Cargando…
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...
Autores principales: | , , , , , , , , , , |
---|---|
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 |
_version_ | 1784693379357999104 |
---|---|
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. |
format | Online Article Text |
id | pubmed-9035805 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT katagirifumihiko fibulin4acceleratesamyloidformationbybindingwithakeratin5peptidefragment AT ueodaisuke fibulin4acceleratesamyloidformationbybindingwithakeratin5peptidefragment AT okubogungeyumi fibulin4acceleratesamyloidformationbybindingwithakeratin5peptidefragment AT usuiaya fibulin4acceleratesamyloidformationbybindingwithakeratin5peptidefragment AT kuwatsukasayaka fibulin4acceleratesamyloidformationbybindingwithakeratin5peptidefragment AT mineyoshiko fibulin4acceleratesamyloidformationbybindingwithakeratin5peptidefragment AT hamadakeisuke fibulin4acceleratesamyloidformationbybindingwithakeratin5peptidefragment AT fujiwarasakuhei fibulin4acceleratesamyloidformationbybindingwithakeratin5peptidefragment AT sasakitakako fibulin4acceleratesamyloidformationbybindingwithakeratin5peptidefragment AT nomizumotoyoshi fibulin4acceleratesamyloidformationbybindingwithakeratin5peptidefragment AT utaniatsushi fibulin4acceleratesamyloidformationbybindingwithakeratin5peptidefragment |