Ask about this productRelated genes to: SNTA1 antibody
- Gene:
- SNTA1 NIH gene
- Name:
- syntrophin alpha 1
- Previous symbol:
- SNT1
- Synonyms:
- TACIP1, LQT12
- Chromosome:
- 20q11.21
- Locus Type:
- gene with protein product
- Date approved:
- 1994-12-14
- Date modifiied:
- 2019-04-23
Related products to: SNTA1 antibody
Related articles to: SNTA1 antibody
- Traumatic brain injury (TBI) is often viewed as a progressively evolving molecular response, yet the molecular and cellular responses that dictate acute TBI may differ fundamentally from those that define the chronically remodeled brain. We integrated temporally-resolved transcriptomic analyses with independent mouse, human, proteomic, and spatial datasets to determine how neural-circuit and astrocyte-homeostatic transcriptional responses reorganize after controlled cortical impact (CCI). In GSE269748, a mouse CCI transcriptomic dataset spanning acute to chronic post-injury timepoints, transcriptomic remodeling was non-monotonic. The number of genes showing large expression changes was greatest at 7 days, with extensive transcriptional changes persisting at 6 months. A more selective astrocytic phenotype emerged at 7 days and persisted at 6 months, with increasing disproportionately relative to , producing a sustained AQP4/SNTA1 expression imbalance. This imbalance occurred alongside heterogeneous endfoot remodeling and could not be explained by inflammatory stress alone. Among 14 prespecified biological processes, potassium and ion homeostasis showed the most specific and robust association with the AQP4/SNTA1 imbalance after adjustment for broader reactivity and AP-1 activity; this observation remained stable to gene, sample, and injury-model perturbation. Circuit-associated analyses provided complementary context, showing that dopamine recipient changes occurred within broader neurotransmitter system remodeling rather than as a unique signal. Integrative temporal analysis distinguished acute stress-dominant remodeling from delayed astrocyte-homeostatic changes, with AQP4/SNTA1 imbalance and potassium and ion homeostatic remodeling becoming most prominent at later stages. External datasets provided limited contextual support while defining clear limits to generalization. Together, these findings identify delayed AQP4/SNTA1 expression imbalance within potassium and ion homeostatic remodeling as a testable feature of chronic post-traumatic astrocyte biology. - Source: PubMed
Publication date: 2026/09/16
George BenuEmmons Eric BZhang Qiang - Aquaporin 4 (AQP4) water channels are polarized to astrocytic endfeet at blood vessel interfaces, and lose polarity in vascular diseases, including stroke, chronic traumatic encephalopathy, and Alzheimer's disease. AQP4 modulates water influx and efflux in the interstitial fluid, yet how AQP4 localization impacts cerebral amyloid angiopathy (CAA) remains poorly understood. Here we show that astrocytic end feet and AQP4 are displaced from amyloid-bearing vessels in a prion-CAA mouse model that expresses GPI-anchorless PrP. Displacing AQP4 genetically through deleting alpha-syntrophin ( ) led to a marked prolongation in survival, together with reduced microglial inflammation and C1q, in prion-CAA-affected mice. Additionally, synaptic structural proteins were better maintained. Finally, the level and distribution of prion aggregates were similar among the mice, indicating that prion conversion and spread was not affected. These results suggest that reducing AQP4 water channel function slows the decline in a vascular amyloid disease by reducing neuroinflammation. - Source: PubMed
Publication date: 2026/07/17
Flores SamanthaWilpitz AmandaOjeda-Juarez DanielWang JinDanque GarrettSumowski PaigeFunk GailMalik AdelaPizzo DonRichards EmilyIliff Jeffrey JSigurdson Christina J - Dystrophin links the actin cytoskeleton to the extracellular matrix through the dystrophin-glycoprotein complex (DGC), providing structural stability to muscle fibers. In mdx mice, which lack dystrophin, neuromuscular junctions (NMJs) remain largely structurally and functionally intact despite extensive muscle pathology. Here, using single- and double-mutant mice deficient in dystrophin and α-syntrophin (α-syn), we investigated how utrophin upregulation contributes to NMJ maintenance in dystrophic muscle. During early postnatal development, when dystrophic muscles are transiently resistant to degeneration, the DGC proteins α-dystrobrevin, α-syn, and β-dystroglycan are broadly distributed along both synaptic and extra-synaptic regions of the sarcolemma, although their overall levels are reduced compared with wild-type (WT) muscle. In contrast, in WT mice, utrophin is restricted to NMJs, whereas in dystrophic muscles from both mutants, it is distributed along both synaptic and extra-synaptic regions of the sarcolemma, particularly within the innervated zone of muscle fibers. As muscles mature and degeneration begins, these DGC components become highly restricted to NMJs while being markedly reduced or absent from the extra-synaptic sarcolemma in many muscle cells. Although utrophin remains highly enriched at synaptic sites in mdx:α-syn-/- muscles, their NMJs display severe structural abnormalities compared with those of mdx mice. These include a dramatic reduction in synaptic fold depth and density, a decrease in presynaptic vesicle density, retraction of nerve terminals, and axonal thinning. These findings demonstrate that utrophin localization at the NMJ is not sufficient to preserve synaptic integrity and that functional interactions between utrophin and α-syn are required to maintain the NMJ in dystrophic muscle. - Source: PubMed
Wierenga AlissaMendoza MichelleMalik Saad OAgrawal AkashReda AyaMaag AbigailAbou-Rjaily AmeenGao ChenlangAkaaboune Mohammed - Impaired glymphatic clearance has been implicated in Alzheimer's disease (AD) through reduced clearance of amyloid-β (Aβ) and other metabolites from the brain. Mislocalisation of aquaporin-4 (AQP4), a water channel protein anchored to astrocytic endfeet by the dystrophin-associated complex (DAC), has been linked to increased Aβ accumulation, neurodegeneration and cognitive impairment. In animal models, genetic ablation of DAC subunits, leading to AQP4 mislocalisation, increases Aβ accumulation. Genetic variation in has been examined in the context of AD, but variation in key DAC genes has not been systematically investigated in humans. This study examined whether variation within glymphatic pathway genes is associated with AD-related phenotypes in individuals on the AD trajectory. - Source: PubMed
Publication date: 2026/05/06
Armstrong Ayeisha MilliganO'Brien Eleanor KFernandez Shane MDoré VincentBourgeat PierrickShishegar RositaMaruff PaulRowe Christopher CVillemagne Victor L Porter TenielleLaws Simon M - Cerebral edema is a severe complication following ischemic stroke. Recent studies have highlighted the crucial role of the glymphatic system (GS) in the clearance of water and macromolecules. GS dysfunction involving the disorders of AQP4 polarization may be crucial in the pathophysiology of cerebral edema. β-Hydroxybutyrate (BHB), the main component of the ketone body, has been shown to alleviate neurological deficits by restoring GS function in subarachnoid hemorrhage models and to reduce Aβ deposition in Alzheimer's disease models. In this study we investigated the effects of BHB on cerebral edema following ischemic stroke and its mechanisms. The mice were fed a ketogenic diet (KD) or a normal diet for 4 weeks before transient middle cerebral artery occlusion (MCAO). Alternatively, the mice received BHB (5 g·kg·d) or vehicle post-MCAO. By using brain section analysis, transcranial macroimaging, two-photon in vivo imaging and MRI, we demonstrated that both KD and BHB treatment significantly enhanced GS function under normal and MCAO conditions. BHB reduced cerebral edema and infarct volume post-MCAO. Notably, delayed BHB treatment initiated 10 h post-MCAO still improved GS function, but did not influence infarct volume. Furthermore, we revealed that BHB increased α1-syntrophin expression and H3K27ac levels in α1-syntrophin (Snta1) enhancer, restoring AQP4 polarization. In addition, BHB also reduced HDAC3 expression and elevated p300 expression. These results suggest that a KD and BHB treatment enhance GS function in mice and that BHB also mitigates brain edema after MCAO. The potentiation of GS function by BHB is likely mediated by the inhibition of HDAC3 activity and the increase in p300 activity, which upregulate α1-syntrophin expression and restore AQP4 polarization. - Source: PubMed
Publication date: 2026/01/14
Yu Ming-JiaXiong Rui-QiWu Jing-WenLi Yong-ChuanXie Jia-XinZhou Hai-PingYe Guan-YuChang YuanHuang Kai-BinPan Su-Yue