P-Glycoprotein and Breast Cancer Resistance Protein Restrict Apical-to-Basolateral Permeability of Human Brain Endothelium to Amyloid-β | Zendy

Leon M. Tai | Zendy; Jane Loughlin | Zendy; David Male | Zendy; Ignacio A. Romero | Zendy

Open Access

P-Glycoprotein and Breast Cancer Resistance Protein Restrict Apical-to-Basolateral Permeability of Human Brain Endothelium to Amyloid-β

Author(s) -

Leon M. Tai,

Jane Loughlin,

David Male,

Ignacio A. Romero

Publication year - 2009

Publication title -

journal of cerebral blood flow and metabolism

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.167

H-Index - 193

eISSN - 1559-7016

pISSN - 0271-678X

DOI - 10.1038/jcbfm.2009.42

Subject(s) - abcg2 , p glycoprotein , blood–brain barrier , vascular permeability , cancer research , endothelium , human brain , adenosine , pharmacology , medicine , transporter , microbiology and biotechnology , atp binding cassette transporter , pathology , neuroscience , chemistry , biology , biochemistry , multiple drug resistance , central nervous system , gene , antibiotics

The clearance of amyloid beta (Abeta) from the brain represents a novel therapeutic target for Alzheimer's disease. Conflicting data exist regarding the contribution of adenosine triphosphate-binding cassette transporters to the clearance of Abeta through the blood-brain barrier. Therefore, we investigated whether Abeta could be a substrate for P-glycoprotein (P-gp) and/or for breast cancer resistance protein (BCRP) using a human brain endothelial cell line, hCMEC/D3. Inhibition of P-gp and BCRP increased apical-to-basolateral, but not basolateral-to-apical, permeability of hCMEC/D3 cells to (125)I Abeta 1-40. Our in vitro data suggest that P-gp and BCRP might act to prevent the blood-borne Abeta 1-40 from entering the brain.

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