Ask about this productRelated genes to: SNAP25 antibody
- Gene:
- SNAP25 NIH gene
- Name:
- synaptosome associated protein 25
- Previous symbol:
- SNAP
- Synonyms:
- SNAP-25, RIC-4, RIC4, SEC9, bA416N4.2, dJ1068F16.2
- Chromosome:
- 20p12.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-01-24
- Date modifiied:
- 2016-10-05
Related products to: SNAP25 antibody
Related articles to: SNAP25 antibody
- Pathological scars, including hypertrophic scars and keloids, remain a significant clinical challenge due to the limitations of current treatments. Botulinum neurotoxin type A (BTX-A) has emerged as a transformative therapy, but its efficacy has often been narrowly attributed to its canonical function of reducing mechanical tone through muscle paralysis. This review synthesises extensive evidence to propose a more comprehensive, macrophage-centric framework for explaining the potent antifibrotic effects of BTX-A. We propose that the mechanism is rooted in two profoundly synergistic pathways of macrophage function. Established indirect pathways involve BTX-A creating mechanically and neurogenetically quiescent microenvironments. This action prevents pathologic extracellular matrix sclerosis and removes key stimuli that drive macrophage polarization toward a sustained profibrotic M2 phenotype. To complement this, we explored a highly plausible direct pathway by which BTX-A might be internalized by macrophages to enzyme digest SNARE proteins such as SNAP-25 and SNAP-23. This would directly compromise the cellular machinery responsible for the secretion of key profibrotic mediators, particularly TGF-β1. Together, these indirect environmental reprogramming and direct cellular interventions constitute a constitute a multiprilled attack to systematically dismantle the self-perpetuating feedback loop of fibrosis. By positioning macrophages as the central convergence point for these pleiotropic effects, this unified model provides a strong mechanistic basis for the clinical success of BTX-A and a clear pathway for optimizing treatment regimens and developing new combination strategies. - Source: PubMed
Publication date: 2026/06/18
Mohyeddin AliQi Fazhi - Mutations in the glucocerebrosidase () gene, originally implicated in Gaucher's disease, are now recognized as a major risk factor for developing Parkinson's disease (PD). While up to 70% of PD patients eventually progress to dementia, mutations further increase the risk of Lewy body dementias (LBD), an umbrella term encompassing both dementia with Lewy bodies and Parkinson's disease dementia. Collectively, these disorders are classified as synucleinopathies. To date, there is no clear understanding of the mechanistic relationships between mutations and synucleinopathies, although, synaptic protein changes have been shown to correlate with cognitive change in LBD as well as in Alzheimer's disease (AD). The aim of this study was to examine synaptic dysfunction in α-synucleinopathies with mutations. The research cohort consisted of 10 controls, PD/LBD- N370S, and 20 PD/LBD-wild type (WT) where seven synaptic markers including four pre-synaptic [synaptosomal-associated protein 25; (SNAP25), synaptophysin; (SYP), ras-related protein; (Rab3A), and vesicle associated membrane proteins 2; (VAMP2)], two post-synaptic [post-synaptic density protein 95; (PSD95), and neurogranin; (NRGN)], and one astrocytic [vesicle associated membrane proteins 3; (VAMP3)] protein were investigated in four cortical regions (prefrontal, temporal, anterior cingulate and parietal) using immunoblot technique. Four markers (NRGN, SNAP25, VAMP2, and VAMP3) were found to be significantly and regionally altered between the three groups. The expression of pre-synaptic (SNAP25), post-synaptic (NRGN), and the astrocytic protein (VAMP3) is different between PD/LBD with mutation and PD/LBD-WT suggesting the potential role of gene due to mutations which could alter the levels of some synaptic markers. Our study is the first to validate several synaptic markers in human post-mortem-associated N370S mutation. - Source: PubMed
Publication date: 2026/07/23
Eid Thamir MLashley TammarynWarner Thomas TKhan AlaaJantrachotechatchawan ChanatiFrancis Paul THardy JohnBandopadhyay Rina - Gastrointestinal (GI) dysfunction is a frequently reported comorbidity of neurodevelopmental disorders (NDDs). Early-life inflammatory challenges from the environment (e.g., infection, toxicants) can increase risk for NDDs, but the impact of such stressors on the developing GI tract is not well understood. We investigated possible mechanisms by which GI comorbidities arise in response to environmental stressors using our well-characterized model of combined gestational exposure to air pollution (diesel exhaust particles, DEP) and maternal stress (MS), which induces social deficits in male, but not female, offspring. We show that DEP/MS disrupts normal GI development in the first two weeks of postnatal life, leading to altered small intestine morphology in males, but not females. Recent evidence shows that resident macrophages of the gut prune enteric neurons during a precise postnatal window. We found decreased pruning of enteric neurons by the resident macrophages of the muscularis externa in DEP/MS exposed males at postnatal day (P)14. In line with this, we saw the expression of neurotransmission-associated genes (SNAP25, ChAT, nNOS, DBH, VIP, PENK) increased between P4 and P14 in males following DEP/MS exposure. Finally, we assessed small intestinal transit in vivo and observed dysmotility in DEP/MS males only. Taken together, these findings establish intestinal macrophages as probable mediators of GI development that are sensitive to early-life perturbations from the environment, highlighting a potential mechanism connecting NDDs with comorbid GI dysfunction. - Source: PubMed
Publication date: 2026/08/10
Nguyen Dang MMonroe Sarah KCampos-Salazar A BrayanRendina Danielle NBoyd Kevin SRispoli Erika DWirfel Olivia MAraujo Anna RVaidyanathan Trisha VKeziah Virginia LDevlin Benjamin ASmith Caroline JBilbo Staci D - Lifestyle habits, cognitive reserve, and affective reserve (secure attachment, extraversion, psychological resilience) predict resilience in the oldest-old, though the underlying biological mechanisms remain unclear. This study explored relationships between these protective factors, 120 + NULISA CNS blood biomarkers, and multidimensional health outcomes (global cognition, mental health, walking speed) in 401 dementia-free participants (age 83-87) from the InveCe.Ab study. Using sparse partial least squares (sPLS) regression, eight biomarkers were stably associated with the protective factors: HBA1, DDC, IFNG, IL15, GOT1, ACHE, SNAP25, and SNCB. Structural equation modeling (SEM) showed that the three protective factors exerted an independent and domain-specific effect on health outcomes. Moreover, lifestyle habits were associated with ACHE (β = 0.26), IL15 (β = 0.22), and GOT1 (β = 0.28); affective reserve showed inverse associations with IFNG (β = -0.13) and IL15 (β = -0.31), and GOT1 (β = -0.18). Regarding health domains, SNAP25 was inversely related to global cognition (β = -0.10), while SNCB was associated with global cognition (β = 0.16) and walking speed (β = 0.13). Notably, no significant mediated effects were found, suggesting that the clinical benefits observed were not directly driven by the aforementioned biological pathways. The present study paves the way for further investigations on the biological mechanisms underlying resilient aging, while further demonstrating the key protective role of individual habits and psychosocial characteristics during the life course. - Source: PubMed
Publication date: 2026/08/05
Rossi MicheleFerrari Riccardo RoccoPola IlariaBrianzoni IrenePellegrini ElisaDavin AnnalisaGuaita AntonioZetterberg HenrikAshton Nicholas JamesBenedet Andrea LessaRolandi Elena - Neuroendocrine cells communicate with other cells by releasing neurotransmitters or hormones by exocytosis, which involves SNARE-mediated fusion between secretory vesicles and the plasma membranes of the secreting cells. In neurons two plasma membrane SNARE proteins, Syntaxin-1a and SNAP25, join with the vesicle membrane SNARE protein Synaptobrevin-2 to form a four-helix bundle, which drives membrane fusion. The assembly of these SNAREs, which is highly orchestrated in cells, has been intensely studied in solution using fragments of the SNARE proteins without their transmembrane domains or lipid anchors. However, in cell and model membranes, Syntaxin and SNAP25 are known to oligomerize and cluster, and little is known about how clustering affects their incorporation into SNARE complexes. In cells, the SM protein Munc18 has been implicated in aiding secretory vesicle docking and facilitating SNARE complex assembly through its interactions with Syntaxin. To understand how Munc18 orchestrates SNARE complex assembly on membranes, we employed protein reconstitution in model membranes as well as biochemical and biophysical assays to show that lipid-dependent oligomerization of Syntaxin affects Munc18-Syntaxin binding and SNAP25 insertion into the plasma membrane acceptor SNARE complex. We showcase the consequences of the different modes of Munc18-Syntaxin and SNAP25 interaction on Syntaxin's oligomerization and orientation relative to the membrane surface, as well as on docking and fusion of purified insulin granules. We also determined low-resolution structures by cryoEM in nanodiscs and on the surface of proteoliposomes of membrane-bound assembly states of Munc18/Syntaxin and Munc18/Syntaxin/SNAP25 complexes. - Source: PubMed
Publication date: 2026/07/15
Tomaka WeronikaKreutzberger MarkBao HuanKiessling VolkerTamm Lukas K