PSD-95, monoclonal antibody, mouse, 100 ul.
- Known as:
- PSD-95, mab (anti-), mouse, 100 ul.
- Catalog number:
- MO50000-100
- Category:
- -
- Supplier:
- Neuromi
- Gene target:
- PSD-95 monoclonal antibody mouse 100 .
Related genes to: PSD-95, monoclonal antibody, mouse, 100 ul.
- Gene:
- DLG4 NIH gene
- Name:
- discs large MAGUK scaffold protein 4
- Previous symbol:
- -
- Synonyms:
- PSD-95, PSD95, SAP90, SAP-90
- Chromosome:
- 17p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1995-11-07
- Date modifiied:
- 2016-05-24
Related products to: PSD-95, monoclonal antibody, mouse, 100 ul.
Related articles to: PSD-95, monoclonal antibody, mouse, 100 ul.
- We report a 34-year-old male with childhood developmental delay, severe intellectual disability in adulthood, episodes of agitation with a previous diagnosis of schizoaffective disorder and adult-onset cognitive regression who developed progressive generalised dystonia due to a de novo DLG4 pathogenic loss-of-function variant. This case expands the phenotypic spectrum of recognised movement disorder manifestations associated with DLG4-related synaptopathy. - Source: PubMed
Publication date: 2026/08/01
Peraferrer-Montesinos LaiaNagaratnam Sai AForwood CaitlinBerry AlexisAshton KatieDong JackZhu YingArpone MartaBecker PalomaDelves MadelineMorales Briceno Hugo - SHINE syndrome is a rare neurodevelopmental disorder caused by mutations in DLG4, which encodes the postsynaptic scaffolding protein PSD-95. Key symptoms include sleep problems, hypotonia, intellectual disability, neurological disorders, and epilepsy, hence the name 'SHINE.' Here, we developed and characterized a mouse model of SHINE syndrome carrying the patient-derived DLG4V692Wfs*12/+ variant associated with a severe form of the disorder. The mutant transcript escapes nonsense-mediated decay but results in reduced PSD-95 protein expression, faithfully reproducing the molecular phenotype observed in the patient. Behavioral analyses revealed that Dlg4V692Wfs*12/+ mice recapitulate several hallmark features of SHINE syndrome, often in a sex-specific manner. Male mutants showed deficits in learning and cognitive flexibility. Dlg4V692Wfs*12/+ mice also demonstrate trends toward altered sensory processing and socialization. Male mutants exhibited an increased proportion of short sleep bouts and compensatory longer average sleep bout length, suggesting sporadic sleep reminiscent of the patient. While spontaneous seizures were not observed, future studies will test susceptibility to provoked seizures. Together, these findings establish Dlg4V692Wfs*12/+ mice as a robust and translationally relevant model that reproduces key molecular and behavioral features of SHINE syndrome. This model provides a valuable resource for elucidating the mechanisms underlying synaptic neurodevelopmental disorders and for identifying potential therapeutic strategies. - Source: PubMed
Tamir SharonPaulose JiffinNguyen AnhGadara DarshakWitt Rochelle MPrasad BhagwatHogenesch John B - The preBötzinger complex (preBötC) is a medullary network that generates the inspiratory phase of respiratory rhythm in mammals and depends critically on glutamatergic transmission. To characterize the anatomical organization of excitatory signaling elements within this network, we analyzed the distribution, morphology, and colocalization of the AMPA receptor subunit GluA2 and the NMDA receptor subunit NR1, together with the postsynaptic scaffold protein PSD95. We also used immunofluorescence and confocal microscopy to examine the spatial relationship between GluA2-positive puncta and the astrocytic glutamate transporter EAAT2 in the preBötC of adult male rats. NR1-positive puncta were more abundant and densely distributed than GluA2-positive puncta, whereas GluA2-NR1 colocalized puncta constituted only a small fraction of either receptor population. NR1-positive puncta also showed limited colocalization with PSD95-positive puncta, indicating that a substantial fraction of NR1 immunoreactivity is not associated with PSD95-defined postsynaptic domains under the present imaging conditions. In contrast, GluA2-positive puncta displayed a non-random spatial proximity with EAAT2 astrocytic profiles and were frequently located within submicron distances. Together, these findings reveal a spatially differentiated organization of glutamatergic elements in the preBötC, characterized by abundant non-PSD95-associated NR1-positive puncta and close apposition between GluA2-positive puncta and EAAT2-immunoreactive astrocytic profiles. This organization provides an anatomical framework for future studies testing how glutamate receptor localization and glutamate clearance mechanisms contribute to excitability and respiratory rhythm generation and modulation. - Source: PubMed
Publication date: 2026/08/06
Olmos-Pastoresa Carol AlejandraVázquez-Mendoza EnriqueVázquez-Martínez OliviaLópez-Meraz María LeonorBeltran-Parrazal LuisMorgado-Valle Consuelo - Huntington disease (HD) is a progressive neurodegenerative disease caused by an expanded CAG repeat in the () gene, leading to the accumulation of mutant HTT (mHTT). IL17A (interleukin 17A), a proinflammatory cytokine primarily secreted by Th17 and γδ T cells, has been implicated in immune-mediated neurodegeneration. However, the role of IL17A in the pathogenesis of HD remains poorly understood. Here, we identify IL17A as a critical pathogenic factor in HD that promotes neuroinflammation, mHTT aggregation, and autophagy-lysosomal dysfunction. IL17A disrupts autophagic flux by downregulating CTSB and CTSD, inducing SQSTM1/p62 and MAP1LC3B-II/LC3-II accumulation, and impairing lysosomal reformation. Mechanistically, IL17A suppresses lysosomal biogenesis by inhibiting the nuclear translocation of TFE3. This regulation occurs via a novel GSK3B/GSK-3β-TFE3 signaling pathway. Therapeutic neutralization of IL17A with a monoclonal antibody (IL17A mAb) ameliorates disease phenotypes in R6/2 HD mice, improving motor performance, extending survival, and reducing gliosis. IL17A mAb also attenuates mHTT aggregation and enhances neuroprotective signaling, as evidenced by increased expression of DLG4/PSD-95, phosphorylated CREB1, and BDNF. Moreover, IL17A mAb restores autophagy-lysosomal function by facilitating the clearance of protein aggregates and upregulating lysosomal enzymes and biogenesis markers, including CTSB, CTSD, PIP5K1A, and LAMP2. These findings establish IL17A as a key modulator of HD pathophysiology and highlight IL17A inhibition as a promising therapeutic strategy for targeting autophagy-lysosomal dysfunction in HD. - Source: PubMed
Publication date: 2026/07/23
Chen Kai-PoJu Tz-Chuen - The synonymous DLG4 variant is annotated with conflicting pathogenicity interpretations, and its molecular mechanism remains uncharacterized. Paternal germline mosaicism has been inferred but never molecularly confirmed in DLG4-related synaptopathy. - Source: PubMed
Chen JingZhao QinfeiZhang XinyueWu NanXi XuxiangZeng YinWu SaYuan KunLiu ZezhangWu XiangshengZeng Shaoying