trp, a Novel Mammalian Gene Family Essential for Agonist-Activated Capacitative Ca2+ Entry

Zhu, Xi; Jiang, Meisheng; Peyton, Michael; Boulay, Guylain; Hurst, Raymond S; Stefani, Enrico; Birnbaumer, Lutz

doi:10.1016/s0092-8674(00)81233-7

Cited by 638 publications

(579 citation statements)

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“…(i) The Drosophila melanogaster trp gene product has a similar sequence to the cq subunit of the L-type Ca 2+ channel, but lacks charged residues in the $4 segment [10], the part of the cxl subunit that is thought to sense a change in voltage [17]. Transfection of mammalian trp gene homologues in a mammalian cell line (COS-M6) enhanced store-operated Ca 2+ entry beyond that found in nontransfected cells, while transfection of mouse fibroblast L-cells with antisense cDNA fragments of murine trp homologues resulted in the abolition of store-operated Ca 2+ influx [18]. This indicates that mammalian trp gene homologues encode proteins that can participate in store-operated Ca 2+ entry in non-excitable mammalian cells.…”

Section: Discussionmentioning

confidence: 99%

Functional importance of the dihydropyridine‐sensitive, yet voltage‐insensitive store‐operated Ca²⁺ influx of U937 cells

1996

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The Ca 2+ current activated by Ca 2+ store depletion in non-excitable cells is classically regarded as being dihydropyridine-insensitive, suggesting that store-operated Ca 2+ channels (SOCs) are dissimilar to voltage-gated Ca 2+ channels (VGCs) of excitable-cells. Here, we demonstrate dihydropyridine-sensitivity for the store-operated Ca 2+ influx induced by ATP and thapsigargin (Tg) in the non-excitable U937 cell-line. Ca 2+ store depletion by prior treatment of cells with either Tg or ATP, stimulated a 2+ Ca entry mechanism that was inhibited by nicardipine, nifedipine, and the specific L-type Ca 2+ channel blocker, calciseptine. A functional requirement for this Ca 2+ influx mechanism in agonist-induced mitogenesis seemed likely, since nicardipine, a particularly potent inhibitor of storeoperated Ca 2+ influx in these cells, suppressed ATP-and Tgstimulated cell proliferation. Depolarisation of cells with KCI, or gramicidin failed to elicit an increase in cytosolic Ca 2÷, suggesting that while the store-operated Ca 2+ influx channel of U937 cells shares pharmacologic properties with the L-type Ca 2+ channel, it is voltage-insensitive and therefore may resemble an L-type Ca 2+ channel lacking a voltage sensor.

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Section: Discussionmentioning

confidence: 99%

Functional importance of the dihydropyridine‐sensitive, yet voltage‐insensitive store‐operated Ca²⁺ influx of U937 cells

1996

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“…Specificity of the antibody was confirmed using in vitro translation products prepared with cDNAs for mTRPC2 clone 14 (24), mTRPC2 clone 17 (24), and mTRPC6 (28), cloned into pcDNA3. The in vitro products were prepared with the TNT quick coupled transcription/translation system (Promega, Madison, WI).…”

Section: Methodsmentioning

confidence: 99%

Erythropoietin Modulates Calcium Influx through TRPC2

Chu¹,

Cheung

Barber

et al. 2002

Journal of Biological Chemistry

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“…A vast number of papers have reported that many TRPC channels function as SOC. Zhu et al (7) first reported that expression of human TRPC3 in cultured human embryonic kidney (HEK) cells gives rise to agonist-and thapsigargin-activated channel activity. Because thapsigargin depletes intracellular Ca 2ϩ stores by inhibiting the endoplasmic reticulum Ca 2ϩ -ATPase, the authors concluded that TRPC3 proteins constitute subunits of SOC.…”

Section: Role Of Trp In Plc-dependent Ca 2ϩ Influxmentioning

confidence: 99%

The Transient Receptor Potential Superfamily of Ion Channels

Huang

2004

Journal of the American Society of Nephrology

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Abstract. The transient receptor potential (TRP) superfamily of proteins is cation-selective ion channels with six predicted transmembrane segments and intracellularly localized amino and carboxyl termini. Members of the TRP superfamily are identified on the basis of amino acid sequence and structural similarity and are classified into TRPC, TRPV, TRPM, TRPP, TRPN, and TRPML subfamilies. TRP channels are widespread and have diverse functions, ranging from thermal, tactile, taste, osmolar, and fluid flow sensing to transepithelial Ca 2ϩ and Mg 2ϩ transport. Mutations of TRP proteins produce many renal diseases, including Mg 2ϩ wasting, hypocalcemia, and polycystic kidney diseases. This review focuses on recent advances in the understanding of their functions.The first transient receptor potential (TRP) protein was discovered in studies that examined Drosophila phototransduction (1). The photoreceptor cells of Drosophila exhibit sustained receptor potentials in response to continuous light exposure. The ionic basis for the sustained receptor potentials is influx of Ca 2ϩ from the extracellular space. Cosens and Manning (1) reported in 1969 that one group of mutant flies exhibits TRP upon continuous light exposure and named it trp, for transient receptor potential. The trp gene was cloned in 1989 (2) and subsequently shown to encode a Ca 2ϩ -permeable cation channel (3). Since then, many channels that bear sequence and structural similarities to the Drosophila TRP have been cloned from flies, worms, and mammals. Together, they form the TRP superfamily.Ion channels (e.g., voltage-gated K ϩ channels) are typically identified by their modes of activation and/or ion selectivity. Each family or superfamily of ion channels of similar activation and selectivity consists of multiple members of channel proteins with amino acid sequence homology. Unlike most ion channel families, the TRP superfamily of ion channels are identified on the basis of homology only. The mode of activation and selectivity for TRP channels are disparate. Some TRP channels are activated by ligands, whereas others are regulated by physical stimuli (e.g., heat) or yet-unknown mechanisms. All TRP channels are cation selective, but the selectivity ratio for Ca 2ϩ versus the monovalent cation Na ϩ (P Ca /P Na ) varies widely, ranging from Ͼ100:1, to 1 to 10:1, to Ͻ0.05:1. The lack of common identifying features has in part contributed to the confusing nomenclature of TRP channels in the literature.A recent consensus report proposed a unified nomenclature for the TRP superfamily (4). It classified TRP channels into TRPC, TRPV, and TRPM subfamilies. More recent classification has expanded TRP superfamily to include three additional, more distantly related subfamilies, TRPP, TRPML, and TRPN ( Figure 1). Structurally, all of these TRP channels have six predicted transmembrane (TM) segments and N-terminal and C-terminal cytoplasmic tails similar to topologies of voltagegated K ϩ , Na ϩ , and Ca 2ϩ channels; cyclic nucleotide-gated channels; and hyperpolarizati...

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trp, a Novel Mammalian Gene Family Essential for Agonist-Activated Capacitative Ca2+ Entry

Cited by 638 publications

References 60 publications

Functional importance of the dihydropyridine‐sensitive, yet voltage‐insensitive store‐operated Ca²⁺ influx of U937 cells

Functional importance of the dihydropyridine‐sensitive, yet voltage‐insensitive store‐operated Ca²⁺ influx of U937 cells

Erythropoietin Modulates Calcium Influx through TRPC2

The Transient Receptor Potential Superfamily of Ion Channels

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trp, a Novel Mammalian Gene Family Essential for Agonist-Activated Capacitative Ca2+ Entry

Cited by 638 publications

References 60 publications

Functional importance of the dihydropyridine‐sensitive, yet voltage‐insensitive store‐operated Ca2+ influx of U937 cells

Functional importance of the dihydropyridine‐sensitive, yet voltage‐insensitive store‐operated Ca2+ influx of U937 cells

Erythropoietin Modulates Calcium Influx through TRPC2

The Transient Receptor Potential Superfamily of Ion Channels

Contact Info

Product

Resources

About

Functional importance of the dihydropyridine‐sensitive, yet voltage‐insensitive store‐operated Ca²⁺ influx of U937 cells

Functional importance of the dihydropyridine‐sensitive, yet voltage‐insensitive store‐operated Ca²⁺ influx of U937 cells