. Two Na-dependent glutamine transporters were found in abluminal-enriched membranes: systems A and N. System N accounted for ∼80% of Na-dependent glutamine transport at 100 μM. Abluminal-enriched membranes showed Na-dependent glutamate transport activity. The presence of 1) Na-dependent carriers capable of pumping glutamine and glutamate from brain into endothelial cells, 2) glutaminase within endothelial cells to hydrolyze glutamine to glutamate and ammonia, and 3) facilitative carriers for glutamine and glutamate at the luminal membrane may provide a mechanism for removing nitrogen and nitrogen-rich amino acids from brain.

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BindingDB Entry 50032114: Monocarboxylate transporter MCT1 is a target for immunosuppression.
BindingDB (2011) · UC San Diego · doi:10.7270/q2mc9063

Authors: Lee, W.-J., Hawkins, R. A., Viña, J. R., & Peterson, D. R.
Affiliations: Department of Physiology and Biophysics, Finch University of Health Science/The Chicago Medical School, North Chicago, Illinois 60064-3095; and
Departamento de Bioquı́mica y Biologı́a Molecular, Facultades de Medicina y Farmacia, Universitat de Valencia, Valencia 46010, Spain
ORCID: Hawkins, Richard A.
Venue: American Journal of Physiology-Cell Physiology
Publisher: American Physiological Society
Published: 1998-04-01
Volume: 274
Issue: 4
Pages: C1101-C1107
ISSN: 0363-6143 (ISSN-L)
1522-1563
DOI: 10.1152/ajpcell.1998.274.4.c1101
OpenAlex: W2243408637
Cited by: 191
References: 37
Citations by year: 2026: 3 · 2025: 3 · 2024: 5 · 2023: 2 · 2022: 5 · 2021: 14 · 2020: 7 · 2019: 7 · 2018: 4 · 2017: 9 · 2016: 6 · 2015: 3 · 2014: 7 · 2013: 6 · 2012: 6
FWCI: 5.21
Type: journal article
Language: en
Open access: closed
Locations: American Journal of Physiology-Cell Physiology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01ns031017-03, 5r01ns016389-15)
National Institute of Neurological Disorders and Stroke (NS-31017, NS16389)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
Keywords: glutamine transport, blood-brain barrier, glutamate uptake, brain endothelial cells, nitrogen removal, glutaminase, sodium-dependent transport, plasma membrane vesicles, system N, system A, ammonia removal, amino acid substitutions
MeSH terms: Animals, Biological Transport, Blood-Brain Barrier, Brain, Cattle, Cell Membrane, Endothelium, Vascular, Glutaminase, Glutamine, Nitrogen, Sodium, Glutamic Acid

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Glutamine transport by the blood-brain barrier: a possible mechanism for nitrogen removal

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