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Related Concept Videos

Mechanically-gated Ion Channels01:12

Mechanically-gated Ion Channels

Mechanically-gated ion channels are proteins found in eukaryotic and prokaryotic cell membranes that open in response to mechanical stress. Tension, compression, swelling, and shear stress can alter the conformation of the protein, opening a transmembrane channel that allows the passage of ions for signal transmission. In eukaryotes, mechanically-gated channels are distributed in several regions like the neurons, lungs, skin, bladder, and heart, where they play critical roles in numerous...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory organs,...
Thermosensation01:43

Thermosensation

Peripheral thermosensation is the perception of external temperature. A change in temperature (on the surface of the skin and other tissues) is detected by a family of temperature-sensitive ion channels called Transient Receptor Potential, or TRP, receptors. These receptors are located on free nerve endings. Those detecting cold temperatures are closer to the surface of the skin than the nerve endings detecting warmth. These thermoTRP channels, while temperature selective, have relatively...
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
Repressible Operon: trp Operon01:21

Repressible Operon: trp Operon

The trp operon in Escherichia coli exemplifies a repressible operon. It regulates the synthesis of tryptophan through repressor-mediated transcriptional control and attenuation. This dual regulatory mechanism ensures tryptophan biosynthesis occurs only when needed, conserving cellular resources.Structure of the trp OperonThe trp operon consists of five structural genes (trpE, trpD, trpC, trpB, and trpA) that encode enzymes for tryptophan biosynthesis. These genes are transcribed as a single...

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Related Experiment Video

Updated: Jun 15, 2026

A Simple and Inexpensive Method for Determining Cold Sensitivity and Adaptation in Mice
08:35

A Simple and Inexpensive Method for Determining Cold Sensitivity and Adaptation in Mice

Published on: March 17, 2015

NPPB structure-specifically activates TRPA1 channels.

Kun Liu1, Manoj Samuel, Melisa Ho

  • 1Department of Screening Sciences, Wyeth Research, 500 Arcola Road, Collegeville, PA 19426, USA. liuk2277@yahoo.com

Biochemical Pharmacology
|March 16, 2010
PubMed
Summary
This summary is machine-generated.

Non-reactive compound NPPB activates TRPA1 channels, crucial for mammalian pain sensation. This structure-specific mechanism differs from covalent activators, suggesting novel interactions within the TRPA1 channel.

Related Experiment Videos

Last Updated: Jun 15, 2026

A Simple and Inexpensive Method for Determining Cold Sensitivity and Adaptation in Mice
08:35

A Simple and Inexpensive Method for Determining Cold Sensitivity and Adaptation in Mice

Published on: March 17, 2015

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Pharmacology

Background:

  • Transient Receptor Potential Ankyrin 1 (TRPA1) channels are key players in mammalian pain sensation, particularly in response to inflammatory chemical irritants.
  • While many diverse chemicals activate TRPA1 through covalent modification, the mechanisms of non-reactive compound activation remain largely unexplored.

Purpose of the Study:

  • To investigate the activation of human TRPA1 channels by the non-reactive compound NPPB, a known chloride channel blocker.
  • To elucidate the mechanism of NPPB-induced TRPA1 activation and compare it with known TRPA1 agonists.

Main Methods:

  • Overexpression of human TRPA1 channels in HEK-293 cells.
  • Functional assays including Ca(2+) imaging, whole-cell, and single-channel patch-clamp recordings.
  • Site-directed mutagenesis studies and analysis of NPPB analog activity.

Main Results:

  • NPPB potently activated human TRPA1 channels in a rapid, reversible, and reproducible manner.
  • Mutagenesis data indicated that NPPB activation differs from covalent activators like AITC and menthol, suggesting a distinct binding site and mechanism.
  • NPPB activation was found to be structure-specific, with no single chemical moiety being sufficient for channel activation.

Conclusions:

  • NPPB represents a novel class of TRPA1 channel activators acting through a non-covalent, structure-specific mechanism.
  • The findings suggest a potential interaction between the S5 and N-terminal domains of the TRPA1 channel during NPPB activation.
  • This study expands our understanding of TRPA1 channel gating and opens new avenues for exploring TRPA1-mediated pain pathways.