Cited by 662Alzheimer's disease research and treatmentsDrug Transport and Resistance MechanismsBarrier Structure and Function Studies

The DOI matches its Crossref record; 33 of the 34 references it cites were found in a registry or an index.

P-glycoprotein deficiency at the blood-brain barrier increases amyloid- deposition in an Alzheimer disease mouse model

Open access

Cirrito, J. R.·2005·Journal of Clinical Investigation

DOI 10.1172/jci25247PMC PMC1257538

Open this paper in CoChat — free account Open PDF

Abstract

Accumulation of amyloid-beta (Abeta) within extracellular spaces of the brain is a hallmark of Alzheimer disease (AD). In sporadic, late-onset AD, there is little evidence for increased Abeta production, suggesting that decreased elimination from the brain may contribute to elevated levels of Abeta and plaque formation. Efflux transport of Abeta across the blood-brain barrier (BBB) contributes to Abeta removal from the brain. P-glycoprotein (Pgp) is highly expressed on the luminal surface of brain capillary endothelial cells and contributes to the BBB. In Pgp-null mice, we show that [I]Abeta40 and [I]Abeta42 microinjected into the CNS clear at half the rate that they do in WT mice. When amyloid precursor protein-transgenic (APP-transgenic) mice were administered a Pgp inhibitor, Abeta levels within the brain interstitial fluid significantly increased within hours of treatment. Furthermore, APP-transgenic, Pgp-null mice had increased levels of brain Abeta and enhanced Abeta deposition compared with APP-transgenic, Pgp WT mice. These data establish a direct link between Pgp and Abeta metabolism in vivo and suggest that Pgp activity at the BBB could affect risk for developing AD as well as provide a novel diagnostic and therapeutic target.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1172/jci25247

Cites

33 of 33 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Multidrug resistance in cancer: role of ATP–dependent transporters
Gottesman, M. M., Fojo, T., & Bates, S. E. (2002) · Nature Reviews Cancer · doi:10.1038/nrc706 · Cited by 5,536
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
Functional polymorphisms of the human multidrug-resistance gene: Multiple sequence variations and correlation of one allele with P-glycoprotein expression and activity in vivo
Hoffmeyer, S., Burk, O., von Richter, O., Arnold, H., Brockmöller, J., Johne, A., Cascorbi, I., Gerloff, T., Roots, I., Eichelbaum, M. F., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.7.3473 · Cited by 2,366
Disruption of the mouse mdr1a P-glycoprotein gene leads to a deficiency in the blood-brain barrier and to increased sensitivity to drugs
Schinkel, A. H., Smit, J., van Tellingen, O., Beijnen, J. H., Wagenaar, E., van Deemter, L., Mol, C. A. A. M., van der Valk, M. A., Robanus-Maandag, E. C., Riele, H. T., et al. (1994) · Cell · doi:10.1016/0092-8674(94)90212-7 · Cited by 2,284
BIOCHEMICAL, CELLULAR, AND PHARMACOLOGICAL ASPECTS OF THE MULTIDRUG TRANSPORTER
Ambudkar, S. V., Dey, S., Hrycyna, C. A., Ramachandra, M., Pastan, I. H., & Gottesman, M. M. (1999) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.39.1.361 · Cited by 2,059
Insulin-degrading enzyme regulates the levels of insulin, amyloid β-protein, and the β-amyloid precursor protein intracellular domain in vivo
Farris, W., Mansourian, S., Chang, Y., Lindsley, L., Eckman, E. A., Frosch, M. P., Eckman, C. B., Tanzi, R. E., Selkoe, D. J., & Guénette, S. Y. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0230450100 · Cited by 1,526
RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain
Deane, R., Du Yan, S., Submamaryan, R. K., LaRue, B., Jovanovic, S., Hogg, E., Welch, D., Manness, L., Lin, C., Yu, J., et al. (2003) · Nature Medicine · doi:10.1038/nm890 · Cited by 1,426
Clearance of Alzheimer’s amyloid-β1-40 peptide from brain by LDL receptor–related protein-1 at the blood-brain barrier
Shibata, M., Yamada, S., Kumar, S. R., Calero, M., Bading, J., Frangione, B., Holtzman, D. M., Miller, C. A., Strickland, D. K., Ghiso, J., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10498 · Cited by 1,413
Polymorphisms in human MDR1 (P-glycoprotein): recent advances and clinical relevance
Marzolini, C. (2004) · Clinical Pharmacology & Therapeutics · doi:10.1016/j.clpt.2003.09.012 · Cited by 907
Lack of apolipoprotein E dramatically reduces amyloid β-peptide deposition
Bales, K. R., Verina, T., Dodel, R. C., Du, Y., Altstiel, L., Bender, M., Hyslop, P., Johnstone, E. M., Little, S. P., Cummins, D. J., et al. (1997) · Nature Genetics · doi:10.1038/ng1197-263 · Cited by 830

Show all 34 references

Sorted by citations

Items 101–200 of 662

A circadian clock regulates efflux by the blood-brain barrier in mice and human cells
Zhang, S., Lahens, N. F., Yue, Z., Arnold, D. M., Pakstis, P. P., Schwarz, J. E., & Sehgal, A. (2021) · Nature Communications · doi:10.1038/s41467-020-20795-9 · Cited by 163
New Therapeutic Targets in the Neurovascular Pathway in Alzheimer's Disease
Zloković, B. V. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.05.011 · Cited by 153
Differences in amyloid-β clearance across mouse and human blood–brain barrier models: Kinetic analysis and mechanistic modeling
Qosa, H., Abuasal, B. S., Romero, I. A., Weksler, B., Couraud, P.-O., Keller, J. N., & Kaddoumi, A. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.01.023 · Cited by 146
Ushering in the study and treatment of preclinical Alzheimer disease
Langbaum, J. B. S., Fleisher, A., Chen, K., Ayutyanont, N., Lopera, F. J., Quiroz, Y. T., Caselli, R. J., Tariot, P. N., & Reiman, E. M. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2013.107 · Cited by 149
Lipopolysaccharide impairs amyloid beta efflux from brain: altered vascular sequestration, cerebrospinal fluid reabsorption, peripheral clearance and transporter function at the blood–brain barrier
Erickson, M. A., Hartvigson, P. E., Morofuji, Y., Owen, J. B., Butterfield, D. A., & Banks, W. A. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-150 · Cited by 145
Therapeutic Potential of γ -Secretase Inhibitors and Modulators
Imbimbo, B. (2008) · Current Topics in Medicinal Chemistry · doi:10.2174/156802608783334015 · Cited by 143
Neurovascular Defects and Faulty Amyloid-β Vascular Clearance in Alzheimer's Disease
Sagare, A. P., Bell, R. D., & Zloković, B. V. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129037 · Cited by 152
Low-density lipoprotein receptor-related protein 1: A physiological Aβ homeostatic mechanism with multiple therapeutic opportunities
Sagare, A. P., Deane, R., & Zloković, B. V. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.07.008 · Cited by 150
The concerted amyloid-beta clearance of LRP1 and ABCB1/P-gp across the blood-brain barrier is linked by PICALM
Storck, S. E., Hartz, A. M. S., Bernard, J., Wolf, A., Kachlmeier, A., Mahringer, A., Weggen, S., Pahnke, J., & Pietrzik, C. U. (2018) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2018.07.017 · Cited by 143
Pericyte-derived Glial Cell Line-derived Neurotrophic Factor Increase the Expression of Claudin-5 in the Blood–brain Barrier and the Blood-nerve Barrier
Shimizu, F., Sano, Y., Saito, K., Abe, M., Maeda, T., Haruki, H., & Kanda, T. (2011) · Neurochemical Research · doi:10.1007/s11064-011-0626-8 · Cited by 144
Regulation of ABC Transporters Blood–Brain Barrier
Miller, D. S. (2015) · Advances in cancer research · doi:10.1016/bs.acr.2014.10.002 · Cited by 146
From Stroke to Dementia: a Comprehensive Review Exposing Tight Interactions Between Stroke and Amyloid-β Formation
Goulay, R., Romo, L. M., Hol, E. M., & Dijkhuizen, R. M. (2019) · Translational Stroke Research · doi:10.1007/s12975-019-00755-2 · Cited by 144
Pathophysiology of the lymphatic drainage of the central nervous system: Implications for pathogenesis and therapy of multiple sclerosis
Weller, R. O., Galea, I., Carare, R. O., & Minagar, A. (2009) · Pathophysiology · doi:10.1016/j.pathophys.2009.10.007 · Cited by 146
Cerebrovascular Dysfunction in Amyloid Precursor Protein Transgenic Mice: Contribution of Soluble and Insoluble Amyloid-β Peptide, Partial Restoration via γ-Secretase Inhibition
Han, B. H., Zhou, M.-L., Abousaleh, F., Brendza, R. P., Dietrich, H. H., Koenigsknecht-Talboo, J., Cirrito, J. R., Milner, E., Holtzman, D. M., & Zipfel, G. J. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4686-08.2008 · Cited by 138
Self-citation
Antidiabetic drugs restore abnormal transport of amyloid-β across the blood–brain barrier and memory impairment in db/db mice
Chen, F., Dong, R. R., Zhong, K. L., Ghosh, A., Tang, S. S., Long, Y., Hu, M. Y., Miao, M. X., Liao, J. M., Sun, H. B., et al. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.07.023 · Cited by 137
Chronic cerebrovascular dysfunction after traumatic brain injury
Jullienne, A., Obenaus, A., Ichkova, A., Savona‐Baron, C., Pearce, W. J., & Badaut, J. (2016) · Journal of Neuroscience Research · doi:10.1002/jnr.23732 · Cited by 141
Role of ABC Transporters in the Pathogenesis of Alzheimer’s Disease
Abuznait, A. H., & Kaddoumi, A. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn300077c · Cited by 145
ABC efflux transporters in brain vasculature of Alzheimer's subjects
Wijesuriya, H. C., Bullock, J. Y., Faull, R. L. M., Hladky, S. B., & Barrand, M. A. (2010) · Brain Research · doi:10.1016/j.brainres.2010.08.034 · Cited by 141
Critical review: involvement of endoplasmic reticulum stress in the aetiology of Alzheimer's disease
Hashimoto, S., & Saido, T. C. (2018) · Open Biology · doi:10.1098/rsob.180024 · Cited by 129
Concentration-Dependent Modulation of Amyloid-β in Vivo and in Vitro Using the γ-Secretase Inhibitor, LY-450139
Lanz, T. A., Karmilowicz, M. J., Wood, K. M., Pozdnyakov, N., Du, P., Piotrowski, M. A., Brown, T. M., Nolan, C. E., Richter, K. E. G., Finley, J. E., et al. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.110700 · Cited by 130
The role of amyloid-beta in the regulation of memory
Morley, J. E., & Farr, S. A. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.018 · Cited by 140
P-glycoprotein expression and amyloid accumulation in human aging and Alzheimer's disease: preliminary observations
Chiu, C., Miller, M. C., Monahan, R., Osgood, D. P., Stopa, E. G., & Silverberg, G. D. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.05.020 · Cited by 134
Blood-brain barrier integrity in the pathogenesis of Alzheimer’s disease
Huang, Z., Wong, L., Su, Y., Huang, X., Wang, N., Chen, H., & Yi, C. (2020) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2020.100857 · Cited by 135
Assessment of the blood–brain barrier in CNS drug discovery
Jeffrey, P., & Summerfield, S. G. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.07.033 · Cited by 125
Cellular Models and In Vitro Assays for the Screening of modulators of P-gp, MRP1 and BCRP
Gameiro, M., Silva, R. V. D. S., Rocha‐Pereira, C., Carmo, H., Carvalho, F. D., Bastos, M. D. L., & Remião, F. (2017) · Molecules · doi:10.3390/molecules22040600 · Cited by 129
Perspectives of P-Glycoprotein Modulating Agents in Oncology and Neurodegenerative Diseases: Pharmaceutical, Biological, and Diagnostic Potentials
Colabufo, N. A., Berardi, F., Cantore, M., Contino, M., Inglese, C., Niso, M., & Perrone, R. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900743c · Cited by 127
Biomarkers in Alzheimer's disease drug development
Cummings, J. L. (2011) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2010.06.004 · Cited by 122
A Neurovascular Perspective for Long-Term Changes After Brain Trauma
Pop, V., & Badaut, J. (2011) · Translational Stroke Research · doi:10.1007/s12975-011-0126-9 · Cited by 125
Age Drives Distortion of Brain Metabolic, Vascular and Cognitive Functions, and the Gut Microbiome
Hoffman, J. D., Parikh, I. J., Green, S. J., Chlipala, G. E., Mohney, R. P., Keaton, M., Bauer, B., Hartz, A. M. S., & Lin, A. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00298 · Cited by 124
Membrane transporter proteins: a challenge for CNS drug development
Girardin, F. R. (2006) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2006.8.3/fgirardin · Cited by 122
ABC Transporters in the CNS – An Inventory
Hartz, A. M. S., & Bauer, B. (2011) · Current Pharmaceutical Biotechnology · doi:10.2174/138920111795164020 · Cited by 124
P-glycoprotein and ‘lipid rafts’: some ambiguous mutual relationships (floating on them, building them or meeting them by chance?)
Orlowski, S., Martin, S., & Escargueil, A. E. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5554-9 · Cited by 120
ABC Transporters and Drug Efflux at the Blood-Brain Barrier
Shen, S., & Zhang, W. (2010) · Reviews in the Neurosciences · doi:10.1515/revneuro.2010.21.1.29 · Cited by 120
P-Glycoprotein and Breast Cancer Resistance Protein Restrict Apical-to-Basolateral Permeability of Human Brain Endothelium to Amyloid-β
Tai, L. M., Loughlin, A. J., Male, D. K., & Romero, I. A. (2009) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2009.42 · Cited by 108
Establishment of a new conditionally immortalized human brain microvascular endothelial cell line retaining an in vivo blood–brain barrier function
Sano, Y., Shimizu, F., Abe, M., Maeda, T., Kashiwamura, Y., Ohtsuki, S., Terasaki, T., Obinata, M., Kajiwara, K., Fujii, M., et al. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22232 · Cited by 128
Disease modifying therapy for AD?1
Golde, T. E. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04211.x · Cited by 117
Aβ1–42 reduces P-glycoprotein in the blood–brain barrier through RAGE–NF-κB signaling
Park, R., Kook, S.-Y., Park, J.-C., & Mook‐Jung, I. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.258 · Cited by 116
Brain–Immune Interactions and Neuroinflammation After Traumatic Brain Injury
Dinet, V., Petry, K. G., & Badaut, J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01178 · Cited by 119
Blood-Brain Barrier: More Contributor to Disruption of Central Nervous System Homeostasis Than Victim in Neurological Disorders
Xiao, M., Xiao, Z. J., Yang, B., Lan, Z., & Fang, F. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00764 · Cited by 119
Amyloid Deposition and Influx Transporter Expression at the Blood-Brain Barrier Increase in Normal Aging
Silverberg, G. D., Miller, M. C., Messier, A. A., Majmudar, S., Machan, J. T., Donahue, J. E., Stopa, E. G., & Johanson, C. E. (2009) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181c8ad2f · Cited by 111
Targeting specific cells in the brain with nanomedicines for CNS therapies
Zhang, F., Lin, Y.-A., Kannan, S., & Kannan, R. M. (2015) · Journal of Controlled Release · doi:10.1016/j.jconrel.2015.12.013 · Cited by 113
ABCG2- and ABCG4-Mediated Efflux of Amyloid-β Peptide 1-40 at the Mouse Blood-Brain Barrier
Minh, T. N., Noël‐Hudson, M., Ribes, S., Besengez, C., Smirnova, M., Cisternino, S., Buyse, M., Calon, F., Chimini, G., Chacun, H., et al. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-112189 · Cited by 116
Functional characterization of the brain-to-blood efflux clearance of human amyloid-β peptide (1–40) across the rat blood–brain barrier
Ito, S., Ohtsuki, S., & Terasaki, T. (2006) · Neuroscience Research · doi:10.1016/j.neures.2006.07.006 · Cited by 99
Modulating P‐glycoprotein regulation: Future perspectives for pharmacoresistant epilepsies?
Potschka, H. (2010) · Epilepsia · doi:10.1111/j.1528-1167.2010.02585.x · Cited by 108
The role of ABCB1 and ABCA1 in beta-amyloid clearance at the neurovascular unit in Alzheimer's disease
ElAli, A., & Rivest, S. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00045 · Cited by 115
The choroid plexus in health and in disease: dialogues into and out of the brain
Marques, F., Sousa, J. C., Brito, M. A., Pahnke, J., Santos, C. R. A., Correia‐Neves, M., & Palha, J. A. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.08.011 · Cited by 115
Evidence of a Role for Lactadherin in Alzheimer's Disease
Boddaert, J., Kinugawa, K., Lambert, J., Boukhtouche, F., Zoll, J., Merval, R., Blanc‐Brude, O., Mann, D. M. A., Berr, C., Vilar, J., et al. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.060664 · Cited by 108
Regulation of major efflux transporters under inflammatory conditions at the blood‐brain barrierin vitro
von Wedel-Parlow, M., Wölte, P., & Galla, H. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06305.x · Cited by 106
ABC Transporters and the Alzheimer’s Disease Enigma
Wolf, A. M., Bauer, B., & Hartz, A. M. S. (2012) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2012.00054 · Cited by 109
ABCB1 and ABCG2 Regulation at the Blood-Brain Barrier: Potential New Targets to Improve Brain Drug Delivery
Schulz, J., Hartz, A. M. S., & Bauer, B. (2023) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000025 · Cited by 118
Depletion of Vitamin E Increases Amyloid β Accumulation by Decreasing Its Clearances from Brain and Blood in a Mouse Model of Alzheimer Disease
Nishida, Y., Ito, S., Ohtsuki, S., Yamamoto, N., Takahashi, T., Iwata, N., Jishage, K.-I., Yamada, H., Sasaguri, H., Yokota, S., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.054056 · Cited by 106
Rapid, Reversible Modulation of Blood–Brain BarrierP-Glycoprotein Transport Activity by Vascular Endothelial Growth Factor
Hawkins, B. T., Sykes, D. B., & Miller, D. S. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5103-09.2010 · Cited by 107
Blood–brain barrier and blood–cerebrospinal fluid barrier in normal and pathological conditions
Ueno, M., Chiba, Y., Murakami, R., Matsumoto, K., Kawauchi, M., & Fujihara, R. (2016) · Brain Tumor Pathology · doi:10.1007/s10014-016-0255-7 · Cited by 106
The Biological Activities of Oleocanthal from a Molecular Perspective
Pang, K. L., & Chin, K. (2018) · Nutrients · doi:10.3390/nu10050570 · Cited by 101
LRP promotes endocytosis and degradation, but not transcytosis, of the amyloid-β peptide in a blood–brain barrier in vitro model
Nazer, B., Hong, S., & Selkoe, D. J. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.12.005 · Cited by 90
A Role for P-Glycoprotein in Clearance of Alzheimer Amyloid ? -Peptide from the Brain
Wang, W., M. Bodles-Brakhop, A., & W. Barger, S. (2016) · Current Alzheimer Research · doi:10.2174/1567205013666160314151012 · Cited by 107
Aβ40 Reduces P-Glycoprotein at the Blood–Brain Barrier through the Ubiquitin–Proteasome Pathway
Hartz, A. M. S., Zhong, Y., Wolf, A. M., LeVine, H., Miller, D. S., & Bauer, B. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0350-15.2016 · Cited by 100
Crocus sativus Extract Tightens the Blood-Brain Barrier, Reduces Amyloid β Load and Related Toxicity in 5XFAD Mice
Batarseh, Y. S., Bharate, S. S., Kumar, V., Kumar, A., Vishwakarma, R. A., Bharate, S. B., & Kaddoumi, A. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00101 · Cited by 100
Inflammation-induced dysfunction of the low-density lipoprotein receptor-related protein-1 at the blood–brain barrier: Protection by the antioxidant N-acetylcysteine
Erickson, M. A., Hansen, K. M., & Banks, W. A. (2012) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2012.07.003 · Cited by 102
P‐glycoprotein: a role in the export of amyloid‐β in Alzheimer's disease?
Chai, A. B., Leung, G. K. F., Callaghan, R., & Gelissen, I. C. (2019) · FEBS Journal · doi:10.1111/febs.15148 · Cited by 100
Pathophysiology of the Blood–Brain Barrier: Animal Models and Methods
Hawkins, B. T., & Egleton, R. D. (2007) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(07)80007-x · Cited by 101
Is Vasomotion in Cerebral Arteries Impaired in Alzheimer’s Disease?
Marco, L. Y. D., Farkas, E., Martin, C. J., Venneri, A., & Frangi, A. F. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142976 · Cited by 94
Dysfunctional Wnt/β-catenin signaling contributes to blood–brain barrier breakdown in Alzheimer’s disease
Liu, L., Wan, W., Xia, S., Kalionis, B., & Li, Y. (2014) · Neurochemistry International · doi:10.1016/j.neuint.2014.05.004 · Cited by 97
Peptides and proteins in plasma and cerebrospinal fluid as biomarkers for the prediction, diagnosis, and monitoring of therapeutic efficacy of Alzheimer's disease
Aluise, C. D., Robinson, R. A. S., & Butterfield, D. A. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.07.008 · Cited by 94
ABC Transporters Are Key Players in Alzheimer’s Disease
Pereira, C. D., Martins, F., Wiltfang, J., Silva, O. A. B. D. C. E., & Rebelo, S. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170639 · Cited by 94
Brain-Penetrant, Orally Bioavailable Microtubule-Stabilizing Small Molecules Are Potential Candidate Therapeutics for Alzheimer’s Disease and Related Tauopathies
Lou, K., Yao, Y., Hoye, A. T., James, M. J., Cornec, A., Hyde, E. G., Gay, B. C., Lee, V. M. ‐., Trojanowski, J. Q., Smith, A. B., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm5005623 · Cited by 93
Understanding the Pathophysiology of Cerebral Amyloid Angiopathy
Gatti, L., Tinelli, F., Scelzo, E., Arioli, F., Fede, G. D., Obici, L. P., Pantoni, L., Giaccone, G., Caroppo, P., Parati, E. A., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103435 · Cited by 99
The penetration of therapeutics across the blood-brain barrier: Classic case studies and clinical implications
Banks, W. A., Rhea, E. M., Reed, M. J., & Erickson, M. A. (2024) · Cell Reports Medicine · doi:10.1016/j.xcrm.2024.101760 · Cited by 90
Can sleep apnea cause Alzheimer's disease?
Pan, W., & Kastin, A. J. (2014) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2014.10.019 · Cited by 91
Systems proteomic analysis reveals that clusterin and tissue inhibitor of metalloproteinases 3 increase in leptomeningeal arteries affected by cerebral amyloid angiopathy
Manousopoulou, A., Gatherer, M., Smith, C., Nicoll, J. A. R., Woelk, C. H., Johnson, M., Kalaria, R. N., Attems, J., Garbis, S. D., & Carare, R. O. (2016) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12342 · Cited by 90
Brain injury-induced dysfunction of the blood brain barrier as a risk for dementia
Abrahamson, E. E., & Ikonomović, M. D. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113257 · Cited by 91
Genetics of ABCB1 in Cancer
Skinner, K. T., Palkar, A. M., & Hong, A. L. (2023) · Cancers · doi:10.3390/cancers15174236 · Cited by 87
Reduced Alzheimer’s Disease Pathology by St. John’s Wort Treatment is Independent of Hyperforin and Facilitated by ABCC1 and Microglia Activation in Mice
Hofrichter, J., Krohn, M., Schumacher, T., Lange, C., Feistel, B., Walbroel, B., Heinze, H., Crockett, S. L., Sharbel, T. F., & Pahnke, J. (2013) · Current Alzheimer Research · doi:10.2174/15672050113106660171 · Cited by 88
The effects of ABCA1 on cholesterol efflux and Aβ levels in vitro and in vivo
Burns, M. P., Vardanian, L., Pajoohesh‐Ganji, A., Wang, L., Cooper, M., Harris, D. C., Duff, K., & Rebeck, G. W. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03925.x · Cited by 106
The gut microbiome and Alzheimer’s disease: Complex and bidirectional interactions
Tarawneh, R. M., & Penhos, E. (2022) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2022.104814 · Cited by 92
Molecular imaging strategies for drug discovery and development
Gross, S., & Piwnica-Worms, D. R. (2006) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2006.06.028 · Cited by 87
Apolipoprotein E, Amyloid-β, and Blood-Brain Barrier Permeability in Alzheimer Disease
Donahue, J. E., & Johanson, C. E. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31816a0dc8 · Cited by 87
The integrity of the blood?brain barrier in Alzheimer?s disease
Algotsson, A., & Winblad, B. G. (2007) · Acta Neurologica Scandinavica · doi:10.1111/j.1600-0404.2007.00823.x · Cited by 85
Early Brain Injury Alters the Blood–Brain Barrier Phenotype in Parallel with β-Amyloid and Cognitive Changes in Adulthood
Pop, V., Sorensen, D. W., Kamper, J. E., Ajao, D. O., Murphy, M. P., Head, E., Hartman, R. E., & Badaut, J. (2012) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2012.154 · Cited by 89
Vascular Risk Factors and Alzheimer’s Disease: Blood-Brain Barrier Disruption, Metabolic Syndromes, and Molecular Links
He, J., Zhao, X., Xu, L., & Mao, C. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190764 · Cited by 88
Acute sleep loss decreases CSF‐to‐blood clearance of Alzheimer's disease biomarkers
Liu, H., Barthélemy, N. R., Ovod, V., Bollinger, J. G., He, Y., Chahin, S. L., Androff, B., Bateman, R. J., & Lucey, B. P. (2023) · Alzheimer s & Dementia · doi:10.1002/alz.12930 · Cited by 89
Limitations of the hCMEC/D3 cell line as a model for Aβ clearance by the human blood‐brain barrier
Biemans, E. A. L. M., Jäkel, L., de Waal, R. M. W., Kuiperij, H. B., & Verbeek, M. M. (2016) · Journal of Neuroscience Research · doi:10.1002/jnr.23964 · Cited by 86
Synthesis and Evaluation of [N-methyl-11C]N-Desmethyl-loperamide as a New and Improved PET Radiotracer for Imaging P-gp Function
Lazarova, N., Zoghbi, S. S., Hong, J. S., Seneca, N. M., Tuan, E., Gladding, R. L., Liow, J., Taku, A., Innis, R. B., & Pike, V. W. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800510m · Cited by 85
Beta-amyloid pathology in human brain microvessel extracts from the parietal cortex: relation with cerebral amyloid angiopathy and Alzheimer’s disease
Bourassa, P., Tremblay, C., Schneider, J. A., Bennett, D. A., & Calon, F. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-01967-4 · Cited by 80
1α,25‐Dihydroxyvitamin D3‐liganded vitamin D receptor increases expression and transport activity of P‐glycoprotein in isolated rat brain capillaries and human and rat brain microvessel endothelial cells
Durk, M. R., Chan, G. N. Y., Campos, C. R., Peart, J. C., Chow, E. C. Y., Lee, E., Cannon, R. E., Bendayan, R., Miller, D. S., & Pang, K. S. (2012) · Journal of Neurochemistry · doi:10.1111/jnc.12041 · Cited by 83
Neurogenetic basis for circadian regulation of metabolism by the hypothalamusPreprint
Cedernaes, J., Waldeck, N. J., & Bass, J. T. (2019) · Genes & Development · doi:10.1101/gad.328633.119 · Cited by 89
Alzheimer’s and ABC transporters — new opportunities for diagnostics and treatment
Pahnke, J., Langer, O., & Krohn, M. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.04.001 · Cited by 84
A critical overview of the influence of inflammation and infection on P-glycoprotein expression and activity in the brain
Roberts, D. J., & Goralski, K. B. (2008) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425255.4.10.1245 · Cited by 81
Therapeutic role of rifampicin in Alzheimer's disease
Yuluğ, B., Hanoğlu, L., Ozansoy, M., Isık, D., Kılıç, Ü., Kılıç, E., & Schabitz, W. R. (2018) · Psychiatry and Clinical Neurosciences · doi:10.1111/pcn.12637 · Cited by 81
Role of CNS efflux drug transporters in antiepileptic drug delivery: Overcoming CNS efflux drug transport
Potschka, H. (2011) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2011.12.007 · Cited by 80
Border-associated macrophages promote cerebral amyloid angiopathy and cognitive impairment through vascular oxidative stress
Uekawa, K., Hattori, Y., Ahn, S. J., Seo, J., Casey, N., Anfray, A., Zhou, P., Luo, W., Anrather, J., Park, L., et al. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00660-1 · Cited by 80
“Mice were then allowed to recover for 4–6 h after surgery [8, 45].”
BackgroundMethodInfluential
Aß peptides accelerate the senescence of endothelial cells in vitro and in vivo , impairing angiogenesis
Donnini, S., Solito, R., Cetti, E., Corti, F., Giachetti, A., Carra, S., Beltrame, M., Cotelli, F., & Ziche, M. (2010) · The FASEB Journal · doi:10.1096/fj.09-146456 · Cited by 80
Targeted inhibition of RAGE reduces amyloid-β influx across the blood-brain barrier and improves cognitive deficits in db/db mice
Wang, H., Chen, F., Du, Y., Long, Y., Reed, M. N., Hu, M. Y., Suppiramaniam, V. D., Hong, H., & Tang, S. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.12.026 · Cited by 80
Amyloid-β and Astrocytes Interplay in Amyloid-β Related Disorders
Batarseh, Y. S., Duong, Q.-V., Mousa, Y. M., Rihani, S. B. A., Elfakhri, K. H., & Kaddoumi, A. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17030338 · Cited by 82
St.John'sWort Reduces Beta‐Amyloid Accumulation in a Double TransgenicAlzheimer's Disease Mouse Model—Role of P‐Glycoprotein
Brenn, A., Grube, M., Jedlitschky, G., Fischer, A., Strohmeier, B., Eiden, M., Keller, M., Groschup, M. H., & Vogelgesang, S. (2014) · Brain Pathology · doi:10.1111/bpa.12069 · Cited by 79
New advances in brain-targeting nano-drug delivery systems for Alzheimer's disease
Ouyang, Q., Meng, Y., Zhou, W., Tong, J., Cheng, Z., & Zhu, Q. (2021) · Journal of drug targeting · doi:10.1080/1061186x.2021.1927055 · Cited by 80
Evaluation of glymphatic system activity by diffusion tensor image analysis along the perivascular space (DTI-ALPS) in dementia patients
Liang, T., Chang, F., Huang, Z., Peng, D., Zhou, X., & Liu, W. (2023) · British Journal of Radiology · doi:10.1259/bjr.20220315 · Cited by 79
Heterogeneity in the Rat Brain Vasculature Revealed by Quantitative Confocal Analysis of Endothelial Barrier Antigen and P-Glycoprotein Expression
Saubaméa, B., Cochois, V., Cisternino, S., & Scherrmann, J. (2011) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2011.109 · Cited by 78
Amyloid Beta Protein and Tau in Cerebrospinal Fluid and Plasma as Biomarkers for Dementia: A Review of Recent Literature
Frankfort, S. V., Tulner, L. R., van Campen, J., Verbeek, M. M., Jansen, R. W. M. M., & Beijnen, J. H. (2008) · Current Clinical Pharmacology · doi:10.2174/157488408784293723 · Cited by 78
Advances in PET Imaging of P-Glycoprotein Function at the Blood-Brain Barrier
Syvänen, S., & Eriksson, J. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn3001729 · Cited by 78

Authors: Cirrito, J. R.
Affiliations: Washington University in St. Louis (US)
Corresponding author: Cirrito, J. R.
ORCID: Cirrito, J. R.
Venue: Journal of Clinical Investigation
Publisher: American Society for Clinical Investigation
Published: 2005-11-01
Volume: 115
Issue: 11
Pages: 3285-3290
ISSN: 0021-9738 (ISSN-L)
DOI: 10.1172/jci25247
PMC: PMC1257538
OpenAlex: W2163209521
Cited by: 660
References: 34
Citations by year: 2026: 21 · 2025: 24 · 2024: 29 · 2023: 36 · 2022: 31 · 2021: 30 · 2020: 37 · 2019: 31 · 2018: 30 · 2017: 35 · 2016: 43 · 2015: 40 · 2014: 41 · 2013: 44 · 2012: 26
FWCI: 12.44
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Journal of Clinical Investigation (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Digital Commons@Becker (Washington University School of Medicine) (submittedVersion)
Funders: U.S. Department of Energy
National Institutes of Health (CA94056, AG13956)
National Institute on Aging (AG023316, R03AG023316, R01AG023084, AG23084, R01AG013956, R37AG023084, R37AG013956)
National Cancer Institute (P50 CA94056, P50CA094056)
National Institute of Allergy and Infectious Diseases (AI-13956)
National Institute of Neurological Disorders and Stroke (NS034467, R37NS034467, R01NS034467)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
Keywords: P-glycoprotein, blood-brain barrier, amyloid-beta, Alzheimer's disease, APP transgenic mice, P-glycoprotein inhibitors, brain interstitial fluid, amyloid-beta clearance, brain microvascular endothelial cells, amyloid-beta deposition
MeSH terms: Alzheimer Disease, Animals, Blood-Brain Barrier, Disease Models, Animal, Mice, Inbred C57BL, Mice, Transgenic, Polymorphism, Genetic, Up-Regulation, Amyloid beta-Peptides, Mice, Knockout, ATP Binding Cassette Transporter, Subfamily B, Member 1, Mice

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

P-glycoprotein deficiency at the blood-brain barrier increases amyloid- deposition in an Alzheimer disease mouse model

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks