Response by Mittal et al to Letter Regarding Article, “Neutrophil Activation of Endothelial Cell-Expressed TRPM2 Mediates Transendothelial Neutrophil Migration and Vascular Injury”

Mittal, Manish; Nepal, Saroj; Tsukasaki, Yoshikazu; Hecquet, Claudie; Soni, Dheeraj; Tiruppathì, Chinnaswamy; Malik, Asrar B.; Rehman, Jalees

doi:10.1161/circresaha.117.312146

Cited by 2 publications

(3 citation statements)

References 7 publications

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“…In support, Malik's group demonstrated that TRPM2-mediated Ca 2+ influx is required for VE-cadherin phosphorylation at Y73, a process necessary for the disassembly of adherens junctions and opening of the paracellular pathways, thereby allowing PMN adhesion and transmigration (Mittal et al, 2017). Indeed, when challenged with LPS injection, TRPM2-depleted mice exhibited reduced PMN accumulation, inflammation, and mortality, suggesting a protective role of TRPM2 inhibition (Mittal et al, 2017). Using the 8-Br-cADPR TRPM2 antagonist, Eraslan and colleagues also showed the therapeutic benefits of TRPM2 inhibition, as it prevented ischemic acute kidney inflammation through reduced production of TNF-α, IL-1β, and myeloperoxidase activity (Eraslan et al, 2019).…”

Section: Trpm2 In Innate Inflammation and Bacterial Infectionmentioning

confidence: 97%

“…Similarly, Yonezawa and collaborators demonstrated that inhibiting TRPM2 reduces bleomycin (BLM)-induced lung inflammation through decreased polymorphonuclear leukocyte (PMN) recruitment and reduced secretion of inflammatory cytokines, including IL-1β, MIP-2, and TNF-α (Yonezawa et al, 2016). In support, Malik's group demonstrated that TRPM2-mediated Ca 2+ influx is required for VE-cadherin phosphorylation at Y73, a process necessary for the disassembly of adherens junctions and opening of the paracellular pathways, thereby allowing PMN adhesion and transmigration (Mittal et al, 2017). Indeed, when challenged with LPS injection, TRPM2-depleted mice exhibited reduced PMN accumulation, inflammation, and mortality, suggesting a protective role of TRPM2 inhibition (Mittal et al, 2017).…”

Section: Trpm2 In Innate Inflammation and Bacterial Infectionmentioning

confidence: 98%

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TRPM2: bridging calcium and ROS signaling pathways—implications for human diseases

Maliougina

Hiani

2023

Front. Physiol.

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TRPM2 is a versatile and essential signaling molecule that plays diverse roles in Ca2+ homeostasis and oxidative stress signaling, with implications in various diseases. Research evidence has shown that TRPM2 is a promising therapeutic target. However, the decision of whether to activate or inhibit TRPM2 function depends on the context and specific disease. A deeper understanding of the molecular mechanisms governing TRPM2 activation and regulation could pave the way for the development of innovative therapeutics targeting TRPM2 to treat a broad range of diseases. In this review, we examine the structural and biophysical details of TRPM2, its involvement in neurological and cardiovascular diseases, and its role in inflammation and immune system function. In addition, we provide a comprehensive overview of the current knowledge of TRPM2 signaling pathways in cancer, including its functions in bioenergetics, oxidant defense, autophagy, and response to anticancer drugs.

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Section: Trpm2 In Innate Inflammation and Bacterial Infectionmentioning

confidence: 97%

Section: Trpm2 In Innate Inflammation and Bacterial Infectionmentioning

confidence: 98%

TRPM2: bridging calcium and ROS signaling pathways—implications for human diseases

Maliougina

Hiani

2023

Front. Physiol.

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“…The TRPM2 channel is a non-selective, Ca 2+ -permeable cation channel, widely expressed in the CNS [110] but also in heart and endothelial cells [111,112], pancreatic β-cells [113], and immune cells [114]. TRPM2 functions as a potent cellular oxidative stress sensor activated by the second messenger adenosine diphosphoribose (ADPR), which is generated in mitochondria in response to oxidative stress [115].…”

Section: Trpm2mentioning

confidence: 99%

Interaction of Calmodulin with TRPM: An Initiator of Channel Modulation

Vydra Bousova,

Zouharova,

Jiraskova

et al. 2023

IJMS

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Transient receptor potential melastatin (TRPM) channels, a subfamily of the TRP superfamily, constitute a diverse group of ion channels involved in mediating crucial cellular processes like calcium homeostasis. These channels exhibit complex regulation, and one of the key regulatory mechanisms involves their interaction with calmodulin (CaM), a cytosol ubiquitous calcium-binding protein. The association between TRPM channels and CaM relies on the presence of specific CaM-binding domains in the channel structure. Upon CaM binding, the channel undergoes direct and/or allosteric structural changes and triggers down- or up-stream signaling pathways. According to current knowledge, ion channel members TRPM2, TRPM3, TRPM4, and TRPM6 are directly modulated by CaM, resulting in their activation or inhibition. This review specifically focuses on the interplay between TRPM channels and CaM and summarizes the current known effects of CaM interactions and modulations on TRPM channels in cellular physiology.

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Response by Mittal et al to Letter Regarding Article, “Neutrophil Activation of Endothelial Cell-Expressed TRPM2 Mediates Transendothelial Neutrophil Migration and Vascular Injury”

Cited by 2 publications

References 7 publications

TRPM2: bridging calcium and ROS signaling pathways—implications for human diseases

TRPM2: bridging calcium and ROS signaling pathways—implications for human diseases

Interaction of Calmodulin with TRPM: An Initiator of Channel Modulation

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