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Mammalian Transient Receptor Potential (TRP) Cation Channels pp 427–459Cite as

TRPM3

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Part of the book series: Handbook of Experimental Pharmacology ((HEP,volume 222))

Abstract

Like most other members of the TRP family, the Trpm3 gene encodes proteins that form cation-permeable ion channels on the plasma membrane. However, TRPM3 proteins have several unique features that set them apart from the other members of this diverse family. The Trpm3 gene encodes for a surprisingly large number of isoforms generated mainly by alternative splicing. Only for two of the (at least) eight sites at which sequence diversity is generated the functional consequences have been elucidated, one leading to nonfunctional channels, the other one profoundly affecting the ionic selectivity. In the Trpm3 gene an intronic microRNA (miR-204) is co-transcribed with Trpm3. By regulating the expression of a multitude of genes, miR-204 increases the functional complexity of the Trpm3 locus. Over the past years, important progress has been made in discovering pharmacological tools to manipulate TRPM3 channel activity. These substances have facilitated the identification of endogenously expressed functional TRPM3 channels in nociceptive neurons, pancreatic beta cells, and vascular smooth muscle cells, among others. TRPM3 channels, which themselves are temperature sensitive, thus have been implicated in sensing noxious heat, in modulating insulin release, and in secretion of inflammatory cytokines. However, in many tissues where TRPM3 proteins are known to be expressed, no functional role has been identified for these channels so far. Because of the availability of adequate pharmacological and genetic tools, it is expected that future investigations on TRPM3 channels will unravel important new aspects and functions of these channels.

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Acknowledgment

We thank C. Goecke and Drs. M. Behrendt and S. Dembla for critically reading the manuscript.

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Authors and Affiliations

  1. Institut für Physiologie und Pathophysiologie, Philipps-Universität Marburg, 35037, Marburg, Germany

    Johannes Oberwinkler

  2. Institut für Experimentelle und Klinische Pharmakologie und Toxikologie der Universität des Saarlandes, 66421, Homburg, Germany

    Stephan E. Philipp

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  1. Johannes Oberwinkler
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Correspondence to Johannes Oberwinkler or Stephan E. Philipp .

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  1. Laboratory Ion Channel Research Campus Gasthuisberg, KU Leuven Department Cell Mol Medicin, Leuven, Belgium

    Bernd Nilius

  2. Institut für Experimentelle u. Klinische, Pharmakologie und Toxikologie, Universität des Saarlandes, Homburg, Saarland, Germany

    Veit Flockerzi

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Oberwinkler, J., Philipp, S.E. (2014). TRPM3. In: Nilius, B., Flockerzi, V. (eds) Mammalian Transient Receptor Potential (TRP) Cation Channels. Handbook of Experimental Pharmacology, vol 222. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-54215-2_17

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