SYBL1 _ VAMP7
- Known as:
- SYBL1 _ VAMP7
- Catalog number:
- Y213454
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- SYBL1 _ VAMP7
Related genes to: SYBL1 _ VAMP7
- Gene:
- VAMP7 NIH gene
- Name:
- vesicle associated membrane protein 7
- Previous symbol:
- SYBL1
- Synonyms:
- VAMP-7, TI-VAMP
- Chromosome:
- Xq28 and Yq12
- Locus Type:
- gene with protein product
- Date approved:
- 1996-06-21
- Date modifiied:
- 2015-11-05
Related products to: SYBL1 _ VAMP7
Anti- SYBL1 VAMP7 AntibodyAnti- SYBL1 / VAMP7 Antibodyanti-anti-SYBL1anti-anti-SYBL1anti-anti-SYBL1 type: Primary antibodies host: MouseAnti-SYBL1(synaptobrevin-like 1) AntibodyAntigens VAMP7, 1-188aa, Human, His tag, E.coli. RecombinantBos taurus,Bovine,SYBL1,Synaptobrevin-like protein 1,VAMP7,VAMP-7,Vesicle-associated membrane protein 7Bovine vesicle-associated membrane protein 7 (VAMP7) ELISA kit, Species Bovine, Sample Type serum, plasmaBovine Vesicle-associated membrane protein 7(VAMP7) ELISA kitBovine Vesicle-associated membrane protein 7(VAMP7) ELISA kitBovine Vesicle-associated membrane protein 7(VAMP7) ELISA kit SpeciesBovineCanine Vesicle-associated membrane protein 7(VAMP7) ELISA kitCanine Vesicle-associated membrane protein 7(VAMP7) ELISA kitChicken vesicle-associated membrane protein 7 (VAMP7) ELISA kit, Species Chicken, Sample Type serum, plasma Related articles to: SYBL1 _ VAMP7
- Ovotesticular Difference of Sex Development (OT-DSD) may result from chimerism, mosaicism, structural or sequence variants. However, even after investigating all known causes, many individuals still lack an established etiology. This study aimed to perform cytogenomic investigation of individuals with OT-DSD. - Source: PubMed
Publication date: 2026/04/28
Lima-Santos JúliaNascimento-Vidoti Carolina GamaCorreia-Costa Gabriela RoldãoCampos Nilma Lúcia ViguettiGuaragna Mara Sanchesde Oliveira Flávia MarcorinBarros Beatriz AmstaldenMiranda Marcio LopesAntolini Tavares ArthurGuerra-Junior GilMaciel-Guerra Andréa TrevasFabbri-Scallet HelenaVieira Társis Paiva - Malaria, caused by parasites, remains a global health crisis, necessitating novel therapeutic strategies targeting host-parasite interactions. During liver-stage infection, parasites exploit host vesicular trafficking machinery, particularly SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins that mediate membrane fusion. Using a CRISPR/Cas9 knockout system in HeLa cells combined with advanced microscopy of -infected HeLa cells, we identified specific endolysosomal SNAREs including Vesicle-Associated Membrane Protein 7 (VAMP7), Vesicle-Associated Membrane Protein 8 (VAMP8), Vesicle Transport Through Interaction With T-SNAREs 1B (Vti1B), and Syntaxin 7 (Stx7) to be recruited to the parasitophorous vacuole membrane (PVM) with distinct temporal profiles. This demonstrates the parasite's precise manipulation of host endolysosomal trafficking pathways. VAMP7 and Vti1B were localized to the PVM within 30 min post-infection, suggesting potential roles during invasion, while VAMP8 and Stx7 appeared later around 24 h post infection (hpi), coinciding with increased nutrient acquisition. Single gene deletions showed minimal impact, but combinatorial knockouts (KO) revealed critical redundancy. VAMP7-VAMP8 as well as VAMP7-Vti1B double KO significantly reduced parasite infection and growth, with Vti1B playing a dominant role. Triple KO phenotypes mirrored VAMP7-Vti1B disruption, underscoring Vti1B's dominant role. SNARE depletion also impaired the lysosome-PVM association and LAMP1 positive vesicle recruitment. Our findings indicate hijacks a coordinated host SNARE network to fuse lysosomes with the PVM for nutrient uptake. Targeting Vti1B-containing complexes disrupts this pathway without host cell toxicity, offering a promising host-directed antimalarial approach. - Source: PubMed
Publication date: 2026/03/25
Atchou KodzoKramer NicolasBindschedler AnninaSchmuckli-Maurer JacquelineCaldelari RetoHeussler Volker T - Kidney stones, as prevalent crystalline disorders within the urinary system, pose significant clinical challenges due to their high incidence and recurrence rates. The lack of clear pathological mechanisms has limited therapeutic options to surgical interventions without effective preventive strategies. In this study, integrated in vitro and in vivo models revealed that calcium oxalate (CaOx) exposure induced concurrent accumulation of LC3B-II and p62 autophagy markers. Blockade of autophagic flux at the late stage was validated via mCherry-GFP-LC3 dual fluorescence assays, demonstrating impaired autolysosome formation. Mechanistically, autophagic flux obstruction triggered oxidative stress, apoptosis, and proinflammatory cascades, collectively exacerbating renal tubular injury. Pharmacological inhibition of autophagy initiation with 3-methyladenine (3-MA) disrupted the maladaptive autophagy-reinforcement cycle, improving cellular viability and renal function. Conversely, lysosomal acidification blockade via bafilomycin A1 (BafA1) failed to mitigate cytotoxicity. Molecular screening identified specific downregulation of VAMP7-a SNARE complex component critical for autophagosome-lysosome fusion-as the primary mediator of CaOx-induced fusion defects. Overexpression of VAMP7 restored autophagic homeostasis and attenuated crystallotoxicity. This work pioneers a phase-specific autophagy targeting strategy: either suppression of pathological autophagic overactivation or restoration of terminal fusion machinery effectively alleviates CaOx nephrotoxicity. These findings provide a mechanistic foundation for precision therapeutics in stone disease management. - Source: PubMed
Publication date: 2026/04/06
Song ZhenyuMao XikeYang YuehanChen YangHao ZongyaoZhang Lvwen - Late endosomal secretion is an unconventional secretion mechanism that depends on the SNARE protein VAMP7. We previously showed that VAMP7 mediates the secretion of the ER protein Reticulon3. However, the functional relevance and molecular mechanism of this secretory pathway remain unclear. Here, we show that VAMP7 knockout cells exhibit impaired secretion of ER- and mitochondrial-derived proteins and signs of ER and mitochondrial stress. In addition, pharmacological induction of organellar stress enhances the VAMP7-dependent secretion. We assess the pathophysiological significance of this mechanism using a preclinical glioblastoma model. VAMP7 knockout glioblastoma cells implanted in male rat brain develop into more necrotic tumors with reduced macrophage infiltration compared to controls, suggesting that VAMP7-dependent late endosomal secretion contributes to the tumor microenvironment and affects macrophage infiltration. Together, our results support a model in which late endosomal secretion functions as an organelle quality-control and stress-communication mechanism, with particular relevance to cancer. - Source: PubMed
Publication date: 2026/02/21
Vats SomyaDionisio PedroLemercier QuentinPineau RaphaelTherreau LudivineLipecka JoannaCholley BéatriceMoog Jean-BaptisteWojnacki JoseKeime CélineZala DianaBun PhilippeFreire SofiaDomingues NeuzaDanglot LydiaGuerrera Ida ChiaraDelevoye CédricChevet EricRaimundo NunoGalli Thierry - Although liver fibrosis presents a substantial global health challenge, therapeutic options that directly target liver fibrosis remain limited. Hepatic stellate cells (HSCs) are key contributors to fibrosis through extracellular matrix production. This study uncovers a previously unrecognized function of HSCs: ATP secretion. We found that HSCs express the vesicular nucleotide transporter (VNUT) on secretory vesicles and actively release ATP. In mouse HSCs, VNUT is localized to the cytosol and around lipid droplets. In a thioacetamide-induced liver fibrosis model, VNUT inhibition with clodronate suppressed HSC proliferation and fibrosis progression, while restoring AMPK phosphorylation. In human hepatic stellate LX-2 cells, VNUT colocalized with v-SNARE proteins VAMP3 and VAMP7 and the vesicular proton pump V-ATPase. ATP secretion from LX-2 cells was observed upon stimulation with the Ca ionophore ionomycin and was inhibited by Ca chelation or low temperature, supporting an exocytotic mechanism. Clodronate and VNUT-targeting siRNA significantly reduced ATP release. Thapsigargin, an inducer of endoplasmic reticulum Ca release, upregulated VNUT expression, suggesting a transcriptional regulation of VNUT-dependent ATP release by Ca signaling. TGF-β1 stimulation also upregulated VNUT expression, suggesting its involvement in TGF-β1-induced fibrogenesis pathway. Additionally, serotonin was identified as an ATP secretion stimulator in LX-2 cells, and this effect was blocked by clodronate. Platelets-a major peripheral serotonin source-were increased in TAA-treated liver and found adjacent to serotonin receptor 5-HT2B-positive HSCs. Clodronate treatment reduced CD41-positive platelets in liver tissue. These findings highlight VNUT-mediated ATP secretion as a key regulator of HSC function and a potential therapeutic target for liver fibrosis. - Source: PubMed
Publication date: 2026/02/04
Kabashima MasaharuHasuzawa NaoWang LixiangRikitake JunjiroNomura SeijiNiimoto TomohiroTokubuchi RieMoriyama SawakoGobaru MizukiInoguchi YukihiroNagayama AyakoAshida KenjiOhta KeisukeMoriyama YoshinoriNomura Masatoshi