Intracellular and extracellular roles of S100 proteins
Open accessAbstract
S100, a multigenic family of non‐ubiquitous Ca 2+‐modulated proteins of the EF‐hand type expressed in vertebrates exclusively, has been implicated in intracellular and extracellular regulatory activities. Members of this protein family have been shown to interact with several effector proteins within cells thereby regulating enzyme activities, the dynamics of cytoskeleton constituents, cell growth and differentiation, and Ca 2+ homeostasis. Structural information indicates that most of S100 proteins exist in the form of antiparallelly packed homodimers (in some cases heterodimers), capable of functionally crossbridging two homologous or heterologous target proteins in a Ca 2+‐dependent (and, in some instances, Ca 2+‐independent) manner. In addition, extracellular roles have been described for several S100 members, although secretion (via an unknown mechanism) has been documented for a few of them. Extracellular S100 proteins have been shown to exert regulatory effects on inflammatory cells, neurons, astrocytes, microglia, and endothelial and epithelial cells, and a cell surface receptor, RAGE, has been identified as a potential S100A12 and S100B receptor transducing the effects of these two proteins on inflammatory cells and neurons. Other cell surface molecules with ability to interact with S100 members have been identified, suggesting that RAGE might not be a universal S100 protein receptor and/or that a single S100 protein might interact with more than one receptor. Collectively, these data indicate that members of the S100 protein family are multifunctional proteins implicated in the regulation of a variety of cellular activities. Microsc. Res. Tech. 60:540–551, 2003. © 2003 Wiley‐Liss, Inc.
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S100A10 is upregulated in multiple human malignancies and plays a key role in regulating tumor progression.
“S100A10, a member of the S100 protein family, is upregulated in multiple human malignancies and plays a key role in regulating tumor progression.”
From miR-21-5p Inhibits the Proliferation, Migration, and Invasion of Glioma by Targeting S100A10 (2023) · cites this paper as [7]
The S100A10 section describes plasminogen activation and blood coagulation, not cancer. The Regulation of Cell Growth and Differentiation section discusses tumor-related findings for other S100 proteins, but our copy does not address whether S100A10 is upregulated in human malignancies or regulates tumor progression (searched: S100A10 with cancer, carcinoma, metastasis, and tumor). (LLM, conf=0.77)
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- Pugh EN Jr, Duda, Sitaramayya T, A Sharma RK. 1997. Photorecep- tor guanylate cyclases: a review. Biosci Rep 17:429 -473.
- Sorci G, Riuzzi F, Marchetti C, Donato R. 2002. S100B causes apo- ptosis in myoblasts and inhibits myogenic differentiation and myo- tube formation in a RAGE-independent manner. Seventh European Symposium on Calcium-Binding Proteins in Normal and Trans- formed Cells Brussels, Belgium, June 12-16, 2002, PJ42.
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- Authors
- Donato, R.
- Affiliations
- University of Perugia (IT)
- Corresponding author
- Donato, Rosario
- ORCID
- Donato, Rosario
- Venue
- Microscopy Research and Technique
- Publisher
- Wiley
- Published
- 2003-03-12
- Volume
- 60
- Issue
- 6
- Pages
- 540-551
- ISSN
- 1059-910X (ISSN-L)
- 1097-0029
- OpenAlex
- W2065140692
- Cited by
- 974
- References
- 0
- Citations by year
- 2026: 7 · 2025: 24 · 2024: 29 · 2023: 25 · 2022: 38 · 2021: 32 · 2020: 25 · 2019: 26 · 2018: 32 · 2017: 29 · 2016: 35 · 2015: 42 · 2014: 45 · 2013: 65 · 2012: 64
- FWCI
- 3.16
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Microscopy Research and Technique (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Università degli Studi di Perugia
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › S100 Proteins and Annexins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Calpain Protease Function and Regulation
- Keywords
- S-100 protein, EF-hand proteins, calcium homeostasis, S100A12, S100B, receptor for advanced glycation end products, RAGE, protein-protein interaction, cytoskeleton regulation, cell growth and differentiation, inflammation, neurons, astrocytes, microglia, endothelial cells, epithelial cells
- MeSH terms
- Animals, Calcium, Cell Physiological Phenomena, Gene Expression Regulation, Humans, Models, Molecular, S100 Proteins, Mice
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