ArticleJournal of neuroscience research2009
Phospholipid transfer protein reduces phosphorylation of tau in human neuronal cells.
Article in Journal of neuroscience research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
15 citing papers in PubMed, 1 synthesis or guideline pooled it, 28 citations in OpenAlex.
- Integrated genomic approaches identify major pathways and upstream regulators in late onset Alzheimer's disease.Scientific reports · 2015Pooled it
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- Spatial transcriptomics at the brain-electrode interface in rat motor cortex and the relationship to recording quality.Journal of neural engineering · 2024Article
- GSK3: A potential target and pending issues for treatment of Alzheimer's disease.CNS neuroscience & therapeutics · 2024Review
- Arc Regulates Transcription of Genes for Plasticity, Excitability and Alzheimer's Disease.Biomedicines · 2022Article
- Effect of dietary palmitic and stearic acids on sucrose motivation and hypothalamic and striatal cell signals in the rat.American journal of physiology. Regulatory, integrative and comparative physiology · 2018Article
- Bpifcl modulates kiss2 expression under the influence of 11-ketotestosterone in female zebrafish.Scientific reports · 2017Article
- Blood RNA biomarkers in prodromal PARK4 and rapid eye movement sleep behavior disorder show role of complexin 1 loss for risk of Parkinson's disease.Disease models & mechanisms · 2017Article
- Cathepsin G degradation of phospholipid transfer protein (PLTP) augments pulmonary inflammation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014Article
- Phospholipid transfer protein is expressed in cerebrovascular endothelial cells and involved in high density lipoprotein biogenesis and remodeling at the blood-brain barrier.The Journal of biological chemistry · 2014Article
- Increased amyloid-β peptide-induced memory deficits in phospholipid transfer protein (PLTP) gene knockout mice.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2013Article
- Role of plasma phospholipid transfer protein in lipid and lipoprotein metabolism.Biochimica et biophysica acta · 2012Review
- Rapid evolution and copy number variation of primate RHOXF2, an X-linked homeobox gene involved in male reproduction and possibly brain function.BMC evolutionary biology · 2011Article
- PLTP regulates STAT3 and NFκB in differentiated THP1 cells and human monocyte-derived macrophages.Biochimica et biophysica acta · 2011Article
- Androgen-induced Rhox homeobox genes modulate the expression of AR-regulated genes.Molecular endocrinology (Baltimore, Md.) · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Tau function is regulated by phosphorylation, and abnormal tau phosphorylation in neurons is one of the key processes associated with development of Alzheimer's disease and other tauopathies. In this study we provide evidence that phospholipid transfer protein (PLTP), one of the main lipid transfer proteins in the brain, significantly reduces levels of phosphorylated tau and increases levels of the inactive form of glycogen synthase kinase-3beta (GSK3 beta) in HCN2 cells. Furthermore, inhibition of phosphatidylinositol-3 kinase (PI3K) reversed the PLTP-induced increase in levels of GSK3 beta phosphorylated at serine 9 (pGSK3 beta(Ser9)) and partially reversed the PLTP-induced reduction in tau phosphorylation. We provide evidence that the PLTP-induced changes are not due to activation of Disabled-1 (Dab1), insofar as PLTP reduced levels of total and phosphorylated Dab1 in HCN2 cells. We have also shown that inhibition of tyrosine kinase activity of insulin receptor (IR) and/or insulin-like growth factor 1 (IGF1) receptor (IGFR) reverses the PLTP-induced increase in levels of phosphorylated Akt (pAkt(Thr308) and pAkt(Ser473)), suggesting that PLTP-mediated activation of the PI3K/Akt pathway is dependent on IR/IGFR receptor tyrosine kinase activity. Our study suggests that PLTP may be an important modulator of signal transduction pathways in human neurons.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.