GPP130 Monoclonal Antibody [A1/118]
- Known as:
- GPP130 Monoclonal Antibody [A1/118]
- Catalog number:
- A-0580-100
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- EpigenTek
- Gene target:
- GPP130 Monoclonal Antibody [A1/118]
Related genes to: GPP130 Monoclonal Antibody [A1/118]
- Gene:
- CEP131 NIH gene
- Name:
- centrosomal protein 131
- Previous symbol:
- AZI1
- Synonyms:
- AZ1, KIAA1118
- Chromosome:
- 17q25.3
- Locus Type:
- gene with protein product
- Date approved:
- 2004-07-15
- Date modifiied:
- 2016-03-30
- Gene:
- GOLIM4 NIH gene
- Name:
- golgi integral membrane protein 4
- Previous symbol:
- GOLPH4
- Synonyms:
- GPP130, GIMPC, P138
- Chromosome:
- 3q26.2
- Locus Type:
- gene with protein product
- Date approved:
- 2001-04-27
- Date modifiied:
- 2016-10-05
Related products to: GPP130 Monoclonal Antibody [A1/118]
Related articles to: GPP130 Monoclonal Antibody [A1/118]
- Recent evidence has established a significant link between N4 acetylcytidine (ac4C) mRNA modification, mediated by N Acetyltransferase 10 (NAT10), and bone metabolism. Nonetheless, the precise role and regulatory targets of NAT10, along with its associated ac4C modification in human bone formation, remain inadequately characterized. This study employed bioinformatics analysis of transcriptomic datasets from primary osteoblasts of individuals with high versus low bone mineral density (BMD), alongside a curated set of ac4C-modified genes, to identify key differentially expressed genes (DEGs) regulated by this pathway within an osteogenic context. Overall, eleven key NAT10/ac4C-associated DEGs linked to BMD status were identified: CFD, CTSF, DCXR, FADS1, GOLIM4, IMPA2, MLEC, NCLN, NT5DC2, PTGFRN, and VASP. Notably, FADS1, NT5DC2, and PTGFRN emerged as crucial ac4C-modified genes across three machine learning models. Furthermore, the tri-gene signature (FADS1/NT5DC2/PTGFRN) showed excellent diagnostic performance in distinguishing different BMD statuses. In vitro validation using MC3T3-E1 osteoblastic cells revealed that the knockdown of NAT10 via lentiviral delivery markedly impaired cell proliferation and osteogenic differentiation. This impairment was evidenced by the results of the CCK-8 proliferation assay, alkaline phosphatase staining, and Alizarin Red staining. Additionally, qRT PCR analysis demonstrated a significant downregulation of FADS1 and NT5DC2 expression subsequent to NAT10 knockdown. These findings underscore the role of NAT10-mediated ac4C modification as a pivotal regulator of osteoblast activity and gene expression programs associated with BMD. This research offers novel insights into the regulation of bone metabolism and proposes potential diagnostic markers and therapeutic targets for osteoporosis. - Source: PubMed
Tang YWang QDong WJiang GLei MHu XWu YJiang WHao JHu Z - - Source: PubMed
Cui XiaoboBai YunfeiGao DongxueWang YapingWang BoqianWang Wei - From a previously performed proteomics screen, GPP130, or Golgi phosphoprotein of 130 kDa, was identified as a potential substrate of the proprotein convertase 7 (PC7; PCSK7). GPP130 is a type-II transmembrane protein with a luminal domain containing endosomal and Golgi-retrieval determinants, enabling a unique trafficking route. Most of the previous work on GPP130 relates to its binding and retrograde trafficking of the Shiga toxin. However, its cellular biology and its biochemical characterization remain understudied. Recently, GPP130 was reported to be implicated in cell cycle progression and cell proliferation in head and neck cancer cells. This led us to analyze the cBioPortal for Cancer Genomics, revealing that the GPP130/GOLIM4 gene is amplified in many cancers, including lung, ovarian, and cervical. This observation led us to use the A549 lung cancer cell line to investigate the growth-regulating roles of endogenous and overexpressed GPP130 and to analyze the impact of its cleavage/shedding by PC7 and/or Furin on cellular growth. Our cell-based assays suggest that GPP130 is a novel pro-protein convertase substrate that increases cell proliferation in A549, SKOV3, and HeLa cells, and that the latter activity is enhanced following its cleavage by PC7 and/or Furin into a membrane-bound N-terminal product and secreted C-terminal fragments. This novel work sheds light on the cell biology of the poorly characterized GPP130, its proliferative activity, and modulation upon its shedding by PC7 and Furin in lung cancer progression. - Source: PubMed
Publication date: 2025/06/26
Prabhala PriyankaDuval StephanieEvagelidis AlexandraLe Dévéhat MaïlysSachan VatsalSeidah Nabil G - Despite extensive efforts to develop strategies to inhibit cancer metastasis-the leading cause of cancer-related deaths-progress has been limited in recent decades. Epithelial-to-mesenchymal transition (EMT) initiates metastasis by enhancing the migratory capacity and plasticity of cancer cells, enabling them to escape the primary tumor site. Identifying vulnerabilities unique to mesenchymal cancer cells is, therefore, critical for developing effective antimetastatic therapies. Our prior research has highlighted the crucial role of the Golgi apparatus in EMT-driven cancer cell motility and metastasis. In this study, we investigated the antimigratory effects of various Golgi-disrupting compounds and identified Monensin, a polyether ionophore antibiotic, as a potent migration suppressor in mesenchymal non-small cell lung cancer (NSCLC) cells. Monensin treatment increases the pH within the Golgi lumen, inducing rapid exocytosis of the promigratory Golgi scaffold protein Golgi Integral Membrane Protein 4 (GOLIM4). GOLIM4 plays a key role in regulating cell motility and adhesion by modulating the post-Golgi trafficking of Talin 1 (TLN1), an essential focal adhesion component. Furthermore, we found that both GOLIM4 and TLN1 are highly expressed in mesenchymal cancer cells and are direct targets of microRNA-200b, a microRNA that is suppressed during EMT. Treatment with Monensin or depletion of GOLIM4 or TLN1 significantly impaired the migratory activity of mesenchymal NSCLC cells. In summary, this study demonstrates that Monensin exhibits potential antimetastatic activity by disrupting the promigratory GOLIM4-TLN1 axis in mesenchymal NSCLC cells. - Source: PubMed
Publication date: 2025/07/09
Tan XiaochaoCardin Derrick LWang ShikeXu YutingRussell William K - Ischemia-reperfusion injury (IRI) is a leading contributor to acute kidney injury (AKI), resulting in severe renal dysfunction and increased mortality. Despite progress in medical research, effective therapies for IRI remain limited. Recently, small extracellular vesicles (sEVs) originating from human umbilical cord mesenchymal stem cells (HucMSC-sEVs) have gained attention as potential therapeutic agents for alleviating organ damage. This study aimed to investigate the protective effects of HucMSC-sEVs in renal IRI and explore the underlying mechanisms involved. - Source: PubMed
Publication date: 2025/05/30
Peng XiangShi WeiYu HaitaoFeng ZhenweiWei ZongjieHe WeiyangGou XinXie Yongpeng