Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing

Abstract Cathelicidins play pivotal roles in host defense. The discovery of novel cathelicidins is important research; however, despite the identification of many cathelicidins in vertebrates, few have been reported in amphibians. Here we identified a novel cathelicidin (named cathelicidin-OA1) from...

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Autores principales:	Xiaoqing Cao, Ying Wang, Chunyun Wu, Xiaojie Li, Zhe Fu, Meifeng Yang, Wenxin Bian, Siyuan Wang, Yongli Song, Jing Tang, Xinwang Yang
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	HaCaT Cell Proliferation Wound Healing Activity Cathelicidin HaCaT Cells Exhibit Antioxidant Activity Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6c7f8aa51ee04668b83b00530bdfea8b
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spelling	oai:doaj.org-article:6c7f8aa51ee04668b83b00530bdfea8b2021-12-02T15:09:08ZCathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing10.1038/s41598-018-19486-92045-2322https://doaj.org/article/6c7f8aa51ee04668b83b00530bdfea8b2018-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-19486-9https://doaj.org/toc/2045-2322Abstract Cathelicidins play pivotal roles in host defense. The discovery of novel cathelicidins is important research; however, despite the identification of many cathelicidins in vertebrates, few have been reported in amphibians. Here we identified a novel cathelicidin (named cathelicidin-OA1) from the skin of an amphibian species, Odorrana andersonii. Produced by posttranslational processing of a 198-residue prepropeptide, cathelicidin-OA1 presented an amino acid sequence of ‘IGRDPTWSHLAASCLKCIFDDLPKTHN′ and a molecular mass of 3038.5 Da. Functional analysis showed that, unlike other cathelicidins, cathelicidin-OA1 demonstrated no direct microbe-killing, acute toxicity and hemolytic activity, but did exhibit antioxidant activity. Importantly, cathelicidin-OA1 accelerated wound healing against human keratinocytes (HaCaT) and skin fibroblasts (HSF) in both time- and dose-dependent manners. Notably, cathelicidin-OA1 also showed wound-healing promotion in a mouse model with full-thickness skin wounds, accelerating re-epithelialization and granulation tissue formation by enhancing the recruitment of macrophages to the wound site, inducing HaCaT cell proliferation and HSF cell migration. This is the first cathelicidin identified from an amphibian that shows potent wound-healing activity. These results will help in the development of new types of wound-healing agents and in our understanding of the biological functions of cathelicidins.Xiaoqing CaoYing WangChunyun WuXiaojie LiZhe FuMeifeng YangWenxin BianSiyuan WangYongli SongJing TangXinwang YangNature PortfolioarticleHaCaT Cell ProliferationWound Healing ActivityCathelicidinHaCaT CellsExhibit Antioxidant ActivityMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-15 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	HaCaT Cell Proliferation Wound Healing Activity Cathelicidin HaCaT Cells Exhibit Antioxidant Activity Medicine R Science Q
spellingShingle	HaCaT Cell Proliferation Wound Healing Activity Cathelicidin HaCaT Cells Exhibit Antioxidant Activity Medicine R Science Q Xiaoqing Cao Ying Wang Chunyun Wu Xiaojie Li Zhe Fu Meifeng Yang Wenxin Bian Siyuan Wang Yongli Song Jing Tang Xinwang Yang Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing
description	Abstract Cathelicidins play pivotal roles in host defense. The discovery of novel cathelicidins is important research; however, despite the identification of many cathelicidins in vertebrates, few have been reported in amphibians. Here we identified a novel cathelicidin (named cathelicidin-OA1) from the skin of an amphibian species, Odorrana andersonii. Produced by posttranslational processing of a 198-residue prepropeptide, cathelicidin-OA1 presented an amino acid sequence of ‘IGRDPTWSHLAASCLKCIFDDLPKTHN′ and a molecular mass of 3038.5 Da. Functional analysis showed that, unlike other cathelicidins, cathelicidin-OA1 demonstrated no direct microbe-killing, acute toxicity and hemolytic activity, but did exhibit antioxidant activity. Importantly, cathelicidin-OA1 accelerated wound healing against human keratinocytes (HaCaT) and skin fibroblasts (HSF) in both time- and dose-dependent manners. Notably, cathelicidin-OA1 also showed wound-healing promotion in a mouse model with full-thickness skin wounds, accelerating re-epithelialization and granulation tissue formation by enhancing the recruitment of macrophages to the wound site, inducing HaCaT cell proliferation and HSF cell migration. This is the first cathelicidin identified from an amphibian that shows potent wound-healing activity. These results will help in the development of new types of wound-healing agents and in our understanding of the biological functions of cathelicidins.
format	article
author	Xiaoqing Cao Ying Wang Chunyun Wu Xiaojie Li Zhe Fu Meifeng Yang Wenxin Bian Siyuan Wang Yongli Song Jing Tang Xinwang Yang
author_facet	Xiaoqing Cao Ying Wang Chunyun Wu Xiaojie Li Zhe Fu Meifeng Yang Wenxin Bian Siyuan Wang Yongli Song Jing Tang Xinwang Yang
author_sort	Xiaoqing Cao
title	Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing
title_short	Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing
title_full	Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing
title_fullStr	Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing
title_full_unstemmed	Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing
title_sort	cathelicidin-oa1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/6c7f8aa51ee04668b83b00530bdfea8b
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Cathelicidin-OA1, a novel antioxidant peptide identified from an amphibian, accelerates skin wound healing

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