An Ankyrin-like Protein with Transmembrane Domains Is Specifically Lost after Oncogenic Transformation of Human Fibroblasts

Jaquemar, Daniel; Schenker, Thomas; Trüeb, Beat

doi:10.1074/jbc.274.11.7325

Cited by 288 publications

(241 citation statements)

References 29 publications

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“…In Situ Hybridization Analysis-Sense and antisense oligodeoxynucleotides corresponding to the amino acid residues 11 LILCLWSK, 637 QDLNRQRI, and 651 FHTRGSED of the CaT-L sequence (Fig. 1a) were synthesized.…”

Section: Construction Of Expression Plasmids and Transfection Of Hekmentioning

confidence: 99%

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

Wissenbach¹,

Niemeyer²,

Fixemer

et al. 2001

Journal of Biological Chemistry

263

232

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The regulation of intracellular Ca 2؉ plays a key role in the development and growth of cells. Here we report the cloning and functional expression of a highly calciumselective channel localized on the human chromosome 7. The sequence of the new channel is structurally related to the gene product of the CaT1 protein cloned from rat duodenum and is therefore called CaT-like (CaT-L). CaT-L is expressed in locally advanced prostate cancer, metastatic and androgen-insensitive prostatic lesions but is undetectable in healthy prostate tissue and benign prostatic hyperplasia. Additionally, CaT-L is expressed in normal placenta, exocrine pancreas, and salivary glands. New markers with well defined biological function that correlate with aberrant cell growth are needed for the molecular staging of cancer and to predict the clinical outcome. The human CaT-L channel represents a marker for prostate cancer progression and may serve as a target for therapeutic strategies.

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Section: Construction Of Expression Plasmids and Transfection Of Hekmentioning

confidence: 99%

“…One of these genes, p120 (11), when overexpressed, appears to interfere with normal cell growth, whereas the second, melastatin (12), is abundantly expressed in benign cutaneous nevi but appears to be down-regulated in primary melanomas and, especially, in metastatic lesions.…”

mentioning

confidence: 99%

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

Wissenbach¹,

Niemeyer²,

Fixemer

et al. 2001

Journal of Biological Chemistry

263

232

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“…TRPA1 (also known as ANKTM1 and P120) (Jaquemar et al, 1999) is a member of branch A of the transient receptor potential (TRP) family of cation channels. It has been reported that TRPA1 is expressed in a small number (3.6%) of small DRG neurons, and that it forms channels activated by icilin, a chemical that induces a cooling sensation, and by temperatures Յ17°C, and thus is proposed to be the painful cold receptor (Story et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Nociceptor and Hair Cell Transducer Properties of TRPA1, a Channel for Pain and Hearing

Nagata¹,

Duggan²,

Kumar³

et al. 2005

J. Neurosci.

567

515

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Mechanosensory channels of sensory cells mediate the sensations of hearing, touch, and some forms of pain. The TRPA1 (a member of the TRP family of ion channel proteins) channel is activated by pain-producing chemicals, and its inhibition impairs hair cell mechanotransduction. As shown here and previously, TRPA1 is expressed by hair cells as well as by most nociceptors (small neurons of dorsal root, trigeminal, and nodose ganglia) and localizes to their sensory terminals (mechanosensory stereocilia and peripheral free nerves, respectively). Thus, TRPA1 channels are proposed to mediate transduction in both hair cells and nociceptors. Accordingly, we find that heterologously expressed TRPA1 display channel behaviors expected for both auditory and nociceptive transducers. First, TRPA1 and the hair cell transducer share a unique set of pore properties not described for any other channel (block by gadolinium, amiloride, gentamicin, and ruthenium red, a ranging conductance of ϳ100 pS that is reduced to 54% by calcium, permeating calcium-induced potentiation followed by closure, and reopening by depolarization), supporting a direct role of TRPA1 as a pore-forming subunit of the hair cell transducer. Second, TRPA1 channels inactivate in hyperpolarized cells but remain open in depolarized cells. This property provides a mechanism for the lack of desensitization, coincidence detection, and allodynia that characterize pain by allowing a sensory neuron to respond constantly to sustained stimulation that is suprathreshold (i.e., noxious) and yet permitting the same cell to ignore sustained stimulation that is subthreshold (i.e., innocuous). Our results support a TRPA1 role in both nociceptor and hair cell transduction.

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“…12 In their study, the authors described a transformation-sensitive mRNA present in fibroblasts, which encoded a transmembranous TRP-like protein supporting several ankyrin-like domains. 12 It was later established that the mammalian TRPA1 gene is orthologous to the nociception gene painless in Drosophila melanogaster, thus suggesting a conserved role for TRPA1 in sensory functions in humans. 13,14 TRPA1, is composed of six putative transmembrane regions (S1-S6), flanked by cytosolic C-and N-terminal tails with several amino-terminal ankyrin repeats (Fig.…”

Section: Trpa1: Structure Distribution and Regulationmentioning

confidence: 99%

The role of TRPA1 in visceral inflammation and pain

Lapointe

Altier

2011

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An Ankyrin-like Protein with Transmembrane Domains Is Specifically Lost after Oncogenic Transformation of Human Fibroblasts

Cited by 288 publications

References 29 publications

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

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

Nociceptor and Hair Cell Transducer Properties of TRPA1, a Channel for Pain and Hearing

The role of TRPA1 in visceral inflammation and pain

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