Identification and quantification of plasma free salusin-β, an endogenous parasympathomimetic peptide

Abstract Salusin-β is an endogenous parasympathomimetic proatherosclerotic peptide. Salusin-β was initially predicted from bioinformatic analyses and later immunologically detected in human biofluids. However, elucidation of salusin-β bioactivity has faced enormous challenges because of its unique p...

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Autores principales:	Kazumi Fujimoto, Akinori Hayashi, Yoshio Kodera, Tatsuya Saito, Takuya Toki, Akifumi Ogawa, Yuji Kamata, Koji Takano, Hideki Katakami, Masayoshi Shichiri
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/12e669158622491cb39e2ea5cf573602
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spelling	oai:doaj.org-article:12e669158622491cb39e2ea5cf5736022021-12-02T12:30:10ZIdentification and quantification of plasma free salusin-β, an endogenous parasympathomimetic peptide10.1038/s41598-017-08288-02045-2322https://doaj.org/article/12e669158622491cb39e2ea5cf5736022017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-08288-0https://doaj.org/toc/2045-2322Abstract Salusin-β is an endogenous parasympathomimetic proatherosclerotic peptide. Salusin-β was initially predicted from bioinformatic analyses and later immunologically detected in human biofluids. However, elucidation of salusin-β bioactivity has faced enormous challenges because of its unique physicochemical characteristics that cause it to strongly adhere to laboratory apparatus materials. In the strictest sense, the discovery of bioactive peptides is not complete until their exact native sequences have been confirmed in the peripheral circulation. In this study, we determined the plasma molecular form and levels of free salusin-β to determine its pathophysiological significance. Ultra-high-yield enrichment and preseparation of non-tryptic human plasma was followed by LC-MS/MS, and full-length salusin-β and seven different endogenous fragment sequences were identified. We established a new ELISA that specifically detects plasma free salusin-β without cross-reacting with any of its identified endogenous fragments. Free salusin-β levels exhibited a profound early morning nadir and rapidly decreased in response to parasympathetic nervous augmentation. Our technical advance in plasma native peptide analysis successfully identified a hard-to-detect bioactive peptide, salusin-β, together with its formerly unrecognized fragments, and further suggests that conventional immunological measurements of target peptides may not be fully representative.Kazumi FujimotoAkinori HayashiYoshio KoderaTatsuya SaitoTakuya TokiAkifumi OgawaYuji KamataKoji TakanoHideki KatakamiMasayoshi ShichiriNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Kazumi Fujimoto Akinori Hayashi Yoshio Kodera Tatsuya Saito Takuya Toki Akifumi Ogawa Yuji Kamata Koji Takano Hideki Katakami Masayoshi Shichiri Identification and quantification of plasma free salusin-β, an endogenous parasympathomimetic peptide
description	Abstract Salusin-β is an endogenous parasympathomimetic proatherosclerotic peptide. Salusin-β was initially predicted from bioinformatic analyses and later immunologically detected in human biofluids. However, elucidation of salusin-β bioactivity has faced enormous challenges because of its unique physicochemical characteristics that cause it to strongly adhere to laboratory apparatus materials. In the strictest sense, the discovery of bioactive peptides is not complete until their exact native sequences have been confirmed in the peripheral circulation. In this study, we determined the plasma molecular form and levels of free salusin-β to determine its pathophysiological significance. Ultra-high-yield enrichment and preseparation of non-tryptic human plasma was followed by LC-MS/MS, and full-length salusin-β and seven different endogenous fragment sequences were identified. We established a new ELISA that specifically detects plasma free salusin-β without cross-reacting with any of its identified endogenous fragments. Free salusin-β levels exhibited a profound early morning nadir and rapidly decreased in response to parasympathetic nervous augmentation. Our technical advance in plasma native peptide analysis successfully identified a hard-to-detect bioactive peptide, salusin-β, together with its formerly unrecognized fragments, and further suggests that conventional immunological measurements of target peptides may not be fully representative.
format	article
author	Kazumi Fujimoto Akinori Hayashi Yoshio Kodera Tatsuya Saito Takuya Toki Akifumi Ogawa Yuji Kamata Koji Takano Hideki Katakami Masayoshi Shichiri
author_facet	Kazumi Fujimoto Akinori Hayashi Yoshio Kodera Tatsuya Saito Takuya Toki Akifumi Ogawa Yuji Kamata Koji Takano Hideki Katakami Masayoshi Shichiri
author_sort	Kazumi Fujimoto
title	Identification and quantification of plasma free salusin-β, an endogenous parasympathomimetic peptide
title_short	Identification and quantification of plasma free salusin-β, an endogenous parasympathomimetic peptide
title_full	Identification and quantification of plasma free salusin-β, an endogenous parasympathomimetic peptide
title_fullStr	Identification and quantification of plasma free salusin-β, an endogenous parasympathomimetic peptide
title_full_unstemmed	Identification and quantification of plasma free salusin-β, an endogenous parasympathomimetic peptide
title_sort	identification and quantification of plasma free salusin-β, an endogenous parasympathomimetic peptide
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/12e669158622491cb39e2ea5cf573602
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Identification and quantification of plasma free salusin-β, an endogenous parasympathomimetic peptide

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