Expression of CaT-like, a Novel Calcium-selective Channel, Correlates with the Malignancy of Prostate Cancer

Wissenbach, Ulrich; Niemeyer, Barbara A.; Fixemer, Thomas; Schneidewind, Arne; Trost, Claudia; Cavalié, Adolfo; Reus, Katrin; Meese, Eckart; Bonkhoff, Helmut; Flockerzi, Veit

doi:10.1074/jbc.m009895200

Cited by 263 publications

(247 citation statements)

References 43 publications

(43 reference statements)

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“…In addition, TRPM8 has originally been cloned from prostate cancer tissue (Tsavaler et al 2001). Moreover, TRPV6 was shown to be strongly upregulated in prostate cancer (Peng et al 2001b;Wissenbach et al 2001Wissenbach et al , 2004. Also in carcinomas of other tissues, such as breast, thyroid, colon and ovary, TRPV6 expression is increased (Zhuang et al 2002).…”

Section: Prostate Cancermentioning

confidence: 99%

“…In human, both channels are coexpressed in organs that mediate transcellular Ca 2+ transport such as duodenum, jejunum, colon, and kidney, but also in pancreas, prostate, mammary, sweat and salivary gland (Hirnet et al 2003;Hoenderop et al 1999Hoenderop et al , 2000aJanssen et al 2002;Muller et al 2000a;Peng et al 1999Peng et al , 2000Peng et al , 2001aWeber et al 2001;Wissenbach et al 2001;Zhuang et al 2002). In general, TRPV5 seems to be the major isoform in kidney, whereas TRPV6 is more ubiquitously expressed with the highest concentrations in the prostate, stomach, brain, lung and small intestine.…”

Section: Molecular Features Of Trpv5 and Trpv6mentioning

confidence: 99%

“…Thus, TRPV6 might be a new marker for tumor progression. Indeed, northern blot analysis, in situ hybridization experiments and immunohistochemistry clearly demonstrated that TRPV6 is highly expressed in prostate cancer cells compared to healthy prostate epithelia (Fixemer et al 2003;Wissenbach et al 2001). …”

Section: Prostate Cancermentioning

confidence: 99%

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The epithelial calcium channels TRPV5 and TRPV6: regulation and implications for disease

Abel

Hoenderop

Bindels

2005

Naunyn-Schmiedeberg's Arch Pharmacol

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The epithelial Ca 2+ channels TRPV5 and TRPV6 represent a new family of Ca 2+ channels that belongs to the superfamily of transient receptor potential channels. TRPV5 and TRPV6 constitute the apical Ca 2+ entry mechanism in active Ca 2+ transport in kidney and intestine. The central role of TRPV5 and TRPV6 in active Ca 2+ (re)absorption makes it a prime target for regulation to maintain Ca 2+ balance. This review covers the hormonal regulation, interaction with accessory proteins and (patho)physiological implications of these epithelial Ca 2+ channels.

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Section: Prostate Cancermentioning

confidence: 99%

Section: Molecular Features Of Trpv5 and Trpv6mentioning

confidence: 99%

See 1 more Smart Citation

The epithelial calcium channels TRPV5 and TRPV6: regulation and implications for disease

Abel

Hoenderop

Bindels

2005

Naunyn-Schmiedeberg's Arch Pharmacol

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“…39 Comparing alignments of orthologs from different species to alignments of homologs -subfamilies, families or superfamilies -can be particularly useful in identifying breaks in sequence similarity. Such an approach was used to determine that the TRPV proteins have six ankyrin repeats, 6,40 although only three or four are recognized by motif search algorithms like Prosite 41 and SMART. 42 Properly folded ankyrin repeats form a very stable scaffold.…”

Section: Experimenting With Ankyrin Repeatsmentioning

confidence: 99%

A primer on ankyrin repeat function in TRP channels and beyond

2008

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Transient Receptor Potential (TRP) channels are rapidly gaining attention as important receptors and transducers of diverse sensory and environmental cues. Recent progress in the field has provided new insights into the structure and function of the ankyrin repeat motifs present in the Nterminal cytosolic domain of many TRP channels. The topics addressed in this review include the structural features of canonical ankyrin repeats, new clues into the functions these repeats perform in cells, and how this information can be applied to develop further experiments on TRP channels and other proteins containing ankyrin repeats.TRP proteins form a large family of ion channels particularly important in animals from worms to man, with more than 30 members in mammals. 1 The founding family member, the Drosophila trp gene -named for the "transient receptor potential" phenotype its mutation causes in light perception by photoreceptors -was first cloned in 1989. 2 The functions assigned to TRP channels in physiology are constantly expanding. They are key transducers of sensory signals, and are generally important in sensing information about the environment in both neuronal and non-neuronal cells (see ref. 3 for comprehensive reviews). Some TRP channels are found in excitable cells of the sensory nervous system, while others are expressed in various other tissues and organs. TRP channels have been implicated in many physiological processes, including calcium and magnesium homeostasis, neuronal growth, temperature sensation and pain perception, to name a few. For example, TRPV1 senses painfully hot temperatures, low extracellular pH and the capsaicin of "hot" chili peppers, while TRPA1 senses many painful chemical stimuli, including the pungent compounds in wasabi and cinnamon. TRPV1 and TRPA1 are expressed in partially overlapping sets of nociceptor neurons that transmit pain signals to the brain.At a molecular level, TRP channels assemble as tetramers through a channel domain that spans the membrane six times and has sequence similarity to voltage-gated ion channels. TRP channels also have large N-and C-terminal cytosolic domains that flank the transmembrane channel domain. These cytosolic domains participate in channel gating and regulation and sense information about the cellular state -ion and metabolite levels, for example. The TRP channel family is divided into seven subfamilies based on sequence similarity 1 : TRPA (ankyrin), TRPC (canonical), TRPM (melastatin), TRPML (mucolipin), TRPP (polycystin), TRPV (vanilloid), and TRPN (NOMPC). Several of these subfamilies -TRPA, TRPC, TRPN and TRPV -have ankyrin repeat sequence motifs in their N-terminal cytosolic domains. Recent work from my lab and others has taken a structural biology approach to elucidate the roles of these ankyrin repeats in TRP channel function. [4][5][6][7][8][9] The emerging structural and functional features of these TRP channel ankyrin repeats are the focus of this short review. NIH Public Access Ankyrin repeats and their structureAnkyrin rep...

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“…Of great importance is the fact that TRPV6 mRNA and protein expression is not only increased in prostate cancer, but also in human carcinomas of the colon, thyroid, ovary, and breast (14,20,27).…”

Section: Introductionmentioning

confidence: 99%

Tamoxifen Inhibits TRPV6 Activity via Estrogen Receptor–Independent Pathways in TRPV6-Expressing MCF-7 Breast Cancer Cells

Bolanz

Kovács

Landowski

et al. 2009

Molecular Cancer Research

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The epithelial calcium channel TRPV6 is upregulated in breast carcinoma compared with normal mammary gland tissue. The selective estrogen receptor modulator tamoxifen is widely used in breast cancer therapy. Previously, we showed that tamoxifen inhibits calcium uptake in TRPV6-transfected Xenopus oocytes. In this study, we examined the effect of tamoxifen on TRPV6 function and intracellular calcium homeostasis in MCF-7 breast cancer cells transiently transfected with EYFP-C1-TRPV6. TRPV6 activity was measured with fluorescence microscopy using Fura-2. The basal calcium level was higher in transfected cells compared with nontransfected cells in calcium-containing solution but not in nominally calcium-free buffer. Basal influxes of calcium and barium were also increased. In transfected cells, 10 μmol/L tamoxifen reduced the basal intracellular calcium concentration to the basal calcium level of nontransfected cells. Tamoxifen decreased the transport rates of calcium and barium in transfected cells by 50%. This inhibitory effect was not blocked by the estrogen receptor antagonist, ICI 182,720. Similarly, a tamoxifen-induced inhibitory effect was also observed in MDA-MB-231 estrogen receptor-negative cells. The effect of tamoxifen was completely blocked by activation of protein kinase C. Inhibiting protein kinase C with calphostin C decreased TRPV6 activity but did not alter the effect of tamoxifen. These findings illustrate how tamoxifen might be effective in estrogen receptor-negative breast carcinomas and suggest that the therapeutic effect of tamoxifen and protein kinase C inhibitors used in breast cancer therapy might involve TRPV6-mediated calcium entry. This study highlights a possible role of TRPV6 as therapeutic target in breast cancer therapy.

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Expression of CaT-like, a Novel Calcium-selective Channel, Correlates with the Malignancy of Prostate Cancer

Cited by 263 publications

References 43 publications

The epithelial calcium channels TRPV5 and TRPV6: regulation and implications for disease

The epithelial calcium channels TRPV5 and TRPV6: regulation and implications for disease

A primer on ankyrin repeat function in TRP channels and beyond

Tamoxifen Inhibits TRPV6 Activity via Estrogen Receptor–Independent Pathways in TRPV6-Expressing MCF-7 Breast Cancer Cells

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