p(HGNC:DLG4)
Abetao exposure induced a translocation of tau into the PSD fraction (***p 0.0002, 2-tailed Student’s t test; control 20.12 1228 vs Abetao 29.74 1.748, N 12 independent culture). There was also an increase of PSD-95 (***p0.0006, 2-tailed Student’s t test; control 19.10 2.557 vs Abetao 33.3 2153, N 9 independent culture), GluA1 (**p 0.0078, 2-tailed Student’s t test; control 18.841.930 vs Abetao 26.221.475,N9 independent culture) and fyn (**p 0.0041, 2-tailed Student’s t test; control 19.42 1.337 vs Abetao 29.67 2.181, N 6 independent cultures; Fig. 6D). PubMed:24760868
After Abetao treatment, synaptic activation did not trigger any increase in synaptic markers and in fact decreased synaptic actin (***p 0.0009, 2-tailed Student’s t test; Abetao 29.64 1.495, Abetao Bic/4-AP 18.56 2.030, N 7 independent cultures; Fig. 7C), PSD-95 (***p0.0007, 2-tailed Student’s t test; Abetao 33.37 2.153, Abetao Bic/4-AP 19.25 2.550, N 7 independent cultures) and tau levels (**p0.0014, 2-tailed Student’s t test; Abetao 29.74 1.748, Abetao Bic/4-AP 20.68 1.751, N 12 independent cultures). PubMed:24760868
Therefore, during a long-lasting synaptic activation, we observed an increase in tau, fyn, actin, GluA1, and PSD-95 content in the PSD-positive fraction, which is consistent with the characteristic features of synaptic plasticity (Ehlers, 2003). PubMed:24760868
In synapses, the projection domain of tau interacts with protein kinase Fyn (plays an important role during myelination [75]), postsynaptic density protein 95 (PSD-95) [76], and N-methyl-D-aspartate receptors (NMDAR). PubMed:26751493
In synapses, the projection domain of tau interacts with protein kinase Fyn (plays an important role during myelination [75]), postsynaptic density protein 95 (PSD-95) [76], and N-methyl-D-aspartate receptors (NMDAR). PubMed:26751493
The measurements showed similar patterns in both tested brain areas, with Adnp deficiency resulting in substantial decreases in spine density (male and female mice) and increases in PSD95-asymmetric shaft synapses (males only, as indicated by increased localization of PSD95 in dendritic shafts rather than spines), which were all rescued by NAP treatment. PubMed:30106381
This genotype- and sex-dependent pathology also extended to the cortex, with increased PSD95 shaft synapse density in Adnp+/– males compared with Adnp+/– females (P < 0.01), and was rescued by NAP treatment. PubMed:30106381
Importantly, in males, NAP treatment did not affect PSD95 shaft synapse density in either tested region (Supplemental Figures 3 and 4, insets). PubMed:30106381
Furthermore, NAP treatment increased PSD95 shaft synapse volume in both tested brain regions (Supplemental Figures 3 and 4, insets, P < 0.05). PubMed:30106381
In this respect, our previous data associated postsynaptic density protein 95 (PSD95, also known as DLG4) with ADNP/NAP activity PubMed:30664622
Figure 3, Supplemental Figure 5 (younger age group), Supplemental Figure 6 (older age group), and Supplemental Tables 5 and 8 reveal an overall similar pattern of Adnp genotype–and NAP treatment–regulated human and mouse protein product interactions across ages with Akt1 (the mosaic mutations of which lead to the Proteus syndrome, characterized by the overgrowth of skin, connective tissue, brain, and other tissues; ref. 37) and discs large MAGUK scaffold protein 4 (Dlg4, also known as Psd95), a key regulator of synaptic plasticity (see above) that plays central roles associated with ADNP and NAP function. PubMed:30106381
The measurements showed similar patterns in both tested brain areas, with Adnp deficiency resulting in substantial decreases in spine density (male and female mice) and increases in PSD95-asymmetric shaft synapses (males only, as indicated by increased localization of PSD95 in dendritic shafts rather than spines), which were all rescued by NAP treatment. PubMed:30106381
This genotype- and sex-dependent pathology also extended to the cortex, with increased PSD95 shaft synapse density in Adnp+/– males compared with Adnp+/– females (P < 0.01), and was rescued by NAP treatment. PubMed:30106381
In this respect, our previous data associated postsynaptic density protein 95 (PSD95, also known as DLG4) with ADNP/NAP activity PubMed:30664622
Therefore, during a long-lasting synaptic activation, we observed an increase in tau, fyn, actin, GluA1, and PSD-95 content in the PSD-positive fraction, which is consistent with the characteristic features of synaptic plasticity (Ehlers, 2003). PubMed:24760868
In synapses, the projection domain of tau interacts with protein kinase Fyn (plays an important role during myelination [75]), postsynaptic density protein 95 (PSD-95) [76], and N-methyl-D-aspartate receptors (NMDAR). PubMed:26751493
In synapses, the projection domain of tau interacts with protein kinase Fyn (plays an important role during myelination [75]), postsynaptic density protein 95 (PSD-95) [76], and N-methyl-D-aspartate receptors (NMDAR). PubMed:26751493
Figure 3, Supplemental Figure 5 (younger age group), Supplemental Figure 6 (older age group), and Supplemental Tables 5 and 8 reveal an overall similar pattern of Adnp genotype–and NAP treatment–regulated human and mouse protein product interactions across ages with Akt1 (the mosaic mutations of which lead to the Proteus syndrome, characterized by the overgrowth of skin, connective tissue, brain, and other tissues; ref. 37) and discs large MAGUK scaffold protein 4 (Dlg4, also known as Psd95), a key regulator of synaptic plasticity (see above) that plays central roles associated with ADNP and NAP function. PubMed:30106381
Figure 3, Supplemental Figure 5 (younger age group), Supplemental Figure 6 (older age group), and Supplemental Tables 5 and 8 reveal an overall similar pattern of Adnp genotype–and NAP treatment–regulated human and mouse protein product interactions across ages with Akt1 (the mosaic mutations of which lead to the Proteus syndrome, characterized by the overgrowth of skin, connective tissue, brain, and other tissues; ref. 37) and discs large MAGUK scaffold protein 4 (Dlg4, also known as Psd95), a key regulator of synaptic plasticity (see above) that plays central roles associated with ADNP and NAP function. PubMed:30106381
Figure 3, Supplemental Figure 5 (younger age group), Supplemental Figure 6 (older age group), and Supplemental Tables 5 and 8 reveal an overall similar pattern of Adnp genotype–and NAP treatment–regulated human and mouse protein product interactions across ages with Akt1 (the mosaic mutations of which lead to the Proteus syndrome, characterized by the overgrowth of skin, connective tissue, brain, and other tissues; ref. 37) and discs large MAGUK scaffold protein 4 (Dlg4, also known as Psd95), a key regulator of synaptic plasticity (see above) that plays central roles associated with ADNP and NAP function. PubMed:30106381
In this respect, our previous data associated postsynaptic density protein 95 (PSD95, also known as DLG4) with ADNP/NAP activity PubMed:30664622
In this respect, our previous data associated postsynaptic density protein 95 (PSD95, also known as DLG4) with ADNP/NAP activity PubMed:30664622
BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.
If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.