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Fibulin-4 Accelerates Amyloid Formation by Binding with a Keratin 5 Peptide Fragment

Keratins are the major amyloid fibril component in localized cutaneous amyloidosis. We analyzed the amyloid components in the skin of patients with localized cutaneous amyloidosis by immunohistochemical staining using antisera against extracellular matrix proteins and keratin 5 (K5). Fibulin-4 and K...

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Autores principales: Katagiri, Fumihiko, Ueo, Daisuke, Okubo-Gunge, Yumi, Usui, Aya, Kuwatsuka, Sayaka, Mine, Yoshiko, Hamada, Keisuke, Fujiwara, Sakuhei, Sasaki, Takako, Nomizu, Motoyoshi, Utani, Atsushi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9035805/
https://www.ncbi.nlm.nih.gov/pubmed/35480396
http://dx.doi.org/10.1016/j.xjidi.2022.100114
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author Katagiri, Fumihiko
Ueo, Daisuke
Okubo-Gunge, Yumi
Usui, Aya
Kuwatsuka, Sayaka
Mine, Yoshiko
Hamada, Keisuke
Fujiwara, Sakuhei
Sasaki, Takako
Nomizu, Motoyoshi
Utani, Atsushi
author_facet Katagiri, Fumihiko
Ueo, Daisuke
Okubo-Gunge, Yumi
Usui, Aya
Kuwatsuka, Sayaka
Mine, Yoshiko
Hamada, Keisuke
Fujiwara, Sakuhei
Sasaki, Takako
Nomizu, Motoyoshi
Utani, Atsushi
author_sort Katagiri, Fumihiko
collection PubMed
description Keratins are the major amyloid fibril component in localized cutaneous amyloidosis. We analyzed the amyloid components in the skin of patients with localized cutaneous amyloidosis by immunohistochemical staining using antisera against extracellular matrix proteins and keratin 5 (K5). Fibulin-4 and K5 colocalized in the amyloid deposits. Using 14 synthetic peptides, we screened for amyloidogenic sequences in the C-terminal region of K5, including the α-helical rod domain and the tail domain. Two peptides stained with thioflavin T possessed a β-sheet structure and formed amyloid-like fibrils. Among the amyloidogenic peptides, a peptide KT5-6 (YQELMNTKLALDVEIATYRKLLEGE) derived from the α-helical rod domain of K5 specifically bound to fibulin-4. In addition, amyloid formation of KT5-6 was accelerated by fibulin-4. These results suggest that degraded fragments of K5 containing the KT5-6 sequence form amyloid fibrils with fibulin-4. The data further suggest that degraded fragments of K5 and fibulin-4 have the potential to initiate cutaneous amyloidosis.
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spelling pubmed-90358052022-04-26 Fibulin-4 Accelerates Amyloid Formation by Binding with a Keratin 5 Peptide Fragment Katagiri, Fumihiko Ueo, Daisuke Okubo-Gunge, Yumi Usui, Aya Kuwatsuka, Sayaka Mine, Yoshiko Hamada, Keisuke Fujiwara, Sakuhei Sasaki, Takako Nomizu, Motoyoshi Utani, Atsushi JID Innov Original Article Keratins are the major amyloid fibril component in localized cutaneous amyloidosis. We analyzed the amyloid components in the skin of patients with localized cutaneous amyloidosis by immunohistochemical staining using antisera against extracellular matrix proteins and keratin 5 (K5). Fibulin-4 and K5 colocalized in the amyloid deposits. Using 14 synthetic peptides, we screened for amyloidogenic sequences in the C-terminal region of K5, including the α-helical rod domain and the tail domain. Two peptides stained with thioflavin T possessed a β-sheet structure and formed amyloid-like fibrils. Among the amyloidogenic peptides, a peptide KT5-6 (YQELMNTKLALDVEIATYRKLLEGE) derived from the α-helical rod domain of K5 specifically bound to fibulin-4. In addition, amyloid formation of KT5-6 was accelerated by fibulin-4. These results suggest that degraded fragments of K5 containing the KT5-6 sequence form amyloid fibrils with fibulin-4. The data further suggest that degraded fragments of K5 and fibulin-4 have the potential to initiate cutaneous amyloidosis. Elsevier 2022-03-09 /pmc/articles/PMC9035805/ /pubmed/35480396 http://dx.doi.org/10.1016/j.xjidi.2022.100114 Text en © 2022 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Original Article
Katagiri, Fumihiko
Ueo, Daisuke
Okubo-Gunge, Yumi
Usui, Aya
Kuwatsuka, Sayaka
Mine, Yoshiko
Hamada, Keisuke
Fujiwara, Sakuhei
Sasaki, Takako
Nomizu, Motoyoshi
Utani, Atsushi
Fibulin-4 Accelerates Amyloid Formation by Binding with a Keratin 5 Peptide Fragment
title Fibulin-4 Accelerates Amyloid Formation by Binding with a Keratin 5 Peptide Fragment
title_full Fibulin-4 Accelerates Amyloid Formation by Binding with a Keratin 5 Peptide Fragment
title_fullStr Fibulin-4 Accelerates Amyloid Formation by Binding with a Keratin 5 Peptide Fragment
title_full_unstemmed Fibulin-4 Accelerates Amyloid Formation by Binding with a Keratin 5 Peptide Fragment
title_short Fibulin-4 Accelerates Amyloid Formation by Binding with a Keratin 5 Peptide Fragment
title_sort fibulin-4 accelerates amyloid formation by binding with a keratin 5 peptide fragment
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9035805/
https://www.ncbi.nlm.nih.gov/pubmed/35480396
http://dx.doi.org/10.1016/j.xjidi.2022.100114
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