International Journal of Molecular Sciences | |
Pro-Inflammatory S100A8 and S100A9 Proteins: Self-Assembly into Multifunctional Native and Amyloid Complexes | |
Thomas Vogl1  Anna L. Gharibyan2  | |
[1] Institute of Immunology, University of Muenster, Röntgenstr. 21, 48149 Muenster, Germany; E-Mail:;Department of Medical Biochemistry and Biophysics, Umea University, SE-901 87 Umea, Sweden; E-Mail: | |
关键词: S100A8; S100A9; S100 proteins; amyloid; inflammation; cancer; self-assembly; calcium-binding; calprotectin; | |
DOI : 10.3390/ijms13032893 | |
来源: mdpi | |
【 摘 要 】
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
【 授权许可】
CC BY
© 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.
【 预 览 】
Files | Size | Format | View |
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RO202003190045716ZK.pdf | 704KB | download |