https://www.cell.com/cell/pdf/S0092-8674(09)01243-4.pdf

Cellular and Molecular Mechanisms of Pain

TRP channels are the vanguard of our sensory systems, responding to temperature, touch, pain, osmolarity, pheromones, taste and other stimuli. But their role is much broader than classical sensory transduction. They are an ancient sensory apparatus for the cell, not just the multicellular organism, and they have been adapted to respond to all manner of stimuli, from both within and outside the cell.

TRP channels as cellular sensors

ANKTM1, a TRP-like Channel Expressed in Nociceptive Neurons, Is Activated by Cold Temperatures

In electrically nonexcitable cells, Ca2+ influx is essential for regulating a host of kinetically distinct processes involving exocytosis, enzyme control, gene regulation, cell growth and prolifera...

Store-operated calcium channels.

http://www.procrastin.fr/blog/images/chimie/menthol.pdf

A TRP Channel that Senses Cold Stimuli and Menthol

Ca2+-permeable channels that are involved in the responses of mammalian cells to changes in extracellular osmolarity have not been characterized at the molecular level. Here we identify a new TRP (transient receptor potential)-like channel protein, OTRPC4, that is expressed at high levels in the kidney, liver and heart. OTRPC4 forms Ca2+-permeable, nonselective cation channels that exhibit spontaneous activity in isotonic media and are rapidly activated by decreases in, and are inhibited by increases in, extracellular osmolarity. Changes in osmolarity of as little as 10% result in significant changes in intracellular Ca2+ concentration. We propose that OTRPC4 is a candidate for a molecular sensor that confers osmosensitivity on mammalian cells.

OTRPC4, a nonselective cation channel that confers sensitivity to extracellular osmolarity.

Lanthanides Potentiate TRPC5 Currents by an Action at Extracellular Sites Close to the Pore Mouth

To investigate the possible role of members of the mammalian transient receptor potential (TRP) channel family (TRPC1–7) in vasoconstrictor-induced Ca2+ entry in vascular smooth muscle cells, we st...

https://www.physiology.org/doi/pdf/10.1152/ajpcell.00283.2001

TRPC6 is a candidate channel involved in receptor-stimulated cation currents in A7r5 smooth muscle cells.

http://www.jbc.org/content/early/2003/04/30/jbc.M302590200.full.pdf

Ca2+-dependent potentiation of the nonselective cation channel TRPV4 is mediated by a C-terminal calmodulin binding site.

Genome-wide scans for positive selection in humans provide a promising approach to establish links between genetic variants and adaptive phenotypes From this approach, lists of hundreds of candidate genomic regions for positive selection have been assembled These candidate regions are expected to contain variants that contribute to adaptive phenotypes, but few of these regions have been associated with phenotypic effects Here we present evidence that a derived nonsynonymous substitution (370A) in EDAR, a gene involved in ectodermal development, was driven to high frequency in East Asia by positive selection prior to 10,000 years ago With an in vitro transfection assay, we demonstrate that 370A enhances NF-κB activity Our results suggest that 370A is a positively selected functional genetic variant that underlies an adaptive human phenotype

/pdf/positive-selection-in-east-asians-for-an-edar-allele-that-31vhrxgcmb.pdf

Rainer Strotmann

Papers

OTRPC4, a nonselective cation channel that confers sensitivity to extracellular osmolarity.

Lanthanides Potentiate TRPC5 Currents by an Action at Extracellular Sites Close to the Pore Mouth

TRPC6 is a candidate channel involved in receptor-stimulated cation currents in A7r5 smooth muscle cells.

Ca2+-dependent potentiation of the nonselective cation channel TRPV4 is mediated by a C-terminal calmodulin binding site.

Positive Selection in East Asians for an EDAR Allele that Enhances NF-κB Activation