All Outputs (10)

Ca2+ Influx through TRPC Channels Is Regulated by Homocysteine–Copper Complexes (2023)
Journal Article
Chen, G., Zeng, B., Jiang, H., Daskoulidou, N., Saurabh, R., Chitando, R. J., & Xu, S. (2023). Ca2+ Influx through TRPC Channels Is Regulated by Homocysteine–Copper Complexes. Biomolecules, 13(6), Article 952. https://doi.org/10.3390/biom13060952

An elevated level of circulating homocysteine (Hcy) has been regarded as an independent risk factor for cardiovascular disease; however, the clinical benefit of Hcy lowering-therapy is not satisfying. To explore potential unrevealed mechanisms, we in... Read More about Ca2+ Influx through TRPC Channels Is Regulated by Homocysteine–Copper Complexes.

Mibefradil, a T-type Ca2+ channel blocker also blocks Orai channels by action at the extracellular surface (2019)
Journal Article
Li, P., Rubaiy, H. N., Chen, G.-L., Hallett, T., Zaibi, N., Zeng, B., Saurabh, R., & Xu, S.-Z. (2019). Mibefradil, a T-type Ca2+ channel blocker also blocks Orai channels by action at the extracellular surface. British Journal of Pharmacology, 176, 3845–3856. https://doi.org/10.1111/bph.14788

Background and purpose
Mibefradil (Mib), a T‐type Ca2+ channel blocker, has been investigated for treating solid tumours. However, its underlying mechanisms are still unclear. Here we aimed to investigate the pharmacological aspect of Mib on ORAI st... Read More about Mibefradil, a T-type Ca2+ channel blocker also blocks Orai channels by action at the extracellular surface.

ORAI channels are critical for receptor-mediated endocytosis of albumin (2017)
Journal Article
Zeng, B., Chen, G.-L., Garcia-Vaz, E., Bhandari, S., Daskoulidou, N., Berglund, L. M., Jiang, H., Hallett, T., Zhou, L.-P., Huang, L., Xu, Z.-H., Nair, V., Nelson, R. G., Ju, W., Kretzler, M., Atkin, S. L., Gomez, M. F., & Xu, S.-Z. (2017). ORAI channels are critical for receptor-mediated endocytosis of albumin. Nature communications, 8(1), Article 1920. https://doi.org/10.1038/s41467-017-02094-y

Impaired albumin reabsorption by proximal tubular epithelial cells (PTECs) has been highlighted in diabetic nephropathy (DN), but little is known about the underlying molecular mechanisms. Here we find that ORAI1-3, are preferentially expressed in PT... Read More about ORAI channels are critical for receptor-mediated endocytosis of albumin.

High glucose enhances store-operated calcium entry by upregulating ORAI/STIM via calcineurin-NFAT signalling (2014)
Journal Article
Daskoulidou, N., Xu, S. Z., Zeng, B., Gomez, M. F., Berglund, L. M., Atkin, S. L., Jiang, H., Griffin, S., Ayoola, J., Bhandari, S., Kotova, O., Chen, G. L., Griffin, S., Jiang, H., Berglund, L. M., Zeng, B., & Daskoulidou, N. (2015). High glucose enhances store-operated calcium entry by upregulating ORAI/STIM via calcineurin-NFAT signalling. Journal of Molecular Medicine, 93(5), 511-521. https://doi.org/10.1007/s00109-014-1234-2

© 2014, Springer-Verlag Berlin Heidelberg. Abstract: ORAI and stromal interaction molecule (STIM) are store-operated channel molecules that play essential roles in human physiology through a coupling mechanism of internal Ca 2+ store to Ca 2+ influx.... Read More about High glucose enhances store-operated calcium entry by upregulating ORAI/STIM via calcineurin-NFAT signalling.

The ryanodine receptor agonist 4-chloro-3-ethylphenol blocks ORAI store-operated channels: 4-Chloro-3-ethylphenol inhibits ORAI channels (2014)
Journal Article
Zeng, B., Chen, G.-L., Daskoulidou, N., & Xu, S.-Z. (2014). The ryanodine receptor agonist 4-chloro-3-ethylphenol blocks ORAI store-operated channels: 4-Chloro-3-ethylphenol inhibits ORAI channels. British Journal of Pharmacology, 171(5), 1250-1259. https://doi.org/10.1111/bph.12528

Background
Depletion of the Ca2+ store by ryanodine receptor (RyR) agonists induces store‐operated Ca2+ entry (SOCE). 4‐Chloro‐3‐ethylphenol (4‐CEP) and 4‐chloro‐m‐cresol (4‐CmC) are RyR agonists commonly used as research tools and diagnostic reagen... Read More about The ryanodine receptor agonist 4-chloro-3-ethylphenol blocks ORAI store-operated channels: 4-Chloro-3-ethylphenol inhibits ORAI channels.

Involvement of TRPC Channels in Lung Cancer Cell Differentiation and the Correlation Analysis in Human Non-Small Cell Lung Cancer (2013)
Journal Article
Jiang, H. N., Zeng, B., Zhang, Y., Daskoulidou, N., Fan, H., Qu, J. M., & Xu, S. Z. (2013). Involvement of TRPC Channels in Lung Cancer Cell Differentiation and the Correlation Analysis in Human Non-Small Cell Lung Cancer. PLoS ONE, 8(6), Article e67637. https://doi.org/10.1371/journal.pone.0067637

The canonical transient receptor potential (TRPC) channels are Ca2+-permeable cationic channels controlling the Ca2+ influx evoked by G protein-coupled receptor activation and/or by Ca2+ store depletion. Here we investigate the involvement of TRPCs i... Read More about Involvement of TRPC Channels in Lung Cancer Cell Differentiation and the Correlation Analysis in Human Non-Small Cell Lung Cancer.

TRPC Channels and Their Splice Variants are Essential for Promoting Human Ovarian Cancer Cell Proliferation and Tumorigenesis (2013)
Journal Article
Zeng, B., Yuan, C., Yang, X., Atkin, S. L., & Xu, S.-Z. (2013). TRPC Channels and Their Splice Variants are Essential for Promoting Human Ovarian Cancer Cell Proliferation and Tumorigenesis. Current Cancer Drug Targets, 13(1), 103-116. https://doi.org/10.2174/156800913804486629

TRPC channels are Ca2+-permeable cationic channels controlling Ca2+ influx response to the activation of G protein-coupled receptors and protein tyrosine kinase pathways or the depletion of Ca2+ stores. Here we aimed to investigate whether TRPC can a... Read More about TRPC Channels and Their Splice Variants are Essential for Promoting Human Ovarian Cancer Cell Proliferation and Tumorigenesis.

Store-independent pathways for cytosolic STIM1 clustering in the regulation of store-operated Ca2+ influx (2012)
Journal Article
Zeng, B., Chen, G.-L., & Xu, S. Z. (2012). Store-independent pathways for cytosolic STIM1 clustering in the regulation of store-operated Ca2+ influx. Biochemical Pharmacology, 84(8), 1024-1035. https://doi.org/10.1016/j.bcp.2012.07.013

STIM1 is a Ca 2+ sensing molecule. Once the Ca 2+ stores are depleted, STIM1 moves towards the plasma membrane (PM) (translocation), forms puncta (clustering), and triggers store-operated Ca 2+ entry (SOCE). Although this process has been regarded as... Read More about Store-independent pathways for cytosolic STIM1 clustering in the regulation of store-operated Ca2+ influx.

Pharmacological comparison of novel synthetic fenamate analogues with econazole and 2-APB on the inhibition of TRPM2 channels (2012)
Journal Article
Chen, G.-L., Zeng, B., Eastmond, S., Elsenussi, S. E., Boa, A. N., & Xu, S.-Z. (2012). Pharmacological comparison of novel synthetic fenamate analogues with econazole and 2-APB on the inhibition of TRPM2 channels. British Journal of Pharmacology, 167(6), 1232-1243. https://doi.org/10.1111/j.1476-5381.2012.02058.x

BACKGROUND: Fenamate analogues, econazole and 2-APB are inhibitors of TRPM2 channels, which have been used as research tools. However, these compounds have different chemical structures and therapeutic applications. Here we aimed to investigate the p... Read More about Pharmacological comparison of novel synthetic fenamate analogues with econazole and 2-APB on the inhibition of TRPM2 channels.

Activation of TRPC cationic channels by mercurial compounds confers the cytotoxicity of mercury exposure (2011)
Journal Article
Xu, S.-Z., Zeng, B., Atkin, S. L., Daskoulidou, N., Chen, G.-L., & Lukhele, B. (2012). Activation of TRPC cationic channels by mercurial compounds confers the cytotoxicity of mercury exposure. Toxicological Sciences, 125(1), 56 - 68. https://doi.org/10.1093/toxsci/kfr268

Mercury is an established worldwide environmental pollutant with well-known toxicity affecting neurodevelopment in humans, but the molecular basis of cytotoxicity and the detoxification procedure are still unclear. Here we examined the involvement of... Read More about Activation of TRPC cationic channels by mercurial compounds confers the cytotoxicity of mercury exposure.