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The protein encoded by TRPM2 is a calcium-permeable cation channel that is regulated by free intracellular ADP-ribose. Additionally we are shipping TRPM2 Antibodies (95) and many more products for this protein.
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Study determined the sequence of pig TRPC1 and TRPC3-7 channels and found pig TRPC cDNAs resemble their human homologs more than the others .
heteromeric cation channels comprised of the TRPP2 mutant and the TRPC3 (show TRPC3 Proteins) or TRPC7 protein induce enhanced receptor-activated Ca(2 (show CA2 Proteins)+) influx that may lead to dysregulated cell growth in ADPKD
oxidative stress activated the TRPM2 (show CLU Proteins)-CaMKII (show CAMK2G Proteins) cascade to further induce intracellular ROS (show ROS1 Proteins) production, which led to mitochondria fragmentation and loss of mitochondrial membrane potential
The work summarized here shows that TRPM2 (show CLU Proteins) channels protect cardiac myocytes from ischaemia-reperfusion injury and tumour cells from doxorubicin toxicity, and demonstrates that the mechanisms involve preservation of mitochondrial bioenergetics and modulation of ROS (show ROS1 Proteins)
Activation of TRPM2 (show CLU Proteins) channels, however, caused intracellular release of not only Ca(2 (show CA2 Proteins)+) but also of Zn(2+) Intriguingly, elevation of intracellular Zn(2+) faithfully reproduced all of the effects of H2O2, whereas Ca(2 (show CA2 Proteins)+) showed opposite effects. Interestingly, H2O2 caused increased trafficking of Zn(2+)-enriched lysosomes to the leading edge of migrating cells, presumably to impart polarisation of Zn(2+) location.
neutrophils sense reactive oxygen species via the TRPM2 (show CLU Proteins) channel to arrest migration at their target site.
The inhibitory function of oxidant sensing by TRPM2 (show CLU Proteins) requires the oxidation of Cys549, which then induces TRMP2 binding to formyl peptide receptor 1 (FPR1 (show FPR1 Proteins)) and subsequent FPR1 (show FPR1 Proteins) internalization and signaling inhibition
findings demonstrate the important function of TRPM2 (show CLU Proteins) in modulation of cell survival through mitochondrial ROS (show ROS1 Proteins), and the potential of targeted inhibition of TRPM2 (show CLU Proteins) as a therapeutic approach to reduce cellular bioenergetics, tumor growth, and enhance susceptibility to chemotherapeutic agents.
Study demonstrate that PRL (show PRL Proteins) is necessary for the survival of (retinal pigment epithelium) RPE (show RPE Proteins) under normal and advancing age conditions and, identified SIRT2 (show SIRT2 Proteins) and TRPM2 (show CLU Proteins) as molecular targets for the antioxidant and antiapoptotic actions of PRL (show PRL Proteins) in the RPE (show RPE Proteins).
TRPM2 (show CLU Proteins) has a role in the DNA damage response of T cell leukemia cells in a BCL-2 (show BCL2 Proteins) dependent manner
Data show that HEK293 cells expressing low levels of receptor potential melastatin 2 (TRPM2) chan (show TRPM3 Proteins)nel wer (show CLU Proteins)e more susceptible to silica nanoparticles (NPs) than those expressing high levels of TRPM2.
This is expected to provide a basis for inhibiting TRPM2 (show CLU Proteins) for the improved treatment of breast cancer, which potentially includes treating breast tumors that are resistant to chemotherapy due to their evasion of apoptosis.
this study shows that TRPM2 ion channels regulate macrophage polarization and gastric inflammation during Helicobacter pylori infection
Overexpression of TRPM2 channel prevented neutrophil transendothelial migration and vascular injury.
These findings of this study suggest that TRPM2 channels play an essential role in mediating hypoxic-ischemic brain injury in neonatal mice.
TRPM2 regulates phagosomal acidification, and is essential for the bacterial killing function of macrophages.
Lysophosphatidylcholine induces intracellular Ca(2 (show CA2 Proteins)+) influx and increases phosphorylation of p38 MAPK (show MAPK14 Proteins) via TRPM2, which in turn activates microglia.
The current study demonstrated that a physiological concentration of adrenaline attenuates insulin (show INS Proteins) release via coupling of alpha2A-adrenoceptor to cAMP/TRPM2 signaling.
Trpm2 does not seem to play a major role in myeloid leukemogenesis. Additionally, loss of Trpm2 does not augment the cytotoxicity of standard AML (show RUNX1 Proteins) chemotherapeutic agents.
TRPM2 channels contribute to visceral nociception in response to noxious stimuli under normal conditions and visceral hypersensitivity in pathological conditions.
Data show that macrophages from young mice showed lower transient receptor potential melastatin 2 (show TRPM3 Proteins) (TRPM2) expression than those from senescent mice and had lower viability after silica nanoparticles (NPs (show NPS Proteins)) exposure than those from senescent ones.
TRPM2 activation is likely to be mediated by ADP-ribose production via PARP (show PARP1 Proteins) pathway
The protein encoded by this gene is a calcium-permeable cation channel that is regulated by free intracellular ADP-ribose. The encoded protein is activated by oxidative stress and confers susceptibility to cell death. Several alternatively spliced transcript variants of this gene have been described, but their full-length nature is not known.
transient receptor potential cation channel, subfamily M, member 2
, transient receptor potential cation channel, subfamily C, member 7
, transient receptor potential cation channel, subfamily C, member 7-like
, short transient receptor potential channel 7-like
, transient receptor potential cation channel subfamily M member 2-like
, transient receptor potential channel subfamily C member 7
, estrogen-responsive element-associated gene 1 protein
, long transient receptor potential channel 2
, transient receptor potential cation channel subfamily M member 2
, transient receptor potential channel 7
, transient receptor protein 7
, transient receptor potential melastatin family 2