CLDN7 antibody - middle region (ARP33613_P050)
- Known as:
- CLDN7 (anti-) - middle region (ARP33613_P050)
- Catalog number:
- arp33613_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- CLDN7 antibody - middle region (ARP33613_P050)
Related genes to: CLDN7 antibody - middle region (ARP33613_P050)
- Gene:
- CLDN7 NIH gene
- Name:
- claudin 7
- Previous symbol:
- CEPTRL2, CPETRL2
- Synonyms:
- Hs.84359
- Chromosome:
- 17p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-11-19
- Date modifiied:
- 2015-09-11
Related products to: CLDN7 antibody - middle region (ARP33613_P050)
Related articles to: CLDN7 antibody - middle region (ARP33613_P050)
- Hydrocephalus is characterized by the abnormal accumulation of cerebrospinal fluid (CSF) due to disrupted secretion, circulation, or reabsorption. CSF homeostasis is regulated by ion and water channels on choroid plexus epithelial (CPe) cells, including the mechanosensitive cation channel, which is transient receptor potential vanilloid 4 (TRPV4). Although TRPV4 antagonism prevents hydrocephalus progression in rats, how TRPV4 activity modulates CSF production remains unclear. Because TRPV4 function is phosphorylation-dependent, we examined its activation (GSK1016790A) and inhibition (RN1734) and the downstream signaling alterations in the human choroid plexus papilloma cell line (HIBCPP) using phosphoproteomic mass spectrometry. Our phosphoproteomic analysis revealed significant changes in kinases and tight junction (TJ) proteins regulating epithelial barrier integrity. TRPV4 activation altered the phosphorylation of TJ proteins, including Zonula Occludens-1 (ZO-1) and Claudin-7 (CLDN7), as well as AMP-activated protein kinase (AMPK), with a notable increase in the phosphorylation of the AMPK inhibitory site (Ser496). Using electrophysiological techniques, we showed that AMPK had a more profound effect on epithelial barrier function than on net transepithelial electrolyte ion flux. The inhibition of AMPK-associated inhibitory phosphorylation prior to TRPV4 activation increased barrier tightness, and these permeability changes were mirrored by changes in ZO-1 continuity within junctional complexes. Furthermore, the pharmacological modulation of AMPK-associated signaling altered TRPV4-stimulated epithelial conductance, while metformin treatment also reduced TRPV4-stimulated conductance under the experimental conditions used. These findings suggest an interaction between TRPV4 signaling, AMPK phosphorylation, and epithelial barrier regulation that warrants further mechanistic investigation. Overall, these findings provide insight into signaling pathways associated with the TRPV4-dependent regulation of choroid plexus epithelial barrier properties and provide a basis for the further investigation of their relevance to CSF homeostasis and hydrocephalus. - Source: PubMed
Publication date: 2026/09/18
Mahendran GowthamiTorabi MaryamBlazer-Yost Bonnie L - 6PPD-quinone (6PPD-Q), a transformation product of the tire antioxidant 6PPD, causes acute mortality in several salmonid species, but its toxicity varies markedly among fish species. Disruption of vascular-barrier integrity and inflammatory signaling has been proposed as a key mechanism of 6PPD-Q toxicity. However, it remains unclear whether related transcriptional responses are specific to lethal effects. In this study, juvenile Japanese medaka (Oryzias latipes) aged 30-35 days post-hatch, an insensitive species, were exposed to 6PPD-Q at 31-500 μg/L to examine acute lethality and the expression of selected genes related to tight-junction function, inflammation, antioxidant defense, and neurotoxicity. No mortality or abnormal behavior was observed after 48 h of exposure at nominal concentrations up to 500 μg/L. After 24 h of exposure, the tight-junction-related genes cldn7, cldn15, and zo1 generally showed concentration-dependent increases at concentrations ranging from 62.5 to 500 μg/L. In contrast, the inflammation-related gene il1b was downregulated, whereas il8 was unaffected. Antioxidant- and neurotoxicity-related genes showed modest or nonmonotonic responses, including decreases in cat, gpx1, and ache. These results demonstrate that 6PPD-Q can alter tight-junction- and epithelial-barrier-related genes and other stress-response genes in medaka without causing overt acute toxicity. Thus, transcriptional changes in these genes alone are not sufficient predictors of acute lethality, although functional vascular-barrier disruption may remain a critical key event in sensitive salmonids. - Source: PubMed
Publication date: 2026/08/29
Hiki Kyoshiro - Hydrocephalus is characterized by abnormal accumulation of cerebrospinal fluid (CSF) due to disrupted secretion, circulation, or reabsorption. CSF homeostasis is regulated by ion and water channels on choroid plexus epithelial (CPe) cells, including the mechanosensitive cation channel, transient receptor potential vanilloid 4 (TRPV4). Although TRPV4 antagonism prevents hydrocephalus progression in rats, how TRPV4 activity modulates CSF production remains unclear. - Source: PubMed
Publication date: 2026/07/18
Mahendran GowthamiTorabi MaryamBlazer-Yost Bonnie - Stomach infection with the bacterium () can cause chronic gastric inflammation, metaplasia (transdifferentiation of mature cell types), dysplasia (abnormal cells), and finally cancer. Obesity can also increase gastric cancer risk. However, host- interactions during obesity are poorly understood. Here we investigated the impact of diet-induced obesity in two mouse models of -associated disease. To model chronic gastric inflammation, we used C57BL/6 mice, and to model more severe disease, we used transgenic mice in which tamoxifen induces gastric expression of a constitutively active allele, leading to metaplasia. We fed mice a high-fat diet (60% kilocalories from fat) to induce obesity, or a matched control diet (10% kilocalories from fat), then infected them with or mock-infected them. In mock-infected C57BL/6 mice, high-fat diet had a minimal impact on gastric pathology and gene expression. In -infected C57BL/6 mice, high-fat diet increased inflammation at the junction between the glandular stomach and non-glandular forestomach, a squamous epithelium similar to the human esophagus, and increased gastric expression of the cancer-associated genes and . In KRAS+ mice with or without infection, the impact of diet-induced obesity was more apparent, with increased metaplasia and dysplasia (abnormal cells). As well, high-fat diet caused an expansion of metaplastic pit cells, a lineage we previously found to be associated with -driven inflammation. Thus, in these mouse models, diet-induced obesity does not directly drive gastric immunopathology, but enhances the development of pre-cancerous changes under susceptible conditions. - Source: PubMed
Publication date: 2026/07/10
Zhao XuyaoWojcicki NicholasKim Kee-HongLanman Nadia AtallahPillai Viju VijayanO'Brien Valerie Phoebe - Claudin-7 is a basolaterally enriched tight junction protein that participates in membrane complexes with EpCAM and Trop-2, linking epithelial adhesion to barrier organization. Although proteolytic processing of EpCAM/Trop-2 has been proposed to regulate this complex, its functional consequences for claudin-7 remain unresolved. Here, we define the role of matriptase in regulating claudin-7 dynamics in HaCaT human keratinocytes. Under steady-state conditions, matriptase knockout had only modest effects on claudin-7 distribution, suggesting a limited role in initial complex formation. In contrast, induction of matriptase autoactivation by mildly acidic stress triggered rapid and pronounced remodeling of claudin-7 complex in parental cells. Claudin-7 underwent progressive redistribution from continuous junctional staining to discontinuous bar-like structures, followed by the appearance of abundant intracellular puncta consistent with endocytosed vesicles, ultimately leading to its removal from the cell surface. This dynamic process was temporally coordinated and accompanied by increased accessibility of the claudin-7 C-terminus, indicating disassembly of claudin-7 complexes. These changes were abolished in matriptase-deficient cells, in which claudin-7 remained stably associated with cell-cell interfaces and failed to internalize. Suppression of matriptase autoactivation by NaCl similarly prevented claudin-7 internalization, demonstrating that proteolytic activity is required for this process. Notably, adherens junctions remained largely intact with E-cadherin continuously localized at cell-cell interfaces. Collectively, these findings establish that matriptase proteolytic activity is essential for disassembly and internalization of claudin-7 complex. This work supports a model in which the EpCAM/Trop-2-claudin-7 axis functions as a protease-regulated membrane complex that dynamically modulates epithelial organization. - Source: PubMed
Publication date: 2026/07/13
Kao Yu-Ling AHuang He-YuYu Yin SHuang NanxiChan Ya-ChinLee Chen-RayJohnson Michael DLin Chen-Yong