GRS2 Cell Lysis Solution 10 ml
- Known as:
- GRS2 Cell disruption Solution 10 milliliter
- Catalog number:
- 40-4093-01
- Product Quantity:
- 10ml
- Category:
- Cells
- Supplier:
- Gene Link
- Gene target:
- GRS2 Cell Lysis Solution 10
Related genes to: GRS2 Cell Lysis Solution 10 ml
- Gene:
- GORASP2 NIH gene
- Name:
- golgi reassembly stacking protein 2
- Previous symbol:
- -
- Synonyms:
- GRASP55, GRS2, GOLPH6
- Chromosome:
- 2q31.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-05-23
- Date modifiied:
- 2015-11-09
Related products to: GRS2 Cell Lysis Solution 10 ml
Related articles to: GRS2 Cell Lysis Solution 10 ml
- ALK-positive large B-cell lymphoma (ALK + LBCL) is a rare subtype of large B-cell lymphoma characterized by plasmablastic morphology, intra-sinusoidal or sheet-like proliferation, loss of pan-B-cell markers, and expression of plasmacytic markers. According to WHO classification, CD30 expression is generally absent and Epstein-Barr virus (EBV) infection is not detected [1,2,5] . We aim to report the first case of ALK-positive, EBV-positive large B-cell lymphoma (ALK + EBV + LBCL) in an HIV-infected patient. A 60-year-old Thai male with HIV infection and severe immunosuppression (CD4 count: 93 cells/mm) presented with generalized lymphadenopathy and an epiglottic mass. Biopsy showed a plasmablastic neoplasm proliferating in loose sheets, negative for pan-B-cell markers except OCT2, and positive for plasmacytic markers and CD30. The tumor also expressed EBER, ALK1 (paranuclear dot pattern), and ALK D5F3; HHV8 was negative. FISH confirmed ALK gene rearrangement, and targeted sequencing revealed a GORASP2::ALK fusion gene. The diagnosis of ALK + EBV + LBCL in the setting of HIV-related immunodeficiency was established. The patient developed pneumonia with septic shock and died during admission. EBV-positive plasmablastic B-cell neoplasms in HIV-infected patients are not always plasmablastic lymphoma. Immunohistochemistry for ALK and HHV8 should be included in the diagnostic panel. Importantly, CD30 and EBER positivity do not exclude ALK + LBCL. - Source: PubMed
Publication date: 2026/03/10
Surintrspanont Chutima PinnarkBuasatit BenjamapornSukswai NaritteeHemla SuphakitTeerapakpinyo ChinachoteShuangshoti Shanop - The Golgi complex is central to cellular homeostasis and serves as a key processing and sorting hub for protein trafficking. In many cell types, the Golgi complex is organized as interconnected stacks of cisternae, forming a structure known as the Golgi ribbon. This ribbon undergoes dynamic remodelling during physiological processes, such as cell division, and under pathological conditions, including cancer and neurodegeneration. A critical step in the unlinking of the Golgi ribbon involves the phosphorylation of the stacking protein GRASP65, which leads to the separation of the ribbon into individual stacks, a process necessary for the G2/M transition of the cell cycle. However, existing tools for selectively manipulating the GRASP65 role in ribbon organization are limited by non-specific effects or technical challenges. Here, we present the development and characterization of a membrane-permeable peptide, R-GRASP65-S277, derived from GRASP65 and containing the phosphorylation site Ser277, which is essential for Golgi unlinking. This peptide effectively inhibited Golgi unlinking and mitotic entry in several cell lines, including cancer models. In contrast, a control peptide with a non-phosphorylatable alanine substitution (R-GRASP65-S277A) showed no such effect, confirming the specificity of the tool. Furthermore, the R-GRASP65-S277 peptide reversed Golgi unlinking induced by the chemotherapeutic agent doxorubicin, demonstrating its utility in studying stress-induced Golgi disassembly. These findings establish the R8-GRASP65-S277 peptide as a specific, potent, and scalable tool for probing the molecular mechanisms of Golgi unlinking, its regulation of cell cycle progression, and its potential contributions to pathological states. - Source: PubMed
Publication date: 2025/12/01
Cervigni Romina InesBonavita RaffaellaBarretta Maria LuisaSpano DanielaAyala InmaculadaMascanzoni FabiolaIannitti RobertaHenklein PetraMonti AlessandraRenna MaurizioDoti NunziannaColanzi Antonino - The settlement levels of indigenous bacteria show circadian rhythms in various regions of the rat alimentary tract. Numerous bacteria colonize between the mucosal folds of the ascending colon in rodents; however, the rhythm of bacteria colonizing the ascending colon remains to be clarified. Therefore, we first aimed to examine the diurnal changes in bacteria colonizing in the rat ascending colon. The settlement levels of indigenous bacteria were significantly higher at zeitgeber time (ZT) 18 (dark phase) than at ZT6 (light phase) in the region encompassing the aggregated lymphoid tissue in the ascending colon (ALT-AC). The bacterial composition around the ALT-AC was dominated by the phylum Firmicutes and the family Lachnospiraceae, displaying notable distinctions from the compositions found in cecal contents and feces. The relative abundance of some bacterial species around the ALT-AC, such as Mucispirillum schaedleri, changed significantly between ZT6 and ZT18. Furthermore, we explored the effect of bacterial expansion on gene expression in the ALT-AC at ZT18 by administrating antibiotics for 1 day to inhibit bacterial growth. The antibiotic-treated group exhibited significant downregulation of multiple genes, including those associated with cell proliferation (Plk3), differentiation into goblet cells (Spdef, Atoh1, Bhlha15), and Golgi organization (Gorasp2). These results suggested that indigenous bacteria around the rat ALT-AC undergo diurnal changes in both settlement levels, peaking at the dark phase, and bacterial composition. In addition, bacterial expansion during the dark phase can induce changes in the expression of diverse genes, including genes associated with goblet cell differentiation. - Source: PubMed
Publication date: 2025/08/26
Shimada AsakaKubota NaotoZheng SikaMorishita RinakoYokoyama ToshifumiHoshi NobuhikoMantani Youhei - Primordial follicle pool is the foundation of female reproductive life and abnormal primordial follicle activation may lead to severe diseases such as premature ovarian failure and premature ovarian insufficiency. Golgi reassembly stacking protein 2 (GORASP2) plays an important role in autophagy by regulating autophagy maturation through glycosylation modification. In the current study we found that GORASP2 is a key factor in mammalian primordial follicle activation through autophagy lysosome pathway. Knocking down of Gorasp2 in the ovaries of newborn mice led to decreased number of activated primary follicles, and the level of FSH (Follicle-stimulating Hormone) in the primary follicles was increased. Comparing with negative control ovaries, transcription profiling showed differentially expressed genes were mainly enriched in the autophagic lysosome, HIF-1 signaling pathway and PI3K-AKT signaling pathway. We found that the ratio of autophagy marker protein LC3-II/LC3-I increased and the level of SQSTM1 protein decreased by Western blot, indicating an elevated autophagy level in GORASP2-knockdown ovaries. Further examination demonstrated that the small G protein Rap1, a member of the Ras superfamily was activated after GORASP2 inhibition and the phosphorylation of mTOR was inhibited by disrupting the mTOR-Raptor interaction, thus initiating autophagy in primordial follicles. In addition, levels of ROS and ATP were increased and citrate lyase was decreased, suggesting a putative disrupted mitochondrial function. Finally, AKT signaling pathways were blocked and may also affect the developmental potential of these affected primordial follicles. In summary, our study emphasized the Golgi stacking protein GORASP2 as an important regulator in primordial follicle activation by participating in the initiation of autophagy, providing an experimental basis for the involvement of Golgi related components in the activation process of primordial follicles through autophagy pathway. This study also shed light upon the deeper understanding of primordial follicle activation related diseases and may contribute a new angle for their future treatment. - Source: PubMed
Hu SaifeiWang YipinWu TianLuo HuiChen JianhuaWang YingnanLi CaoYin SiyueGuo ZhihanZhu YanyanBian HaijunQian YunFeng Ruizhi - Improving treatment options for head and neck squamous cell carcinoma (HNSCC) requires a deeper understanding of the tumor microenvironment, particularly cancer-associated fibroblasts (CAFs). We previously reported that HNSCC-derived FGF2/bFGF (fibroblast growth factor 2) triggers cytokine release from CAFs via secretory autophagy. Here, using transmission electron microscopy, live-cell imaging, and immunofluorescence, we show that CAF autophagosomes transport cargo, including IL6, to the plasma membrane for secretion. Autophagy in CAFs is constitutive and independent of STAT3, MAPK1/ERK2-MAPK3/ERK1 and phosphoinositide 3-kinase (PI3K) signaling. Despite the significant role of secretory autophagy in CAFs, its molecular machinery has remained elusive. Using both a literature based, and an unbiased approach, we studied the molecular machinery involved in autophagosome trafficking in CAFs. We identified TRIM16, a protein previously reported to traffic to autophagosomes, upregulated in CAFs compared to normal oral fibroblasts. Immunohistochemistry of patient HNSCC stroma revealed co-expression of TRIM16 and LC3B, linking TRIM16 to autophagosome function. An unbiased proteomics profiling of immunoprecipitated LC3B vesicles in primary HNSCC CAFs revealed enrichment in trafficking proteins, focal adhesion, and mitochondrial proteins. We demonstrate that SEC22B, SNAP23, VAMP3, and STX4 colocalize with LC3B, IL6, and TRIM16 in CAFs. TRIM16 knockdown reduced autophagosomes at the plasma membrane and decreased IL6 secretion from CAFs. These findings uncover key molecular components involved in autophagy-mediated IL6 secretion in CAFs and suggest potential therapeutic targets for HNSCC.: ACTA2/αSMA: actin alpha 2, smooth muscle; CAF: cancer-associated fibroblasts; CM: conditioned media; CQ: chloroquine; DAPI: 4',6-diamidino-2-phenylindole; DMSO: dimethylsulfoxide; EGFP: enhanced green fluorescent protein; ELISA: enzyme-linked immunosorbent assay; ER: endoplasmic reticulum; FGF2/bFGF: fibroblast growth factor 2; FGFR: fibroblast growth factor receptor; GO: gene ontology; GORASP2/GRASP55: golgi reassembly stacking protein 2; HMGB1: high mobility group box 1; HNSCC: head and neck squamous cell carcinoma; HPV: human papillomavirus; IL6: interleukin 6; IP: immunoprecipitation; LC-MS/MS: liquid chromatography-mass spectrometry/mass spectrometry; LIR: LC3-interacting region; MAP1LC3B/LC3B: microtubule associated protein 1 light chain 3 beta; MAPK1/ERK2: mitogen-activated protein kinase 1; MAPK3/ERK1: mitogen-activated protein kinase 3; NFs: normal oral fibroblasts; NSCLC: non-small cell lung cancer; PLA: proximity ligation assay; SQSTM1/p62: sequestosome 1; STAT3: signal transducer and activator of transcription 3; SNAP23: synaptosome associated protein 23; SNARE: soluble N-ethyl-maleimide-sensitive factor attachment protein receptor; STX4: syntaxin 4; TEM: transmission electron microscopy; TGFB1: transforming growth factor beta 1; TMA: tissue microarray; TRIM: tri-partite motif; VAMP: vesicle associated membrane protein; VC: vehicle control. - Source: PubMed
Publication date: 2025/05/22
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