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the tau isoforms with exon-2 and exon-10 segments increase in CSF (show CSF2 Proteins) of sporadic Creutzfeldt-Jakob disease and some types of genetic Creutzfeldt-Jakob disease.
Tau protein, along with amyloidBeta42 and GFAP (show GFAP Proteins), were increased in plasma up to 90 days after traumatic brain injury compared with controls.
Regions other than the constitutive promoter may be involved in microtubule-associated protein tau gene regulation in tauopathies.
LRRK2 (show LRRK2 Proteins) regulates intracellular Tau levels, contributing to the progression of the pathology caused by the LRRK2 (show LRRK2 Proteins)-mediated proteasome impairment.
Insulin (show INS Proteins) is accumulated and retained as oligomers in hyperphosphorylated tau-bearing neurons in Alzheimer's disease and in several of the most prevalent human tauopathies.
Inhibition of CaN attenuated the hTau-induced CREB (show CREB1 Proteins) dephosphorylation with improved synapse and memory functions.
Study describes a protocol to extract and measure tau seeding activity from small volumes (.04 mm(3)) of formaldehyde-fixed tissue immediately adjacent to that used for immunohistochemistry, validated this method with the PS19 transgenic mouse model, and easily observed seeding well before the development of phospho-tau pathology. Also accurately isolated two tau strains, DS9 and DS10, from fixed brain tissues in mice.
evidence that JNK (show MAPK8 Proteins) signaling pathway is an upstream regulator of hyperosmotic stress-induced Tau cleavage and apoptosis in SH-SY5Y through the control of caspase-3 (show CASP3 Proteins) activation.
Central nervous system (CNS)-derived tau in L1CAM-containing exosomes was characterized extensively in human plasma, including by single molecule array technology with 303 subjects. In human plasma, tau was explicitly identified within L1CAM exoso (show L1CAM Proteins)mes. In contrast to Alzheimer's patients, L1CAM exosomal tau was significantly higher in Parkinson's patients than controls and correlated with cerebrospinal fluid tau.
Our findings unmask tau-mediated perturbations of specific pathways associated with neuronal vulnerability, revealing potential early disease biomarkers and therapeutic targets for FTD (show FTL Proteins) and other tauopathies.
Csnk1e (show CSNK1E Proteins) deletion increased mu opioid receptor (show OPRM1 Proteins)-dependent behaviors.
Study demonstrates a mechanistic link between brain Abeta (show APP Proteins) deposition and CSF (show CSF2 Proteins) tau, and thus, CSF (show CSF2 Proteins) tau may present an important readout of Abeta (show APP Proteins) deposition in mouse models and likely in Alzheimer's disease.
Tau efflux from the brain to the blood was evaluated by administering radioactively labeled and unlabeled tau intracerebroventricularly in wild-type and tau knock-out mice, respectively. The efflux of Tau, including a fraction via CNS-derived L1CAM (show L1CAM Proteins) exosomes, was observed in mice. Tau is readily transported from the brain to the blood.
Somatodendritic accumulation of Tau in Alzheimer's disease is promoted by Fyn (show FYN Proteins)-mediated local protein translation.
The authors concluded that the FcgammaRIIb-SHIP2 (show INPPL1 Proteins) axis links Abeta (show APP Proteins) neurotoxicity to tau pathology by dysregulating phosphoinositide metabolism, providing insight into therapeutic potential against Alzheimer's disease.
Pin1 (show PIN1 Proteins) serves as a positive regulatory molecule of proplatelet formation of megakaryocytes by enhancing the function of phosphorylated tau.
Here, the authors identify another Wnt (show WNT2 Proteins) signaling amplifier, CKIepsilon (show CSNK1E Proteins), which is specifically upregulated in intestinal stem cells and is essential for intestinal stem cell maintenance, especially in the absence of its close isoform CKIdelta (show CSNK1D Proteins).
PGRN (show GRN Proteins) decrease, resulting from pathogenic mutations, might compromise the trophism of cortical neurons by affecting GluN2B (show GRIN2B Proteins)-contaning NMDA receptors
These results suggest that tau haploinsufficiency, without the compensation effect of MAP1A (show MAP1A Proteins), induces reduction of Otx2 (show OTX2 Proteins) expression, increases prenatal cell death, and accordingly leads to selective loss of VTA DA neurons in the early postnatal stage.
High-glucose induces tau hyperphosphorylation through activation of TLR9 (show TLR9 Proteins)-P38 MAPK (show MAPK14 Proteins) pathway.
Findings suggest that the endothelin-1 (show EDN1 Proteins)-induced down-regulation of NaV1.7 (SCN9A (show SCN9A Proteins)) diminishes NaV1.7 (show SCN9A Proteins)-related catecholamine secretion and dephosphorylation of tau.
The protein phosphatase PP2A/Balpha binds to the microtubule-associated proteins Tau and MAP2 at a motif also recognized by the kinase Fyn (show FYN Proteins).
show that cathepsin D (show CTSD Proteins) cleaves both tau and beta-amyloid precursor protein (APP). Both tau and APP (show APP Proteins) are involved in the pathogenesis of Alzheimer's disease
results suggest that Nav1.7-Ca2+ influx-protein kinase C-alpha pathway activated ERK1/ERK2 and p38, which increased phosphorylation of glycogen synthase kinase-3beta, decreasing tau phosphorylation
We conclude that GSK3beta phosphorylates tau directly at S(202) but requires the previous phosphorylation on S(235) to phosphorylate T(231). Phosphorylation of S(396), on the other hand, occurs sequentially.
Suppressing the expression of all tau isoforms disrupted only those neuronal microtubules containing class II beta-tubulin (show TUBB Proteins), and that boosting the expression of the largest 'big', but not the smallest, tau isoform enhanced neurite outgrowth.
We found that inversion of the MAPT region is similarly polymorphic in other great ape species, and we present evidence that the inversions occurred independently in chimpanzees and humans
age-related increase in cAMP-dependent protein kinase (show CDK7 Proteins) (PKA) phosphorylation of tau at serine 214 (pS214-tau) in monkey dorsolateral prefrontal association cortex specifically targets spine synapses and the Ca(2 (show CA2 Proteins)+)-storing spine apparatus.
This gene encodes the microtubule-associated protein tau (MAPT) whose transcript undergoes complex, regulated alternative splicing, giving rise to several mRNA species. MAPT transcripts are differentially expressed in the nervous system, depending on stage of neuronal maturation and neuron type. MAPT gene mutations have been associated with several neurodegenerative disorders such as Alzheimer's disease, Pick's disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy.
G protein beta1/gamma2 subunit-interacting factor 1
, neurofibrillary tangle protein
, paired helical filament-tau
, CKI, epsilon
, KC1 epsilon
, casein kinase I isoform epsilon
, Tau microtubule-associated protein
, microtubule associated protein tau
, tau-like protein
, tau-like protein-2
, microtubule-associated protein tau
, Microtubule-associated protein tau
, Neurofibrillary tangle protein
, Paired helical filament-tau
, sodium- and chloride-dependent taurine transporter
, solute carrier family 6 (neurotransmitter transporter, taurine), member 6
, solute carrier family 6 (neurotransmitter transporter, taurine), member 6b
, taurine transporter