Smooth Muscle-Depressant Activity of AP-18, a Putative TRPA1 Antagonist in the Guinea Pig Intestine

Barthó, L.; Sándor, Zsolt; Kelemen, Dezső; Pierpoint, Robert; Benkó, Rita

doi:10.1159/000366023

Cited by 5 publications

(1 citation statement)

References 11 publications

(18 reference statements)

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“…Transcripts and functional expression of TRPA1 have been found in NG and DRG neurons innervating mouse and rat stomach and colon (128,417,822), mouse jejunum and ileum (128,144,162,501,654), and guinea pig esophagus (482,931,932). TRPA1 has been also detected in intestinal tissue samples of mouse, guinea pig, and dog (71,214,654), as well as in rat and human colonic epithelial cells (362,363) and enterochromaffin cells (EC), mouse duodenal and colonic enterocytes (255), and mouse and human mucosa (81,214,604,675). Moreover, TRPA1 is expressed in mouse enteroendocrine cells (EEC), commonly in the duodenum and jejunum, and in human enteric glial cells cultures, where TRPA1 transcripts are upregulated by E. coli LPS incubation (159,476).…”

Section: E Trpa1 In Gastrointestinal Tract Diseasesmentioning

confidence: 99%

Mammalian Transient Receptor Potential TRPA1 Channels: From Structure to Disease

Talavera

Startek

Alvarez‐Collazo

et al. 2020

Physiological Reviews

274

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The transient receptor potential ankyrin (TRPA) channels are Ca2+-permeable nonselective cation channels remarkably conserved through the animal kingdom. Mammals have only one member, TRPA1, which is widely expressed in sensory neurons and in non-neuronal cells (such as epithelial cells and hair cells). TRPA1 owes its name to the presence of 14 ankyrin repeats located in the NH2 terminus of the channel, an unusual structural feature that may be relevant to its interactions with intracellular components. TRPA1 is primarily involved in the detection of an extremely wide variety of exogenous stimuli that may produce cellular damage. This includes a plethora of electrophilic compounds that interact with nucleophilic amino acid residues in the channel and many other chemically unrelated compounds whose only common feature seems to be their ability to partition in the plasma membrane. TRPA1 has been reported to be activated by cold, heat, and mechanical stimuli, and its function is modulated by multiple factors, including Ca2+, trace metals, pH, and reactive oxygen, nitrogen, and carbonyl species. TRPA1 is involved in acute and chronic pain as well as inflammation, plays key roles in the pathophysiology of nearly all organ systems, and is an attractive target for the treatment of related diseases. Here we review the current knowledge about the mammalian TRPA1 channel, linking its unique structure, widely tuned sensory properties, and complex regulation to its roles in multiple pathophysiological conditions.

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