Nejvíce citovaný článek - PubMed ID 35762104
Cellular context determines primary characteristics of human TRPC5 as a cold-activated channel
Our understanding of how the mammalian somatosensory system detects noxious cold is still limited. While the role of TRPM8 in signaling mild non-noxious coolness is reasonably understood, the molecular identity of channels transducing painful cold stimuli remains unresolved. TRPC5 was originally described to contribute to moderate cold responses of dorsal root ganglia neurons in vitro, but mice lacking TRPC5 exhibited no change in behavioral responses to cold temperature. The question of why a channel endowed with the ability to be activated by cooling contributes to the cold response only under certain conditions is currently being intensively studied. It seems increasingly likely that the physiological detection of cold temperatures involves multiple different channels and mechanisms that modulate the threshold and intensity of perception. In this review, we aim to outline how TRPC5 may contribute to these mechanisms and what molecular features are important for its role as a cold sensor.
- Klíčová slova
- Cold sensation, Orai1, Stromal interaction molecule 1, Thermo-TRP channel, Transient receptor potential canonical, Voltage-dependent gating,
- MeSH
- kationtové kanály TRPC * metabolismus MeSH
- kationtové kanály TRPM metabolismus MeSH
- lidé MeSH
- myši MeSH
- nízká teplota * MeSH
- spinální ganglia metabolismus fyziologie MeSH
- vnímání teploty * fyziologie MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- přehledy MeSH
- Názvy látek
- kationtové kanály TRPC * MeSH
- kationtové kanály TRPM MeSH
- TRPC5 protein, human MeSH Prohlížeč
- Trpc5 protein, mouse MeSH Prohlížeč