umu.sePublikationer
Ändra sökning
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
S100A8/A9 amyloidosis in the ageing prostate: relating ex vivo and in vitro studies
Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk kemi och biofysik.
Department of Life Sciences, Ben Gurion University of the Negev, Israel.
Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk kemi och biofysik.
2012 (Engelska)Ingår i: Amyloid Proteins: Methods and Protocols / [ed] Einar M. Sigurdsson, Miguel Calero, María Gasset, Springer Science+Business Media B.V., 2012, Vol. 849, s. 387-401Kapitel i bok, del av antologi (Refereegranskat)
Abstract [en]

The family of S100 proteins encompasses more than 20 members characterized by remarkable conformational and functional diversity. S100 proteins act as central regulators of various cellular processes, including cell survival, proliferation, differentiation, and motility. Many S100 proteins are implicated in various types of cancer as well as neurodegenerative, inflammatory, and autoimmune diseases. Recently, we have found that S100A8⁄A9 proteins are involved in amyloidogenic process in the ageing prostate, contributing to the formation of calcified corpora amylacea (CA) inclusions, which commonly accompany age-dependent prostate tissue remodelling and cancer. Amyloid formation by S100A8/A9 proteins can also be modelled in vitro. Amyloid assembly of S100A8/A9 proteins into oligomeric and fibrillar complexes is modulated by metal ions such as calcium and zinc. Here, we provide insights into the extraction procedures and review the common structural features of ex vivo and in vitro S100A8/A9 amyloids, showing that they share the same generic origin.

Ort, förlag, år, upplaga, sidor
Springer Science+Business Media B.V., 2012. Vol. 849, s. 387-401
Serie
Methods and Protocols, ISSN 1064-3745 ; 849
Nationell ämneskategori
Biokemi och molekylärbiologi
Forskningsämne
biomedicinsk laboratorievetenskap
Identifikatorer
URN: urn:nbn:se:umu:diva-55619DOI: 10.1007/978-1-61779-551-0_26ISBN: 978-1-61779-550-3 (tryckt)ISBN: 978-1-61779-551-0 (tryckt)OAI: oai:DiVA.org:umu-55619DiVA, id: diva2:528116
Tillgänglig från: 2012-05-24 Skapad: 2012-05-24 Senast uppdaterad: 2018-06-08Bibliografiskt granskad

Open Access i DiVA

Fulltext saknas i DiVA

Övriga länkar

Förlagets fulltexthttp://www.springerprotocols.com/Abstract/doi/10.1007/978-1-61779-551-0_26

Personposter BETA

Gharibyan, AnnaMorozova-Roche, Ludmilla

Sök vidare i DiVA

Av författaren/redaktören
Gharibyan, AnnaMorozova-Roche, Ludmilla
Av organisationen
Institutionen för medicinsk kemi och biofysik
Biokemi och molekylärbiologi

Sök vidare utanför DiVA

GoogleGoogle Scholar

doi
isbn
urn-nbn

Altmetricpoäng

doi
isbn
urn-nbn
Totalt: 250 träffar
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf