Change search
ReferencesLink to record
Permanent link

Direct link
Pro-Inflammatory S100A8 and S100A9 Proteins: Self-Assembly into Multifunctional Native and Amyloid Complexes
Institute of Immunology, University of Muenster, Germany.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
2012 (English)In: International Journal of Molecular Sciences, ISSN 1422-0067, Vol. 13, no 3, 2893-2917 p.Article in journal (Refereed) Published
Abstract [en]

S100A8 and S100A9 are EF-hand Ca2+ binding proteins belonging to the S100 family. They are abundant in cytosol of phagocytes and play critical roles in numerous cellular processes such as motility and danger signaling by interacting and modulating the activity of target proteins. S100A8 and S100A9 expression levels increased in many types of cancer, neurodegenerative disorders, inflammatory and autoimmune diseases and they are implicated in the numerous disease pathologies. The Ca2+ and Zn2+-binding properties of S100A8/A9 have a pivotal influence on their conformation and oligomerization state, including self-assembly into homo- and heterodimers, tetramers and larger oligomers. Here we review how the unique chemical and conformational properties of individual proteins and their structural plasticity at the quaternary level account for S100A8/A9 functional diversity. Additional functional diversification occurs via non-covalent assembly into oligomeric and fibrillar amyloid complexes discovered in the aging prostate and reproduced in vitro. This process is also regulated by Ca2+ and Zn2+-binding and effectively competes with the formation of the native complexes. High intrinsic amyloid-forming capacity of S100A8/A9 proteins may lead to their amyloid depositions in numerous ailments characterized by their elevated expression patterns and have additional pathological significance requiring further thorough investigation.

Place, publisher, year, edition, pages
2012. Vol. 13, no 3, 2893-2917 p.
Keyword [en]
S100A8, S100A9, S100 proteins, amyloid, inflammation, cancer, self-assembly, calcium-binding, calprotectin
National Category
Structural Biology Biochemistry and Molecular Biology
URN: urn:nbn:se:umu:diva-55620DOI: 10.3390/ijms13032893ISI: 000302174500024OAI: diva2:528123
Available from: 2012-05-24 Created: 2012-05-24 Last updated: 2012-05-29Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Gharibyan, AnnaMorozova-Roche, Ludmilla
By organisation
Department of Medical Biochemistry and Biophysics
In the same journal
International Journal of Molecular Sciences
Structural BiologyBiochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 72 hits
ReferencesLink to record
Permanent link

Direct link