The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Stimulation of the Retinoid X Receptor Facilitates Beta-Amyloid Clearance Across the Blood–Brain Barrier
Abstract
Alzheimer's disease (AD) is a neurodegenerative process characterized, in part, by the accumulation of beta-amyloid proteins (Aβ) in the brain. Evidence now suggests that the excessive Aβ accumulation is the result of impaired clearance from the brain. Recent studies have indicated that retinoid X receptor (RXR) activation stimulates the metabolic clearance of Aβ and rapidly reverses Aβ-induced behavioral deficits, doing so in an apoE-dependent manner. Previously, we reported that soluble apoE (i.e., not bound to Aβ) facilitated Aβ transit across the blood-brain barrier (BBB). As Aβ clearance from the brain involves both metabolic and BBB-mediated processes, the current studies investigated the impact of RXR stimulation on Aβ clearance across the BBB. Treatment with RXR agonists increased Aβ clearance across the BBB both in vitro and in vivo. Moreover, this processes appeared to involve apoE as RXR agonism did not stimulate Aβ BBB clearance when apoE was absent. Thus, RXR activation could mitigate Aβ brain burden by promoting both the metabolic and BBB clearance of Aβ, offering a novel approach to the treatment of AD.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
Bexarotene can promote the brain-to-blood transport of Aβ peptides in vitro and in vivo in the presence of ApoE.
“For example, previous research has demonstrated that bexarotene can promote the brain-to-blood transport of A peptides in vitro and in vivo in the presence of ApoE [65].”
The brain efflux of Aβ peptide across the BBB is increased by bexarotene.
“The brain efflux of A peptide across the BBB is increased [65]”
Citations
Cites
Decreased Clearance of CNS β-Amyloid in Alzheimer’s Disease
Mawuenyega, K. G., Sigurdson, W., Ovod, V., Munsell, L., Kasten, T., Morris, J. C., Yarasheski, K. E., & Bateman, R. J. (2010) · Science · doi:10.1126/science.1197623 · Cited by 2,078
Intracellular amyloid-β in Alzheimer's disease
LaFerla, F. M., Green, K. N., & Oddo, S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2168 · Cited by 1,942
The role of apolipoprotein E in Alzheimer's disease
Kim, J., Basak, J. M., & Holtzman, D. M. (2009) · Neuron · doi:10.1016/j.neuron.2009.06.026 · Cited by 1,661
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
Human ApoE isoforms differentially regulate brain amyloid-β peptide clearance
Castellano, J. M., Kim, J., Stewart, F. R., Jiang, H., DeMattos, R. B., Patterson, B. W., Fagan, A. M., Morris, J. C., Mawuenyega, K. G., Cruchaga, C., et al. (2011) · Science Translational Medicine · doi:10.1126/scitranslmed.3002156 · Cited by 1,242
Apolipoprotein E and its receptors in Alzheimer's disease: pathways, pathogenesis and therapy
Bu, G. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2620 · Cited by 1,168
ApoE-Directed Therapeutics Rapidly Clear β-Amyloid and Reverse Deficits in AD Mouse Models
Cramer, P. E., Cirrito, J. R., Wesson, D. W., Lee, C. Y. D., Karlo, J. C., Zinn, A. E., Casali, B. T., Restivo, J. L., Goebel, W. D., James, M. J., et al. (2012) · Science · doi:10.1126/science.1217697 · Cited by 1,050
ApoE Promotes the Proteolytic Degradation of Aβ
Jiang, Q., Lee, C. Y. D., Mandrekar, S., Wilkinson, B., Cramer, P., Zelcer, N., Mann, K., Lamb, B., Willson, T. M., Collins, J. L., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.04.010 · Cited by 876
apoE isoform–specific disruption of amyloid β peptide clearance from mouse brain
Deane, R., Sagare, A., Hamm, K., Parisi, M., Lane, S., Finn, M. B., Holtzman, D. M., & Zlokovic, B. V. (2008) · Journal of Clinical Investigation · doi:10.1172/jci36663 · Cited by 771
Cirrito, J. R. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25247 · Cited by 660
Paris, D., Bachmeier, C., Patel, N., Quadros, A., Volmar, C.-H., Laporte, V., Ganey, J., Beaulieu-Abdelahad, D., Ait-Ghezala, G., Crawford, F., et al. (2011) · Molecular Medicine · doi:10.2119/molmed.2010.00180 · Cited by 114
Self-citationYue, L., & Mazzone, T. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808482200 · Cited by 49
Flagged first, then by citations
Research works printed but not linked: 33
- Bachmeier C, Mullan M, Paris D (2010) Characterization and use of human brain microvascular endothelial cells to examine beta-amyloid exchange in the blood–brain barrier. Cytotechnology 62:519–529 · DOI
- Bachmeier C, Paris D, Beaulieu-Abdelahad D, Mouzon B, Mullan M, Crawford F (2012) A multifaceted role for apoe in the clearance of beta-amyloid across the blood–brain barrier. Neurodegener Dis. doi: 10.1159/000337231 · DOI
- Bachmeier CJ, Beaulieu-Abdelahad D, Mullan MJ, Paris D (2011) Epitope-dependent effects of beta-amyloid antibodies on beta-amyloid clearance in an in vitro model of the blood–brain barrier. Microcirculation 18:373–379 · DOI
- Burgess JW, Marcel YL (2001) Dynamic and stable pools of apoE differ functionally at the hepg2 cell surface. J Lipid Res 42:1413–1420 · DOI
- Camacho IE, Serneels L, Spittaels K, Merchiers P, Dominguez D, De Strooper B (2004) Peroxisome-proliferator-activated receptor gamma induces a clearance mechanism for the amyloid-beta peptide. J Neurosci 24:10908–10917 · DOI
- Chan GN, Hoque MT, Cummins CL, Bendayan R (2011) Regulation of p-glycoprotein by orphan nuclear receptors in human brain microvessel endothelial cells. J Neurochem 118:163–175 · DOI
- Dawson MI, Xia Z (2012) The retinoid x receptors and their ligands. Biochim Biophys Acta 1821:21–56 · DOI
- Do TM, Noel-Hudson MS, Ribes S et al (2012) Abcg2- and abcg4-mediated efflux of amyloid-beta peptide 1-40 at the mouse blood–brain barrier. J Alzheimers Dis 30:155–166 · DOI
- Fitz NF, Cronican A, Pham T et al (2010) Liver x receptor agonist treatment ameliorates amyloid pathology and memory deficits caused by high-fat diet in app 23 mice. J Neurosci 30:6862–6872 · DOI · Paper page
- Gauthier A, Vassiliou G, Benoist F, McPherson R (2003) Adipocyte low density lipoprotein receptor-related protein gene expression and function is regulated by peroxisome proliferator-activated receptor gamma. J Biol Chem 278:11945–11953 · DOI · Paper page
- Hessel S, Lampen A (2010) All-trans retinoic acid enhances the transport of phase ii metabolites of benzo[a]pyrene by inducing the breast cancer resistance protein expression in caco-2 cells. Toxicol Lett 197:151–155 · DOI
- Kockx M, Guo DL, Huby T et al (2007) Secretion of apolipoprotein e from macrophages occurs via a protein kinase A and calcium-dependent pathway along the microtubule network. Circ Res 101:607–616 · DOI
- Kockx M, Jessup W, Kritharides L (2008) Regulation of endogenous apolipoprotein E secretion by macrophages. Arterioscler Thromb Vasc Biol 28:1060–1067 · DOI · Paper page
- Krohn M, Lange C, Hofrichter J et al (2011) Cerebral amyloid-beta proteostasis is regulated by the membrane transport protein abcc1 in mice. J Clin Invest 121:3924–3931 · DOI · Paper page
- Kuhnke D, Jedlitschky G, Grube M et al (2007) Mdr1-p-glycoprotein (abcb1) mediates transport of Alzheimer’s amyloid-beta peptides–implications for the mechanisms of abeta clearance at the blood–brain barrier. Brain Pathol 17:347–353 · DOI
- Lefebvre P, Benomar Y, Staels B (2010) Retinoid x receptors: common heterodimerization partners with distinct functions. Trends Endocrinol Metab 21:676–683 · DOI
- Liang Y, Lin S, Beyer TP et al (2004) A liver x receptor and retinoid x receptor heterodimer mediates apolipoprotein e expression, secretion and cholesterol homeostasis in astrocytes. J Neurochem 88:623–634 · DOI · Paper page
- Lucas M, Mazzone T (1996) Cell surface proteoglycans modulate net synthesis and secretion of macrophage apolipoprotein E. J Biol Chem 271:13454–13460 · DOI
- McLean CA, Cherny RA, Fraser FW et al (1999) Soluble pool of abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer’s disease. Ann Neurol 46:860–866 · DOI
- Mehta PD (2007) Amyloid beta protein as a marker or risk factor of Alzheimer’s disease. Curr Alzheimer Res 4:359–363 · DOI
- Nordberg A (2008) Amyloid imaging in Alzheimer’s disease. Neuropsychologia 46:1636–1641 · DOI
- Piedrahita JA, Zhang SH, Hagaman JR, Oliver PM, Maeda N (1992) Generation of mice carrying a mutant apolipoprotein E gene inactivated by gene targeting in embryonic stem cells. Proc Natl Acad Sci USA 89:4471–4475 · DOI · Paper page
- Podlisny MB, Ostaszewski BL, Squazzo SL et al (1995) Aggregation of secreted amyloid beta-protein into sodium dodecyl sulfate-stable oligomers in cell culture. J Biol Chem 270:9564–9570 · DOI
- Podlisny MB, Walsh DM, Amarante P et al (1998) Oligomerization of endogenous and synthetic amyloid beta-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red. Biochemistry 37:3602–3611 · DOI
- Suon S, Zhao J, Villarreal SA et al (2010) Systemic treatment with liver x receptor agonists raises apolipoprotein E, cholesterol, and amyloid-beta peptides in the cerebral spinal fluid of rats. Mol Neurodegener 5:44 · DOI
- Tai LM, Loughlin AJ, Male DK, Romero IA (2009) P-glycoprotein and breast cancer resistance protein restrict apical-to-basolateral permeability of human brain endothelium to amyloid-beta. J Cereb Blood Flow Metab 29:1079–1083 · DOI · Paper page
- Tao H, Aakula S, Abumrad NN, Hajri T (2010) Peroxisome proliferator-activated receptor-gamma regulates the expression and function of very-low-density lipoprotein receptor. Am J Physiol Endocrinol Metab 298:E68–E79 · DOI
- Tsukuda K, Mogi M, Iwanami J et al (2009) Cognitive deficit in amyloid-beta-injected mice was improved by pretreatment with a low dose of telmisartan partly because of peroxisome proliferator-activated receptor-gamma activation. Hypertension 54:782–787 · DOI
- Vogelgesang S, Cascorbi I, Schroeder E et al (2002) Deposition of Alzheimer’s beta-amyloid is inversely correlated with p-glycoprotein expression in the brains of elderly non-demented humans. Pharmacogenetics 12:535–541 · DOI
- Weller RO, Boche D, Nicoll JA (2009) Microvasculature changes and cerebral amyloid angiopathy in Alzheimer’s disease and their potential impact on therapy. Acta Neuropathol 118:87–102 · DOI · Paper page
- Wells JM, Amaratunga A, McKenna DC, Abraham CR, Fine RE (1995) Amyloid β-protein precursor and apolipoprotein e production in cultured cerebral endothelial cells isolated from brains of patients with neurodegenerative disorders at autopsy. Amyloid 2:229–233 · DOI
- Zelcer N, Khanlou N, Clare R et al (2007) Attenuation of neuroinflammation and Alzheimer’s disease pathology by liver x receptors. Proc Natl Acad Sci USA 104:10601–10606 · DOI · Paper page
- Zhong N, Weisgraber KH (2009) Understanding the basis for the association of apoe4 with Alzheimer’s disease: opening the door for therapeutic approaches. Curr Alzheimer Res 6:415–418 · DOI
Cited by
Sorted by citations
APOE4-specific Changes in Aβ Accumulation in a New Transgenic Mouse Model of Alzheimer Disease
Youmans, K. L., Tai, L. M., Nwabuisi-Heath, E., Jungbauer, L., Kanekiyo, T., Gan, M., Kim, J., Eimer, W. A., Estus, S., Rebeck, G. W., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407957 · Cited by 268
The role of APOE in cerebrovascular dysfunction
Tai, L. M., Thomas, R., Marottoli, F. M., Koster, K. P., Kanekiyo, T., Morris, A. W. J., & Bu, G. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1547-z · Cited by 231
Hudry, E., Dashkoff, J., Roe, A. D., Takeda, S., Koffie, R. M., Hashimoto, T., Scheel, M., Spires-Jones, T., Arbel-Ornath, M., Betensky, R., et al. (2013) · Science Translational Medicine · doi:10.1126/scitranslmed.3007000 · Cited by 187
Tai, L. M., Bilousova, T., Jungbauer, L., Roeske, S. K., Youmans, K. L., Yu, C., Poon, W. W., Cornwell, L. B., Miller, C. A., Vinters, H. V., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.442103 · Cited by 165
Reversal of apoE4-driven brain pathology and behavioral deficits by bexarotene
Boehm-Cagan, A., & Michaelson, D. M. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.5198-13.2014 · Cited by 134
Paris, D., Ait-Ghezala, G., Bachmeier, C., Laco, G., Beaulieu-Abdelahad, D., Lin, Y., Jin, C., Crawford, F., & Mullan, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.608091 · Cited by 73
Self-citationKuntz, M., Candela, P., Saint-Pol, J., Lamartinière, Y., Boucau, M.-C., Sevin, E., Fenart, L., & Gosselet, F. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-150469 · Cited by 55
Metadata
- Authors
- Bachmeier, C., Beaulieu-Abdelahad, D., Crawford, F., Mullan, M., & Paris, D.
- Venue
- Journal of Molecular Neuroscience
- Published
- 2012-08-14
- Volume
- 49
- Issue
- 2
- Pages
- 270-276
- ISSN
- 0895-8696
- 1559-1166
- Cited by
- 39
- References
- 12
- Language
- en
- Licence
- www.springer.com/tdm (tdm)
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