Multicolor imaging of calcium-binding proteins in human kidney stones for elucidating the effects of proteins on crystal growth

Abstract The pathogenesis of kidney stone formation includes multi-step processes involving complex interactions between mineral components and protein matrix. Calcium-binding proteins in kidney stones have great influences on the stone formation. The spatial distributions of these proteins in kidne...

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Autores principales: Yutaro Tanaka, Mihoko Maruyama, Atsushi Okada, Yoshihiro Furukawa, Koichi Momma, Yuki Sugiura, Rie Tajiri, Koichi P. Sawada, Shunichi Tanaka, Kazufumi Takano, Kazumi Taguchi, Shuzo Hamamoto, Ryosuke Ando, Katsuo Tsukamoto, Masashi Yoshimura, Yusuke Mori, Takahiro Yasui
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Publicado: Nature Portfolio 2021
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spelling oai:doaj.org-article:e20f8be2b4294a01b3254129c79fb04c2021-12-02T19:02:23ZMulticolor imaging of calcium-binding proteins in human kidney stones for elucidating the effects of proteins on crystal growth10.1038/s41598-021-95782-12045-2322https://doaj.org/article/e20f8be2b4294a01b3254129c79fb04c2021-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-95782-1https://doaj.org/toc/2045-2322Abstract The pathogenesis of kidney stone formation includes multi-step processes involving complex interactions between mineral components and protein matrix. Calcium-binding proteins in kidney stones have great influences on the stone formation. The spatial distributions of these proteins in kidney stones are essential for evaluating the in vivo effects of proteins on the stone formation, although the actual distribution of these proteins is still unclear. We reveal micro-scale distributions of three different proteins, namely osteopontin (OPN), renal prothrombin fragment 1 (RPTF-1), and calgranulin A (Cal-A), in human kidney stones retaining original mineral phases and textures: calcium oxalate monohydrate (COM) and calcium oxalate dihydrate (COD). OPN and RPTF-1 were distributed inside of both COM and COD crystals, whereas Cal-A was distributed outside of crystals. OPN and RPTF-1 showed homogeneous distributions in COM crystals with mosaic texture, and periodically distributions parallel to specific crystal faces in COD crystals. The unique distributions of these proteins enable us to interpret the different in vivo effects of each protein on CaOx crystal growth based on their physico-chemical properties and the complex physical environment changes of each protein. This method will further allow us to elucidate in vivo effects of different proteins on kidney stone formation.Yutaro TanakaMihoko MaruyamaAtsushi OkadaYoshihiro FurukawaKoichi MommaYuki SugiuraRie TajiriKoichi P. SawadaShunichi TanakaKazufumi TakanoKazumi TaguchiShuzo HamamotoRyosuke AndoKatsuo TsukamotoMasashi YoshimuraYusuke MoriTakahiro YasuiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Yutaro Tanaka
Mihoko Maruyama
Atsushi Okada
Yoshihiro Furukawa
Koichi Momma
Yuki Sugiura
Rie Tajiri
Koichi P. Sawada
Shunichi Tanaka
Kazufumi Takano
Kazumi Taguchi
Shuzo Hamamoto
Ryosuke Ando
Katsuo Tsukamoto
Masashi Yoshimura
Yusuke Mori
Takahiro Yasui
Multicolor imaging of calcium-binding proteins in human kidney stones for elucidating the effects of proteins on crystal growth
description Abstract The pathogenesis of kidney stone formation includes multi-step processes involving complex interactions between mineral components and protein matrix. Calcium-binding proteins in kidney stones have great influences on the stone formation. The spatial distributions of these proteins in kidney stones are essential for evaluating the in vivo effects of proteins on the stone formation, although the actual distribution of these proteins is still unclear. We reveal micro-scale distributions of three different proteins, namely osteopontin (OPN), renal prothrombin fragment 1 (RPTF-1), and calgranulin A (Cal-A), in human kidney stones retaining original mineral phases and textures: calcium oxalate monohydrate (COM) and calcium oxalate dihydrate (COD). OPN and RPTF-1 were distributed inside of both COM and COD crystals, whereas Cal-A was distributed outside of crystals. OPN and RPTF-1 showed homogeneous distributions in COM crystals with mosaic texture, and periodically distributions parallel to specific crystal faces in COD crystals. The unique distributions of these proteins enable us to interpret the different in vivo effects of each protein on CaOx crystal growth based on their physico-chemical properties and the complex physical environment changes of each protein. This method will further allow us to elucidate in vivo effects of different proteins on kidney stone formation.
format article
author Yutaro Tanaka
Mihoko Maruyama
Atsushi Okada
Yoshihiro Furukawa
Koichi Momma
Yuki Sugiura
Rie Tajiri
Koichi P. Sawada
Shunichi Tanaka
Kazufumi Takano
Kazumi Taguchi
Shuzo Hamamoto
Ryosuke Ando
Katsuo Tsukamoto
Masashi Yoshimura
Yusuke Mori
Takahiro Yasui
author_facet Yutaro Tanaka
Mihoko Maruyama
Atsushi Okada
Yoshihiro Furukawa
Koichi Momma
Yuki Sugiura
Rie Tajiri
Koichi P. Sawada
Shunichi Tanaka
Kazufumi Takano
Kazumi Taguchi
Shuzo Hamamoto
Ryosuke Ando
Katsuo Tsukamoto
Masashi Yoshimura
Yusuke Mori
Takahiro Yasui
author_sort Yutaro Tanaka
title Multicolor imaging of calcium-binding proteins in human kidney stones for elucidating the effects of proteins on crystal growth
title_short Multicolor imaging of calcium-binding proteins in human kidney stones for elucidating the effects of proteins on crystal growth
title_full Multicolor imaging of calcium-binding proteins in human kidney stones for elucidating the effects of proteins on crystal growth
title_fullStr Multicolor imaging of calcium-binding proteins in human kidney stones for elucidating the effects of proteins on crystal growth
title_full_unstemmed Multicolor imaging of calcium-binding proteins in human kidney stones for elucidating the effects of proteins on crystal growth
title_sort multicolor imaging of calcium-binding proteins in human kidney stones for elucidating the effects of proteins on crystal growth
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/e20f8be2b4294a01b3254129c79fb04c
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