Neutrophil stimulation with citrullinated histone H4 slows down calcium influx and reduces NET formation compared with native histone H4.

Peptidylarginine deiminase 4 (PAD4) catalyzes posttranslational modification of many target proteins through converting protein arginine or mono-methylarginine to citrulline. Neutrophil extracellular trap (NET) formation is the most dramatic manifestation of PAD4-mediated hypercitrullination reactio...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Lai Shi, Karen Aymonnier, Denisa D Wagner
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/10b48c4213034cfe8a35d083d9e0bafc
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:10b48c4213034cfe8a35d083d9e0bafc
record_format	dspace
spelling	oai:doaj.org-article:10b48c4213034cfe8a35d083d9e0bafc2021-11-25T06:19:10ZNeutrophil stimulation with citrullinated histone H4 slows down calcium influx and reduces NET formation compared with native histone H4.1932-620310.1371/journal.pone.0251726https://doaj.org/article/10b48c4213034cfe8a35d083d9e0bafc2021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0251726https://doaj.org/toc/1932-6203Peptidylarginine deiminase 4 (PAD4) catalyzes posttranslational modification of many target proteins through converting protein arginine or mono-methylarginine to citrulline. Neutrophil extracellular trap (NET) formation is the most dramatic manifestation of PAD4-mediated hypercitrullination reaction in neutrophils, which is characterized by the release of nuclear chromatin to form a chromatin network in the extracellular space. Histones H4, one of the major protein components of chromatin, is released into the extracellular space during sepsis, trauma, and ischemia-reperfusion injury and can also be released during the process of NET formation, along with its citrullinated form. The present study showed that histone H4 can induce NET formation in a calcium and PAD4 dependent manner. Histone H4 caused permeabilization of the neutrophil membrane and sustained rise in intracellular calcium that is necessary for activation of PAD4. In comparison, citrullinated histone H4 induced less calcium influx compared with its native form, leading to reduced NET formation. These studies suggest that citrullinated histone H4 could serve as a brake in the pathology of NETs, slowing down the vicious circle between histone H4 and NETs.Lai ShiKaren AymonnierDenisa D WagnerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 5, p e0251726 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Lai Shi Karen Aymonnier Denisa D Wagner Neutrophil stimulation with citrullinated histone H4 slows down calcium influx and reduces NET formation compared with native histone H4.
description	Peptidylarginine deiminase 4 (PAD4) catalyzes posttranslational modification of many target proteins through converting protein arginine or mono-methylarginine to citrulline. Neutrophil extracellular trap (NET) formation is the most dramatic manifestation of PAD4-mediated hypercitrullination reaction in neutrophils, which is characterized by the release of nuclear chromatin to form a chromatin network in the extracellular space. Histones H4, one of the major protein components of chromatin, is released into the extracellular space during sepsis, trauma, and ischemia-reperfusion injury and can also be released during the process of NET formation, along with its citrullinated form. The present study showed that histone H4 can induce NET formation in a calcium and PAD4 dependent manner. Histone H4 caused permeabilization of the neutrophil membrane and sustained rise in intracellular calcium that is necessary for activation of PAD4. In comparison, citrullinated histone H4 induced less calcium influx compared with its native form, leading to reduced NET formation. These studies suggest that citrullinated histone H4 could serve as a brake in the pathology of NETs, slowing down the vicious circle between histone H4 and NETs.
format	article
author	Lai Shi Karen Aymonnier Denisa D Wagner
author_facet	Lai Shi Karen Aymonnier Denisa D Wagner
author_sort	Lai Shi
title	Neutrophil stimulation with citrullinated histone H4 slows down calcium influx and reduces NET formation compared with native histone H4.
title_short	Neutrophil stimulation with citrullinated histone H4 slows down calcium influx and reduces NET formation compared with native histone H4.
title_full	Neutrophil stimulation with citrullinated histone H4 slows down calcium influx and reduces NET formation compared with native histone H4.
title_fullStr	Neutrophil stimulation with citrullinated histone H4 slows down calcium influx and reduces NET formation compared with native histone H4.
title_full_unstemmed	Neutrophil stimulation with citrullinated histone H4 slows down calcium influx and reduces NET formation compared with native histone H4.
title_sort	neutrophil stimulation with citrullinated histone h4 slows down calcium influx and reduces net formation compared with native histone h4.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/10b48c4213034cfe8a35d083d9e0bafc
work_keys_str_mv	AT laishi neutrophilstimulationwithcitrullinatedhistoneh4slowsdowncalciuminfluxandreducesnetformationcomparedwithnativehistoneh4 AT karenaymonnier neutrophilstimulationwithcitrullinatedhistoneh4slowsdowncalciuminfluxandreducesnetformationcomparedwithnativehistoneh4 AT denisadwagner neutrophilstimulationwithcitrullinatedhistoneh4slowsdowncalciuminfluxandreducesnetformationcomparedwithnativehistoneh4
_version_	1718413905730994176

Neutrophil stimulation with citrullinated histone H4 slows down calcium influx and reduces NET formation compared with native histone H4.

Ejemplares similares