Maturation, Barrier Function, Aging, and Breakdown of the Blood–Brain Barrier
Shamim I. Ahmad in Aging: Exploring a Complex Phenomenon, 2017
AJs are found throughout the CNS microvasculature and are responsible for intercellular adherence between adjacent ECs (Hawkins and Davis 2005, Sanchez-Covarrubias et al. 2014). AJs are composed of multiple protein components including vascular endothelium (VE) cadherin, actin, and catenin (Vorbrodt and Dobrogowska 2003). Cell–cell adhesion is mediated by homophilic interactions of VE-cadherin expressed on adjacent ECs. Such interactions mediate calcium-dependent cell adhesion by binding to the actin cytoskeleton. Cytoskeletal binding occurs via catenin accessory proteins. Specifically, β-catenin links VE-cadherin to α-catenin, an interaction that induces the direct binding to actin (Oldendorf et al. 1977, Sanchez del Pino et al. 1995) (Figure 15.3).
Bone Regeneration Effect of Cassia occidentalis Linn. Extract and Its Isolated Compounds
Brijesh Kumar, Vikas Bajpai, Vikaskumar Gond, Subhashis Pal, Naibedya Chattopadhyay in Phytochemistry of Plants of Genus Cassia, 2021
In cultures of rat chondrocytes, emodin suppressed the cytotoxic impact of IL-1β, downregulated the expressions of MMP-1 and MMP-13 and inhibited the ERK and Wnt/β-catenin signaling (Liu et al., 2018). In murine chondrogenic cell line, ATDC5, emodin treatment caused the loss of cell viability at 15- and 20 μM. However, at 10 μM, emodin blocked the LPS-induced apoptosis of and production of proinflammatory cytokines (TNFα, IL-6 and MCP1) from ATDC5 cells. The pro-survival, anti-apoptotic and anti-inflammatory roles of emodin in ATDC5 were likely regulated by the long noncoding RNA, taurine upregulated gene 1-mediated notch and NFκB pathways (Liang and Ren, 2018). Given this action mechanism of emodin chondrocytes, a salutary role of this compound in OA is surmised.
The rectum
Professor Sir Norman Williams, Professor P. Ronan O’Connell, Professor Andrew W. McCaskie in Bailey & Love's Short Practice of Surgery, 2018
The most common abnormality found in colorectal cancer is mutation in the Wnt signaling pathway, which increases cell signalling activity. The mutations can be inherited or acquired. The most commonly mutated gene is the APC gene, which results in accumulation of the P-catenin protein. P-catenin activates the transcription of various proto-oncogenes that are responsible for normal cell renewal and differentiation, but when overexpressed can cause cancer. Many other mutations, other than in the Wnt signaling pathway, are found in colorectal cancer, and include mutations in the TP53 gene that controls normal cell division and death, and mutations in genes responsible for programmed cell death, such as the gene encoding transforming growth factor (TGF)-P and DCC (deleted in colorectal cancer). Other genetic abnormalities include overexpression of oncogenes, including genes encoding the proteins KRAS (Kirsten rat sarcoma homologue), RAF (rapidly accelerated fibrosarcoma) and PI3K (phosphoinositide 3-kinase), which lead to increased cell proliferation, and inactivation of tumour suppressor genes, such as PTEN (phosphatase and tensin homologue), which normally inactivates the PI3K signalling pathway.
Synthesis and biological evaluation of thieno[3,2-c]pyrazol-3-amine derivatives as potent glycogen synthase kinase 3β inhibitors for Alzheimer’s disease
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2022
Ning Yan, Xiao-Long Shi, Long-Qian Tang, De-Feng Wang, Xun Li, Chao Liu, Zhao-Peng Liu
GSK-3β is implicated in the Wnt/β-catenin signalling pathway, which plays an important role in neuronal development29. GSK-3β, together with adenomatous polyposis coli (APC), Axin, and casein kinase 1 (CK1), form a ploy-protein complex that regulates the hyperphosphorylation of β-catenin. Phospho-β-catenin is recognised by ubiquitin and degraded by proteasomes52–54. Pharmacological inhibition of GSK-3β leads to the activation and stabilisation of β-catenin, subsequently resulting in the accumulation of β-catenin in cytoplasm55–57. The activation of Wnt/β-catenin signalling pathway can promote synaptic growth, alleviate spatial memory impairment and neurodegeneration in Alzheimer’s models 58–60. Moreover, β-catenin also plays a pivotal role in cell adhesion complexes. The combination of β-catenin and N-cadherin elevates cell-to-cell interactions which is prerequisite for neuronal differentiation61,62. Therefore, we further evaluated the effect of 16b on β-catenin. In agreement with its GSK-3β inhibitory activity on SH-SY5Y cells, 16b increased β-catenin abundance in a dose-dependent manner. As shown in Figure 6(B), after treatment with 16b at the concentration of 5 μM, 10 μM and 20 μM, the β-catenin/GADPH ratio increased from 0.41 of the control to 0.54, 0.64, 0.76, respectively.
Qici Sanling decoction suppresses bladder cancer growth by inhibiting the Wnt/Β-catenin pathway
Published in Pharmaceutical Biology, 2019
Hua Gong, Weihua Chen, Lanhua Mi, Dan Wang, Youkang Zhao, Chao Yu, Aiguang Zhao
It has been reported that β-catenin plays a central role in cell adhesion (McCrea et al. 1991). Other studies have revealed a regulatory role of β-catenin in contributing to the transmission of proliferation signals to the WNT/T-cell factor pathway (Miller and Moon 1996; Peifer 1997). Usually, β-catenin is located in the cell membrane to carry out its cell adhesion functions. The function of β-catenin in the cytoplasm and nucleus reflects its role as a mediator of WNT/β-catenin signalling (Barth et al. 1997). C-myc (He et al. 1998) and cyclin D1 were reported as putative target genes of WNT signalling. In this study, to test the effects of QCSL on WNT/β-catenin signalling, we immunoblotted for components of the pathway and found that increased doses of QCSL dramatically inhibited β-catenin, survivin, c-myc and cyclin D1 (Figure 4). As reported, survivin is upregulated in almost all human tumours including bladder cancer (Ambrosini et al. 1997; Fukuda and Pelus 2006). Survivin could be regulated by Wnt signalling and may play an antagonist role in cancer stem cells (Reya et al. 2001).
Suspended cell lines for inactivated virus vaccine production
Published in Expert Review of Vaccines, 2023
Jiayou Zhang, Zhenyu Qiu, Siya Wang, Zhenbin Liu, Ziling Qiao, Jiamin Wang, Kai Duan, Xuanxuan Nian, Zhongren Ma, Xiaoming Yang
The calcium dependent cell adhesins (cadherin) family is one of the earliest adhesion molecules that Takeichi discovered to mediate cell aggregation. In the presence of Ca2+, it can resist protease hydrolysis. The connection between the cytoskeleton transmembrane protein E-cadherin (also known as uvomorulin, L-CAM, cell CAM 120/80, or ARC-1) and actin filament is the key to cell-cell adhesion. Cells lacking E-cadherin expression do not aggregate or adhere to each other because the production of cadherin-catenin adhesion complexes is affected [106]. α-Catenin is a key subunit of the cadherin catenin adhesion complex, which affects cell-cell adhesion. In the absence of stable α-Catenin expression in poorly differentiated cell lines, the addition of α- Catenin cDNA will increase Ca2+-dependent cell-cell aggregation, indicating that α-Catenin directly leads to the loss of cell-cell adhesion in some cell lines [109]. In α-Catenin-ablated keratinocytes, cell-cell connection defects could be observed using immunofluorescence microscopy along with excessive cell proliferation [110].
Related Knowledge Centers
- Actin
- Cadherin
- Cell Adhesion
- Epithelium
- Protein
- Cell
- Catenin Beta-1
- Plakoglobin
- Δ-Catenin
- Protein Dynamics