Product Citations: 34

Fig.2.E showing Western Blotting from the publication: Neuronal double-stranded DNA accumulation induced by DNase II deficiency drives tau phosphorylation and neurodegeneration.
Fig.5.C showing Western Blotting from the publication: Silencing of hypothalamic FGF11 prevents diet-induced obesity.
Fig.6.C showing Western Blotting from the publication: Silencing of hypothalamic FGF11 prevents diet-induced obesity.
Fig.6.G showing Western Blotting from the publication: Silencing of hypothalamic FGF11 prevents diet-induced obesity.
Fig.1.B showing Western Blotting from the publication: Paraquat, but not maneb, induces synucleinopathy and tauopathy in striata of mice through inhibition of proteasomal and autophagic pathways.
Fig.4.A showing Western Blotting in a Mus musculus (House mouse) sample from the publication: Region-specific tauopathy and synucleinopathy in brain of the alpha-synuclein overexpressing mouse model of Parkinson's disease.
Fig.1.C showing Western Blotting in a Mus musculus (House mouse) sample from the publication: Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.
Fig.2.C showing Western Blotting in a Mus musculus (House mouse) sample from the publication: Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.
Fig.3.B showing Western Blotting from the publication: Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.
Fig.4.A showing Western Blotting from the publication: Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.
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Alpha-Synuclein co-pathology in Alzheimer’s Disease drives tau accumulation

Preprint on Research Square on 21 May 2025 by Struebing, F. L., Song, X., et al.

Abstract The molecular basis for accelerated cognitive decline seen in Alzheimer’s Disease (AD) cases presenting with cortical alpha-Synuclein (SNCA/⍺-Syn) co-pathology is not well understood. We show that such AD co-pathology brains are characterized by an increased polygenic risk score for Parkinson’s Disease (PD), which is related to an enrichment in the MAPT H1 haplotype as well as risk factors known to increase SNCA transcription. AD + ASYN brains express higher levels of ⍺-Syn and neuronal microtubule-associated protein tau (MAPT), and increasing SNCA expression is sufficient to drive transcription, translation and phosphorylation of tau. In addition, tau is significantly elevated in subjects with a positive cerebrospinal fluid ⍺-Syn seeding aggregation assay. Our results reveal a hitherto unknown link between the pathogenesis of AD and PD whereby tau and ⍺-Syn synergistically drive dementia-related pathology.

  • WB
  • Neuroscience
  • Pathology
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Neuronal double-stranded DNA accumulation induced by DNase II deficiency drives tau phosphorylation and neurodegeneration.

In Translational Neurodegeneration on 2 August 2024 by Li, L. J., Sun, X. Y., et al.

Deoxyribonuclease 2 (DNase II) plays a key role in clearing cytoplasmic double-stranded DNA (dsDNA). Deficiency of DNase II leads to DNA accumulation in the cytoplasm. Persistent dsDNA in neurons is an early pathological hallmark of senescence and neurodegenerative diseases including Alzheimer's disease (AD). However, it is not clear how DNase II and neuronal cytoplasmic dsDNA influence neuropathogenesis. Tau hyperphosphorylation is a key factor for the pathogenesis of AD. The effect of DNase II and neuronal cytoplasmic dsDNA on neuronal tau hyperphosphorylation remains unclarified.
The levels of neuronal DNase II and dsDNA in WT and Tau-P301S mice of different ages were measured by immunohistochemistry and immunolabeling, and the levels of DNase II in the plasma of AD patients were measured by ELISA. To investigate the impact of DNase II on tauopathy, the levels of phosphorylated tau, phosphokinase, phosphatase, synaptic proteins, gliosis and proinflammatory cytokines in the brains of neuronal DNase II-deficient WT mice, neuronal DNase II-deficient Tau-P301S mice and neuronal DNase II-overexpressing Tau-P301S mice were evaluated by immunolabeling, immunoblotting or ELISA. Cognitive performance was determined using the Morris water maze test, Y-maze test, novel object recognition test and open field test.
The levels of DNase II were significantly decreased in the brains and the plasma of AD patients. DNase II also decreased age-dependently in the neurons of WT and Tau-P301S mice, along with increased dsDNA accumulation in the cytoplasm. The DNA accumulation induced by neuronal DNase II deficiency drove tau phosphorylation by upregulating cyclin-dependent-like kinase-5 (CDK5) and calcium/calmodulin activated protein kinase II (CaMKII) and downregulating phosphatase protein phosphatase 2A (PP2A). Moreover, DNase II knockdown induced and significantly exacerbated neuron loss, neuroinflammation and cognitive deficits in WT and Tau-P301S mice, respectively, while overexpression of neuronal DNase II exhibited therapeutic benefits.
DNase II deficiency and cytoplasmic dsDNA accumulation can initiate tau phosphorylation, suggesting DNase II as a potential therapeutic target for tau-associated disorders.
© 2024. The Author(s).

  • WB
  • Genetics
  • Neuroscience
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Neuronal downregulation of PLCG2 impairs synaptic function and elicits Alzheimer disease hallmarks

Preprint on Research Square on 31 May 2024 by Lambert, J., Coulon, A., et al.

Abstract We developed a high content screening to investigate how Alzheimer disease (AD) genetic risk factors may impair synaptic mechanisms in rat primary neuronal cultures. Out of the gene targets identified, we found that shRNA-mediated downregulation of Plcg2 in mouse dentate gyrus neurons consistently impaired dendritic morphology and synaptic function. In human neuronal cultures (hNCs), PLCG2 downregulation also impaired synaptic function and was associated with increased levels of Aβ and Tau phosphorylation, potentially via the AKT/GSK3β axis. Very rare PLCG2 loss-of-functon(LoF) variants were associated with a 10-fold increased AD risk. PLCG2 LoF carriers exhibit low mRNA/protein PLCG2/PLCγ2 levels, consistent with nonsense-mediated mRNA decay mechanisms. Restoring PLCγ2 levels in shPLCG2-hNCs fully reversed the disease-related phenotypes. Our findings indicate that the downregulation of PLCγ2 increases the risk of AD by impairing synaptic function and increasing the levels of Aβ and Tau phosphorylation in neurons.

  • WB
  • Neuroscience
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Augmenting hematoma-scavenging capacity of innate immune cells by CDNF reduces brain injury and promotes functional recovery after intracerebral hemorrhage.

In Cell Death & Disease on 15 February 2023 by Tseng, K. Y., Stratoulias, V., et al.

During intracerebral hemorrhage (ICH), hematoma formation at the site of blood vessel damage results in local mechanical injury. Subsequently, erythrocytes lyse to release hemoglobin and heme, which act as neurotoxins and induce inflammation and secondary brain injury, resulting in severe neurological deficits. Accelerating hematoma resorption and mitigating hematoma-induced brain edema by modulating immune cells has potential as a novel therapeutic strategy for functional recovery after ICH. Here, we show that intracerebroventricular administration of recombinant human cerebral dopamine neurotrophic factor (rhCDNF) accelerates hemorrhagic lesion resolution, reduces peri-focal edema, and improves neurological outcomes in an animal model of collagenase-induced ICH. We demonstrate that CDNF acts on microglia/macrophages in the hemorrhagic striatum by promoting scavenger receptor expression, enhancing erythrophagocytosis and increasing anti-inflammatory mediators while suppressing the production of pro-inflammatory cytokines. Administration of rhCDNF results in upregulation of the Nrf2-HO-1 pathway, but alleviation of oxidative stress and unfolded protein responses in the perihematomal area. Finally, we demonstrate that intravenous delivery of rhCDNF has beneficial effects in an animal model of ICH and that systemic application promotes scavenging by the brain's myeloid cells for the treatment of ICH.
© 2023. The Author(s).

  • WB
  • Cell Biology
  • Immunology and Microbiology
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Silencing of hypothalamic FGF11 prevents diet-induced obesity.

In Molecular Brain on 5 September 2022 by Cho, J. H., Kim, K., et al.

Fibroblast growth factor 11 (FGF11) is a member of the intracellular fibroblast growth factor family. Here, we report the central role of FGF11 in the regulation of metabolism. Lentiviral injection of Fgf11 shRNA into the arcuate nucleus of the mouse hypothalamus decreased weight gain and fat mass, increased brown adipose tissue thermogenesis, and improved glucose and insulin intolerances under high-fat diet conditions. Fgf11 was expressed in the NPY-expressing neurons, and Fgf11 knockdown considerably decreased Npy expression and projection, leading to increased expression of tyrosine hydroxylase in the paraventricular nucleus. Mechanistically, FGF11 regulated Npy gene expression through the glycogen synthase kinase 3-cAMP response element-binding protein pathway. Our study defines the physiological significance of hypothalamic FGF11 in the regulation of metabolism in response to overnutrition such as high-fat diet.
© 2022. The Author(s).

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Neuronal double-stranded DNA accumulation induced by DNase II deficiency drives tau phosphorylation and neurodegeneration.

In Transl Neurodegener on 2 August 2024 by Li, L. J., Sun, X. Y., et al.

Fig.2.E
Fig.2.E showing Western Blotting from the publication: Neuronal double-stranded DNA accumulation induced by DNase II deficiency drives tau phosphorylation and neurodegeneration.
  • WB
DNase II deficiency promotes tau phosphorylation in primary hippocampal neurons through activation of the CDK5, CaMKII and PP2A signaling pathway. a Representative images of AT8 (red) and pThr231 (red) fluorescence staining in primary hippocampal neurons infected with shDNase2a or shCON. Scale ba... more
DNase II deficiency promotes tau phosphorylation in primary hippocampal neurons through activation of the CDK5, CaMKII and PP2A signaling pathway. a Representative images of AT8 (red) and pThr231 (red) fluorescence staining in primary hippocampal neurons infected with shDNase2a or shCON. Scale bars, 10 μm. b Quantification of AT8 and pThr231 fluorescent areas in (a) by Image J software. c Western blotting of AT8 and pThr231 in the primary hippocampal neurons infected with shDNase2a or shCON. d Quantitation of the levels of AT8 and pThr231 in (c). e Western blotting of CDK5, Calpain2, p25, p35, CaMKII-α, p-CaMKII-α, PP2A, p-PP2A, CIP2A, GSK-3β, p-GSK-3β, Chk1, p-Chk1, Chk2 and p-Chk2 in the primary hippocampal neurons infected with shDNase2a or shCON. f Quantitation of the bands in (e) by the Image J software. g Representative images of pSer416 (cyan) fluorescence staining in primary hippocampal neurons infected with shDNase2a or shCON. Scale bars, 10 μm. h Quantification of pSer416 fluorescent area in (g) by the Image J software. i Western blotting of pSer416 in the primary hippocampal neurons infected with shDNase2a or shCON. j Quantitation of the levels of pSer416 in (i). In a, c, e, g and i, data are representative of three independent experiments. In b, d, f, h, and j, data were pooled from three independent experiments. Mean ± SEM, unpaired t-test with two-tailed P values was used for statistical analysis. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001, ns, not significant less

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Silencing of hypothalamic FGF11 prevents diet-induced obesity.

In Mol Brain on 5 September 2022 by Cho, J. H., Kim, K., et al.

Fig.5.C
Fig.5.C showing Western Blotting from the publication: Silencing of hypothalamic FGF11 prevents diet-induced obesity.
  • WB
Fgf11 knockdown in NPY/AgRP co-expressing hypothalamic cells increases CREB and decreases GSK3 activity. N41 cells were transfected with non-silencing siRNA control or siFgf11 for 48 h. A Western blots of N41 cells: transcription factors of NPY. B Quantitation of immunoblots. C Western blots of t... more
Fgf11 knockdown in NPY/AgRP co-expressing hypothalamic cells increases CREB and decreases GSK3 activity. N41 cells were transfected with non-silencing siRNA control or siFgf11 for 48 h. A Western blots of N41 cells: transcription factors of NPY. B Quantitation of immunoblots. C Western blots of the regulators of CREB activity. D, E Quantification of immunoblots. *p < 0.05, **p < 0.01, and ***p < 0.001 (non-silencing siRNA control versus siFgf11). n = 3 or 4 less

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Silencing of hypothalamic FGF11 prevents diet-induced obesity.

In Mol Brain on 5 September 2022 by Cho, J. H., Kim, K., et al.

Fig.6.C
Fig.6.C showing Western Blotting from the publication: Silencing of hypothalamic FGF11 prevents diet-induced obesity.
  • WB
FGF11 regulates Npy gene expression via GSK3-dependent CREB regulation in NPY/AgRP co-expressing hypothalamic cells. N41 cells were treated with dimethyl sulfoxide (vehicle) or BIO (1 μM) for 1, 3, or 6 h. A, B mRNA expression of Fgf11 and Npy after the treatment of BIO. C, D Western blots of GSK... more
FGF11 regulates Npy gene expression via GSK3-dependent CREB regulation in NPY/AgRP co-expressing hypothalamic cells. N41 cells were treated with dimethyl sulfoxide (vehicle) or BIO (1 μM) for 1, 3, or 6 h. A, B mRNA expression of Fgf11 and Npy after the treatment of BIO. C, D Western blots of GSK3, β-catenin, and CREB following the treatment of BIO. * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001 (vehicle versus BIO). n = 4–6. E–H N41 cells were transfected with non-silencing siRNA control or siFgf11 for 48 h, followed by the treatment with vehicle or BIO for 6 h. E, F mRNA expression of Fgf11 and Npy after Fgf11 knockdown with BIO treatment. G, H Western blots of GSK3, β-catenin, and CREB after Fgf11 knockdown with BIO treatment. * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001, n = 3–9 less

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Silencing of hypothalamic FGF11 prevents diet-induced obesity.

In Mol Brain on 5 September 2022 by Cho, J. H., Kim, K., et al.

Fig.6.G
Fig.6.G showing Western Blotting from the publication: Silencing of hypothalamic FGF11 prevents diet-induced obesity.
  • WB
FGF11 regulates Npy gene expression via GSK3-dependent CREB regulation in NPY/AgRP co-expressing hypothalamic cells. N41 cells were treated with dimethyl sulfoxide (vehicle) or BIO (1 μM) for 1, 3, or 6 h. A, B mRNA expression of Fgf11 and Npy after the treatment of BIO. C, D Western blots of GSK... more
FGF11 regulates Npy gene expression via GSK3-dependent CREB regulation in NPY/AgRP co-expressing hypothalamic cells. N41 cells were treated with dimethyl sulfoxide (vehicle) or BIO (1 μM) for 1, 3, or 6 h. A, B mRNA expression of Fgf11 and Npy after the treatment of BIO. C, D Western blots of GSK3, β-catenin, and CREB following the treatment of BIO. * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001 (vehicle versus BIO). n = 4–6. E–H N41 cells were transfected with non-silencing siRNA control or siFgf11 for 48 h, followed by the treatment with vehicle or BIO for 6 h. E, F mRNA expression of Fgf11 and Npy after Fgf11 knockdown with BIO treatment. G, H Western blots of GSK3, β-catenin, and CREB after Fgf11 knockdown with BIO treatment. * p < 0.05, ** p < 0.01, *** p < 0.001, and **** p < 0.0001, n = 3–9 less

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Paraquat, but not maneb, induces synucleinopathy and tauopathy in striata of mice through inhibition of proteasomal and autophagic pathways.

In PLoS One on 1 February 2012 by Wills, J., Credle, J., et al.

Fig.1.B
Fig.1.B showing Western Blotting from the publication: Paraquat, but not maneb, induces synucleinopathy and tauopathy in striata of mice through inhibition of proteasomal and autophagic pathways.
  • WB
Effect of maneb and paraquat on synucleins, p-GSK-3β and GSK-3β in striata.Striata from saline, maneb, paraquat, and maneb+paraquat injected mice were dissected and homogenized in a modified RIPA buffer containing 1.0% sodium cholate. Cholate-soluble fractions were isolated by centrifugation and ... more
Effect of maneb and paraquat on synucleins, p-GSK-3β and GSK-3β in striata.Striata from saline, maneb, paraquat, and maneb+paraquat injected mice were dissected and homogenized in a modified RIPA buffer containing 1.0% sodium cholate. Cholate-soluble fractions were isolated by centrifugation and analyzed by Western blots, as described under “Materials and Methods”. After exposure to antibodies, blots were stripped and re-probed for other proteins. The blots show representative gels while the bar graphs are composites of blots summarized from all animals (n = 5–6). (A) α-Syn and β-Syn were expressed relative to β-actin used as a loading control. (B) p-GSK-3β levels were probed using antibodies which recognizes a phosphorylation site at Tyr216; both p-GSK-3β and total GSK-3β were expressed relative to β-actin used as a loading control. Values are mean ± SEM as compared to saline-injected animals. Asterisks (**) indicate values significantly different from saline controls (p<0.01). Student's t-test was performed to compare saline-treated controls and treatment groups for all data. less

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Region-specific tauopathy and synucleinopathy in brain of the alpha-synuclein overexpressing mouse model of Parkinson's disease.

In BMC Neurosci on 3 August 2011 by Kaul, T., Credle, J., et al.

Fig.4.A
Fig.4.A showing Western Blotting in a Mus musculus (House mouse) sample from the publication: Region-specific tauopathy and synucleinopathy in brain of the alpha-synuclein overexpressing mouse model of Parkinson's disease.
  • WB
  • Mus musculus (House mouse)
Western blots of p-GSK-3β, p-p38, p-ERK, and p-JNK levels in brain stem, hippocampus, frontal cortex, and cerebellum of PDGF-α-Syn overexpressing transgenic mice. Brain stem [BS], hippocampus [HP], frontal cortex [FC], and cerebellum [CB] from PDGF-α-Syn transgenic mice and litter-mate non-transg... more
Western blots of p-GSK-3β, p-p38, p-ERK, and p-JNK levels in brain stem, hippocampus, frontal cortex, and cerebellum of PDGF-α-Syn overexpressing transgenic mice. Brain stem [BS], hippocampus [HP], frontal cortex [FC], and cerebellum [CB] from PDGF-α-Syn transgenic mice and litter-mate non-transgenic mice [WT] were solubilized in RIPA buffer and analyzed by Western blots for p-GSK-3β [A], p-p38 [B], p-ERK [C], and p-JNK [D]. p-GSK-3β was normalized to GSK-3β, p-p38 to p38, p-ERK to ERK, and p-JNK to JNK. p-p38MAPK was not detected in brain stem and therefore this data is not shown. All values are expressed as percent change relative to changes observed in WT control animals. Results are from 3-4 animals per group; [*, p < 0.05] and [**, p < 0.01] compared to corresponding protein levels in WT animals. All blots are representative of samples. less

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Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.

In PLoS One on 30 March 2011 by Wills, J., Credle, J., et al.

Fig.1.C
Fig.1.C showing Western Blotting in a Mus musculus (House mouse) sample from the publication: Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.
  • WB
  • Mus musculus (House mouse)
Elevated levels of α-Syn, p-Tau and p-GSK-3β in striata of α-Syn A53T mutant mice.Striata from wild type non-transgenic mice and A53T α-Syn mutant transgenic mice, 8 months of age, were dissected and homogenized in RIPA buffer, and analyzed by Western blots, as described under “Materials and Meth... more
Elevated levels of α-Syn, p-Tau and p-GSK-3β in striata of α-Syn A53T mutant mice.Striata from wild type non-transgenic mice and A53T α-Syn mutant transgenic mice, 8 months of age, were dissected and homogenized in RIPA buffer, and analyzed by Western blots, as described under “Materials and Methods”. After exposure to initial antibodies, blots were stripped and probed for other proteins. The blots show representative gels while the bar graphs are composites summarized from all animals (n = 4–9). (A) α-Syn and p-α-Syn were expressed relative to β-actin used as a loading control. (B). p-Tau was probed using antibodies specific for pSer202, pSer262 and pSer396/404, and expressed relative to total Tau used as loading control. (C). p-GSK-3β levels were probed using antibodies which recognize phosphorylation at Tyr216, and expressed relative to total GSK-3β. (D) PP1, PP2A and PP2B levels were probed using specific antibodies and normalized to β-actin. Asterisks (*) indicate values significantly different from wild-type animals (P<0.05). Student's t-test was performed for all data. less

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Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.

In PLoS One on 30 March 2011 by Wills, J., Credle, J., et al.

Fig.2.C
Fig.2.C showing Western Blotting in a Mus musculus (House mouse) sample from the publication: Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.
  • WB
  • Mus musculus (House mouse)
Postmortem PD brains show increased levels of α-Syn, p-GSK-3β and p-Tau at phosphorylation sites Ser202, Ser262 and Ser396/404 similar to striatum in the 8 month-old A53T mice.Postmortem control and PD brain lysates were prepared and immunoblots probed for (A) α-synuclein and p-α-synuclein, (B) p... more
Postmortem PD brains show increased levels of α-Syn, p-GSK-3β and p-Tau at phosphorylation sites Ser202, Ser262 and Ser396/404 similar to striatum in the 8 month-old A53T mice.Postmortem control and PD brain lysates were prepared and immunoblots probed for (A) α-synuclein and p-α-synuclein, (B) phospho-specific Tau epitopes at Ser202, Ser262 and Ser396/404 and (C) p-GSK-3β. (D) PP1, PP2A and PP2B levels were probed using specific antibodies and normalized to β-actin. Representative immunoblots from postmortem samples are shown. β-actin levels were measured as loading controls. Increases in the level of α-synuclein and are normalized to β-actin and data are expressed as a percent increase relative to amounts present in control, non-diseased brains (100%). Phospho-specific Tau and p-GSK-3β are expressed as a percent increase with respect to non-diseased controls (100%) after normalization to total Tau and GSK-3β, respectively. Values are mean ± SEM. Asterisks (*) indicate values significantly different from age-matched control postmortem striata (p<0.05). Student's t-test was performed for all data. less

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Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.

In PLoS One on 30 March 2011 by Wills, J., Credle, J., et al.

Fig.3.B
Fig.3.B showing Western Blotting from the publication: Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.
  • WB
Triton X-100 solubilization of striatal lysates from A53T α-Syn mutant and age-matched control animals.Striatal lysates from A53T α-Syn mutant mice and control, non-Tg mice [4 animals per group] were extracted with Triton X-100 as described in Methods. Proteins in Triton X-100-soluble and Triton ... more
Triton X-100 solubilization of striatal lysates from A53T α-Syn mutant and age-matched control animals.Striatal lysates from A53T α-Syn mutant mice and control, non-Tg mice [4 animals per group] were extracted with Triton X-100 as described in Methods. Proteins in Triton X-100-soluble and Triton X-100-insoluble fractions were measured by Western blots. Blots show representative gels while the bar graphs are composites summarized from all animals, expressed as percent of control, non-Tg mice. (A) β-actin was added as a loading control. (B) p-GSK-3β was normalized to GSK-3β from within each fraction on the blot. (C) pSer202, pSer262 and PSer396/404 were all normalized to total Tau in each fraction, and β-actin was added as a loading control. *, P<0.05; **, P<0.01 and indicate values significantly different from wild-type animals. Student's t-test was performed for all data. less

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Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.

In PLoS One on 30 March 2011 by Wills, J., Credle, J., et al.

Fig.4.A
Fig.4.A showing Western Blotting from the publication: Tauopathic changes in the striatum of A53T α-synuclein mutant mouse model of Parkinson's disease.
  • WB
Binding of striatal proteins from A53T α-Syn mutant and wild-type non-Tg mice to cytoskeleton.Lysates from striata of mutant and non-Tg mice [n = 4 per group] were extracted in PIPES buffer and SDS buffer to obtain cytoskeleton-free and cytoskeleton-bound fractions, as described in Methods. (A) α... more
Binding of striatal proteins from A53T α-Syn mutant and wild-type non-Tg mice to cytoskeleton.Lysates from striata of mutant and non-Tg mice [n = 4 per group] were extracted in PIPES buffer and SDS buffer to obtain cytoskeleton-free and cytoskeleton-bound fractions, as described in Methods. (A) α-Syn and p-GSK-3β were normalized to β-actin and GSK-3β, respectively, while (B) pSer396/404 was normalized to total Tau. Results were expressed as percent of control non-Tg mice. Blots show representative gels while the bar graphs are composites summarized from all animals. *, P<0.05; **, P<0.01 and indicate values significantly different from wild-type animals. Student's t-test was performed for all data. less

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