Cited by 314Barrier Structure and Function StudiesDrug Transport and Resistance MechanismsIon Transport and Channel Regulation

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Blood-brain barrier glucose transporter is asymmetrically distributed on brain capillary endothelial lumenal and ablumenal membranes: an electron microscopic immunogold study.

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Farrell, C L, Pardridge, W M·1991·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.88.13.5779PMC PMC51961

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Abstract

It is generally assumed that there is symmetric distribution of the glucose transporter on the lumenal and ablumenal membranes of the brain capillary endothelial cell that makes up the blood-brain barrier (BBB) in vivo. However, the presence of brain endothelial tight junctions allows for asymmetric distribution of BBB plasma membrane proteins. Glucose transporter isoform 1 (GLUT-1), the principal glucose transporter at the BBB, was assessed in rat brain in the present studies using immunogold electron microscopy. The distribution of the immunoreactive GLUT-1 protein on the endothelial lumenal membrane, the ablumenal membrane, and the cytoplasmic compartment was 12%, 48%, and 40%, respectively, and no significant immunolabeling of the neuropil was measurable. These studies suggest (i) that GLUT-1 is asymmetrically distributed on the BBB plasma membrane with an approximately 4-fold greater abundance on the ablumenal membrane as compared to the lumenal membrane; (ii) that approximately 40% of the endothelial glucose transporter protein is contained within the cytoplasmic space, which provides a mechanism for rapid up-regulation of the transporter by altered distribution of transporter between cytoplasmic and plasma membrane compartments; and (iii) that no significant labeling of neuropil is found with antisera directed against the GLUT-1 protein. These studies also suggest mechanisms of regulation of glucose transport from blood to brain that involve differential distribution of the BBB glucose transporter in subcellular compartments of brain capillary endothelial cells.

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Authors: Farrell, C. L., & Pardridge, W. M.
Affiliations: University of California, Los Angeles (US)
ORCID: Pardridge, W M
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 1991-07
Volume: 88
Issue: 13
Pages: 5779-5783
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.88.13.5779
PMC: PMC51961
OpenAlex: W1985944040
Cited by: 314
References: 32
Citations by year: 2026: 2 · 2025: 3 · 2024: 7 · 2023: 4 · 2022: 9 · 2021: 6 · 2020: 9 · 2019: 5 · 2018: 12 · 2017: 8 · 2016: 11 · 2015: 11 · 2014: 11 · 2013: 3 · 2012: 9
FWCI: 8.20
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5p01ns025554-08)
National Institute of Neurological Disorders and Stroke (P01-NS-25554)
Topics: Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
Keywords: blood-brain barrier, GLUT1, glucose transporters, brain microvascular endothelial cells, tight junctions, subcellular localization, glucose transport regulation, cytoplasmic compartments, rat brain
MeSH terms: Animals, Blood-Brain Barrier, Brain, Cell Compartmentation, Cell Membrane, Endothelium, Vascular, Immunohistochemistry, Microscopy, Electron, Monosaccharide Transport Proteins, Rats

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Blood-brain barrier glucose transporter is asymmetrically distributed on brain capillary endothelial lumenal and ablumenal membranes: an electron microscopic immunogold study.

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