Expression of transient receptor potential vanilloid 1 (TRPV1) and 2 (TRPV2) in human peripheral blood

Saunders, Cassandra; Kunde, Dale; Crawford, Amanda; Geraghty, Dominic P.

doi:10.1016/j.molimm.2006.04.027

Cited by 91 publications

(64 citation statements)

References 15 publications

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“…It is also expressed in nonneuronal cells, such as prostate cells (19,35), or in human blood cells, suggesting that, in addition to its role as a noxious heat sensor (34), this channel may encompass other cellular functions (36). One of such function of TRPV2 in cancer cells is the control of cell migration.…”

Section: Discussionmentioning

confidence: 99%

Role of Cationic Channel TRPV2 in Promoting Prostate Cancer Migration and Progression to Androgen Resistance

et al. 2010

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Castration resistance in prostate cancer (PCa) constitutes an advanced, aggressive disease with poor prognosis, associated with uncontrolled cell proliferation, resistance to apoptosis, and enhanced invasive potential. The molecular mechanisms involved in the transition of PCa to castration resistance are obscure. Here, we report that the nonselective cationic channel transient receptor potential vanilloid 2 (TRPV2) is a distinctive feature of castration-resistant PCa. TRPV2 transcript levels were higher in patients with metastatic cancer (stage M1) compared with primary solid tumors (stages T2a and T2b). Previous studies of the TRPV2 channel indicated that it is primarily involved in cancer cell migration and not in cell growth. Introducing TRPV2 into androgen-dependent LNCaP cells enhanced cell migration along with expression of invasion markers matrix metalloproteinase (MMP) 9 and cathepsin B. Consistent with the likelihood that TRPV2 may affect cancer cell aggressiveness by influencing basal intracellular calcium levels, small interfering RNA-mediated silencing of TRPV2 reduced the growth and invasive properties of PC3 prostate tumors established in nude mice xenografts, and diminished expression of invasive enzymes MMP2, MMP9, and cathepsin B. Our findings establish a role for TRPV2 in PCa progression to the aggressive castration-resistant stage, prompting evaluation of TRPV2 as a potential prognostic marker and therapeutic target in the setting of advanced PCa. Cancer Res; 70(3); 1225-35. ©2010 AACR.

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Section: Discussionmentioning

confidence: 99%

Role of Cationic Channel TRPV2 in Promoting Prostate Cancer Migration and Progression to Androgen Resistance

et al. 2010

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“…Among them, TRPV2 still remains poorly characterized, mainly because of the lack of specific pharmacological and molecular tools. TRPV2 is highly expressed in human blood cells, suggesting that, in addition to its role as a noxious heat sensor (Caterina et al, 1999), this channel certainly encompasses other cellular functions (Saunders et al, 2007). Diphenyl borate derivatives have been identified as chemical activators of TRPV1 to -3 channels (Hu et al, 2004); in the case of TRPV3, these compounds have led to a better understanding of channel gating and have also proved to be useful tools to Fig.…”

Section: Discussionmentioning

confidence: 99%

Pharmacological Characterization and Molecular Determinants of the Activation of Transient Receptor Potential V2 Channel Orthologs by 2-Aminoethoxydiphenyl Borate

Juvin

Penna²,

Chemin³

et al. 2007

Mol Pharmacol

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Despite its expression in different cell types, transient receptor potential V2 (TRPV2) is still the most cryptic members of the TRPV channel family. 2-Aminoethoxydiphenyl borate (2APB) has been shown to be a common activator of TRPV1, TRPV2, and TRPV3, but 2APB-triggered TRPV2 activation remains to be thoroughly characterized. In this study, we have developed an assay based on cell lines stably expressing mouse TRPV2 channels and intracellular calcium measurements to perform a pharmacological profiling of the channel. Phenyl borate derivatives were found to activate mouse TRPV2 with similar potencies and thus were used to screen a panel of channel blockers. Besides the classic TRP inhibitors ruthenium red (RR) and 1-(␤-[3-(4-methoxyphenyl) propoxy]-4-methoxyphenethyl)-1H-imidazole hydrochloride (SKF96365), two potassium channel blockers, tetraethylammonium (TEA) and 4-aminopyridine, and an inhibitor of capacitative calcium entry, 1-(2-(trifluoromethyl) phenyl) imidazole (TRIM), were found to inhibit TRPV2 activation by 100 M 2APB. Activation by 300 M 2APB, however, could only be inhibited by RR and TRIM. Electrophysiological recordings demonstrated that TEA inhibition was use-dependent, suggesting that high concentrations of 2APB might induce a progressive conformational change of the channel. Comparison of TRPV2 orthologs revealed that the human channel was insensitive to 2APB. Analysis of chimeric constructs of mouse and human TRPV2 channels showed that the molecular determinants of 2APB sensitivity could be localized to the intracellular amino and carboxyl domains. Finally, using lentiviraldriven expression, we demonstrate that hTRPV2 exerts a dominant-negative effect on 2APB activation of native rodent TRPV2 channels and thus may provide an interesting tool to investigate cellular functions of TRPV2 channels.Transient receptor potential (TRP) proteins are cationic channels that were first discovered in Drosophila melanogaster, in which they play a crucial role in the initial steps of visual transduction (Hardie, 2001;Montell, 2005a). Since then, more than 30 mammalian TRP channels have been identified and are classified into seven families, which are TRPC, TRPV, TRPM, TRPN, TRPA and the two distantly related TRPP and TRPML (Montell, 2005b). All members of the TRP superfamily share the same membrane topology as voltage-gated potassium channels; they contain six hydrophobic domains spanning the plasma membrane and an additional P-loop structure between the fifth and the sixth transmembrane segments that participates in the pore-forming domain of the channel. TRP proteins possess long cytoThis work was supported in part by Centre National de la Recherche Scientifique and Institut National de la Santé et de la Recherche Médicale. J.V. and P.A. were supported by student fellowships from Association de la Recherche sur le Cancer.Article, publication date, and citation information can be found at

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“…However, a number of recent pharmacological, genetic, radioligand binding and immunohistochemical studies suggest widespread distribution and functionality of TRPV1 across the CNS (Cavanaugh et al, 2011;Goswami et al, 2010;Han et al, 2013;O'Sullivan et al,2000;Sanchez et al, 2001). TRPV1 is also found on nonneuronal cells such as keratinocytes (Southall et al, 2003), bladder urothelium (Lazzeri et al, 2004), smooth muscle (Birder et al, 2002), liver (Reilly et al, 2003), polymorphonuclear granulocytes (Heiner et al, 2003), pancreatic β-cells (Akiba et al, 2004), endothelial cells (Golech et al, 2004), lymphocytes (Saunders et al, 2007) and macrophages (Chen et al, 2003). (Cavanaugh et al, 2011;Cristino et al, 2006;Mezey et al, 2000;Roberts et al, 2004) Midbrain and hindbrain regions…”

Section: Localisationmentioning

confidence: 99%

Genotype-dependent responsivity to inflammatory pain: A role for TRPV1 in the periaqueductal grey

Madasu

Okine

Olango

et al. 2016

Pharmacological Research

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Expression of transient receptor potential vanilloid 1 (TRPV1) and 2 (TRPV2) in human peripheral blood

Cited by 91 publications

References 15 publications

Role of Cationic Channel TRPV2 in Promoting Prostate Cancer Migration and Progression to Androgen Resistance

Role of Cationic Channel TRPV2 in Promoting Prostate Cancer Migration and Progression to Androgen Resistance

Pharmacological Characterization and Molecular Determinants of the Activation of Transient Receptor Potential V2 Channel Orthologs by 2-Aminoethoxydiphenyl Borate

Genotype-dependent responsivity to inflammatory pain: A role for TRPV1 in the periaqueductal grey

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