Allicin disrupts cardiac Cav1.2 channels via trafficking

Context: Allicin is a potential antiarrhythmic agent. The antiarrhythmic properties of allicin rely on its blockade of various cardiac ion channels. The l-type calcium (Cav1.2) channel provides a pivotal substrate for cardiac electrophysiologic activities. The mechanism of allicin on Cav1.2 remains...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Dan Han, Lingping Xu, Peng Liu, Yingying Liu, Chaofeng Sun, Yanrong Yin
Formato:	article
Lenguaje:	EN
Publicado:	Taylor & Francis Group 2019
Materias:	antiarrhythmia trafficking dysfunction Therapeutics. Pharmacology RM1-950
Acceso en línea:	https://doaj.org/article/f3bad6817d204abb9efb23e6c54424af
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:f3bad6817d204abb9efb23e6c54424af
record_format	dspace
spelling	oai:doaj.org-article:f3bad6817d204abb9efb23e6c54424af2021-11-17T14:21:56ZAllicin disrupts cardiac Cav1.2 channels via trafficking1388-02091744-511610.1080/13880209.2019.1577469https://doaj.org/article/f3bad6817d204abb9efb23e6c54424af2019-01-01T00:00:00Zhttp://dx.doi.org/10.1080/13880209.2019.1577469https://doaj.org/toc/1388-0209https://doaj.org/toc/1744-5116Context: Allicin is a potential antiarrhythmic agent. The antiarrhythmic properties of allicin rely on its blockade of various cardiac ion channels. The l-type calcium (Cav1.2) channel provides a pivotal substrate for cardiac electrophysiologic activities. The mechanism of allicin on Cav1.2 remains unclear. Objective: This study evaluated the potential of allicin on the synthesis and trafficking of Cav1.2 channels. Materials and methods: Primary cardiomyocytes (CMs) from neonatal Sprague-Dawley (SD) rats were exposed to allicin (0, 0.0001, 0.001, 0.01, 0.1, 1, 10, 100 μg/mL) for 24 and 48 h. The CellTiter-Glo assay was performed to measure CM viability. Western blot with grayscale analysis and confocal laser scanning microscopy were used to evaluate the effects of allicin on the synthesis and trafficking of Cav1.2 channel proteins in primary CMs. Results: There was no significant difference in apoptotic toxicity from the actual cell viability (p > 0.05) in any group (0, 0.0001, 0.001, 0.01, 0.1, 1, 10, 100 μg/mL allicin), except that viability in the 0.001 and 0.01 μg/mL groups at 24 h were significantly greater (137.37 and 135.96%) (p < 0.05). Western blot with grayscale analysis revealed no substantial inhibition by allicin of the synthesis of Cav1.2 proteins. Confocal laser scanning microscopy revealed trafficking dysfunction of Cav1.2 channels caused by allicin in primary CMs. Conclusion: This study is the first to demonstrate that allicin inhibits cardiac Cav1.2 channels by disrupting trafficking, possibly mediating its antiarrhythmic benefits. Therefore, allicin might serve as a new antiarrhythmic agent in the future.Dan HanLingping XuPeng LiuYingying LiuChaofeng SunYanrong YinTaylor & Francis Grouparticleantiarrhythmiatrafficking dysfunctionTherapeutics. PharmacologyRM1-950ENPharmaceutical Biology, Vol 57, Iss 1, Pp 245-249 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	antiarrhythmia trafficking dysfunction Therapeutics. Pharmacology RM1-950
spellingShingle	antiarrhythmia trafficking dysfunction Therapeutics. Pharmacology RM1-950 Dan Han Lingping Xu Peng Liu Yingying Liu Chaofeng Sun Yanrong Yin Allicin disrupts cardiac Cav1.2 channels via trafficking
description	Context: Allicin is a potential antiarrhythmic agent. The antiarrhythmic properties of allicin rely on its blockade of various cardiac ion channels. The l-type calcium (Cav1.2) channel provides a pivotal substrate for cardiac electrophysiologic activities. The mechanism of allicin on Cav1.2 remains unclear. Objective: This study evaluated the potential of allicin on the synthesis and trafficking of Cav1.2 channels. Materials and methods: Primary cardiomyocytes (CMs) from neonatal Sprague-Dawley (SD) rats were exposed to allicin (0, 0.0001, 0.001, 0.01, 0.1, 1, 10, 100 μg/mL) for 24 and 48 h. The CellTiter-Glo assay was performed to measure CM viability. Western blot with grayscale analysis and confocal laser scanning microscopy were used to evaluate the effects of allicin on the synthesis and trafficking of Cav1.2 channel proteins in primary CMs. Results: There was no significant difference in apoptotic toxicity from the actual cell viability (p > 0.05) in any group (0, 0.0001, 0.001, 0.01, 0.1, 1, 10, 100 μg/mL allicin), except that viability in the 0.001 and 0.01 μg/mL groups at 24 h were significantly greater (137.37 and 135.96%) (p < 0.05). Western blot with grayscale analysis revealed no substantial inhibition by allicin of the synthesis of Cav1.2 proteins. Confocal laser scanning microscopy revealed trafficking dysfunction of Cav1.2 channels caused by allicin in primary CMs. Conclusion: This study is the first to demonstrate that allicin inhibits cardiac Cav1.2 channels by disrupting trafficking, possibly mediating its antiarrhythmic benefits. Therefore, allicin might serve as a new antiarrhythmic agent in the future.
format	article
author	Dan Han Lingping Xu Peng Liu Yingying Liu Chaofeng Sun Yanrong Yin
author_facet	Dan Han Lingping Xu Peng Liu Yingying Liu Chaofeng Sun Yanrong Yin
author_sort	Dan Han
title	Allicin disrupts cardiac Cav1.2 channels via trafficking
title_short	Allicin disrupts cardiac Cav1.2 channels via trafficking
title_full	Allicin disrupts cardiac Cav1.2 channels via trafficking
title_fullStr	Allicin disrupts cardiac Cav1.2 channels via trafficking
title_full_unstemmed	Allicin disrupts cardiac Cav1.2 channels via trafficking
title_sort	allicin disrupts cardiac cav1.2 channels via trafficking
publisher	Taylor & Francis Group
publishDate	2019
url	https://doaj.org/article/f3bad6817d204abb9efb23e6c54424af
work_keys_str_mv	AT danhan allicindisruptscardiaccav12channelsviatrafficking AT lingpingxu allicindisruptscardiaccav12channelsviatrafficking AT pengliu allicindisruptscardiaccav12channelsviatrafficking AT yingyingliu allicindisruptscardiaccav12channelsviatrafficking AT chaofengsun allicindisruptscardiaccav12channelsviatrafficking AT yanrongyin allicindisruptscardiaccav12channelsviatrafficking
_version_	1718425520877600768

Allicin disrupts cardiac Cav1.2 channels via trafficking

Ejemplares similares