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TRPV Protein Family—From Mechanosensing to Cancer Invasion

Biophysical cues from the cellular microenvironment are detected by mechanosensitive machineries that translate physical signals into biochemical signaling cascades. At the crossroads of extracellular space and cell interior are located several ion channel families, including TRP family proteins, th...

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Detalles Bibliográficos
Autores principales: Kärki, Tytti, Tojkander, Sari
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8301805/
https://www.ncbi.nlm.nih.gov/pubmed/34356643
http://dx.doi.org/10.3390/biom11071019
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author Kärki, Tytti
Tojkander, Sari
author_facet Kärki, Tytti
Tojkander, Sari
author_sort Kärki, Tytti
collection PubMed
description Biophysical cues from the cellular microenvironment are detected by mechanosensitive machineries that translate physical signals into biochemical signaling cascades. At the crossroads of extracellular space and cell interior are located several ion channel families, including TRP family proteins, that are triggered by mechanical stimuli and drive intracellular signaling pathways through spatio-temporally controlled Ca(2+)-influx. Mechanosensitive Ca(2+)-channels, therefore, act as critical components in the rapid transmission of physical signals into biologically compatible information to impact crucial processes during development, morphogenesis and regeneration. Given the mechanosensitive nature of many of the TRP family channels, they must also respond to the biophysical changes along the development of several pathophysiological conditions and have also been linked to cancer progression. In this review, we will focus on the TRPV, vanilloid family of TRP proteins, and their connection to cancer progression through their mechanosensitive nature.
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spelling pubmed-83018052021-07-24 TRPV Protein Family—From Mechanosensing to Cancer Invasion Kärki, Tytti Tojkander, Sari Biomolecules Review Biophysical cues from the cellular microenvironment are detected by mechanosensitive machineries that translate physical signals into biochemical signaling cascades. At the crossroads of extracellular space and cell interior are located several ion channel families, including TRP family proteins, that are triggered by mechanical stimuli and drive intracellular signaling pathways through spatio-temporally controlled Ca(2+)-influx. Mechanosensitive Ca(2+)-channels, therefore, act as critical components in the rapid transmission of physical signals into biologically compatible information to impact crucial processes during development, morphogenesis and regeneration. Given the mechanosensitive nature of many of the TRP family channels, they must also respond to the biophysical changes along the development of several pathophysiological conditions and have also been linked to cancer progression. In this review, we will focus on the TRPV, vanilloid family of TRP proteins, and their connection to cancer progression through their mechanosensitive nature. MDPI 2021-07-13 /pmc/articles/PMC8301805/ /pubmed/34356643 http://dx.doi.org/10.3390/biom11071019 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Kärki, Tytti
Tojkander, Sari
TRPV Protein Family—From Mechanosensing to Cancer Invasion
title TRPV Protein Family—From Mechanosensing to Cancer Invasion
title_full TRPV Protein Family—From Mechanosensing to Cancer Invasion
title_fullStr TRPV Protein Family—From Mechanosensing to Cancer Invasion
title_full_unstemmed TRPV Protein Family—From Mechanosensing to Cancer Invasion
title_short TRPV Protein Family—From Mechanosensing to Cancer Invasion
title_sort trpv protein family—from mechanosensing to cancer invasion
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8301805/
https://www.ncbi.nlm.nih.gov/pubmed/34356643
http://dx.doi.org/10.3390/biom11071019
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