The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Functions of S100 Proteins
Open accessAbstract
The S100 protein family consists of 24 members functionally distributed into three main subgroups: those that only exert intracellular regulatory effects, those with intracellular and extracellular functions and those which mainly exert extracellular regulatory effects. S100 proteins are only expressed in vertebrates and show cell-specific expression patterns. In some instances, a particular S100 protein can be induced in pathological circumstances in a cell type that does not express it in normal physiological conditions. Within cells, S100 proteins are involved in aspects of regulation of proliferation, differentiation, apoptosis, Ca2+ homeostasis, energy metabolism, inflammation and migration/invasion through interactions with a variety of target proteins including enzymes, cytoskeletal subunits, receptors, transcription factors and nucleic acids. Some S100 proteins are secreted or released and regulate cell functions in an autocrine and paracrine manner via activation of surface receptors (e.g. the receptor for advanced glycation end-products and toll-like receptor 4), G-protein-coupled receptors, scavenger receptors, or heparan sulfate proteoglycans and N-glycans. Extracellular S100A4 and S100B also interact with epidermal growth factor and basic fibroblast growth factor, respectively, thereby enhancing the activity of the corresponding receptors. Thus, extracellular S100 proteins exert regulatory activities on monocytes/macrophages/microglia, neutrophils, lymphocytes, mast cells, articular chondrocytes, endothelial and vascular smooth muscle cells, neurons, astrocytes, Schwann cells, epithelial cells, myoblasts and cardiomyocytes, thereby participating in innate and adaptive immune responses, cell migration and chemotaxis, tissue development and repair, and leukocyte and tumor cell invasion.
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Cites
Donato, R. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00046-2 · Cited by 1,580
Self-citationVogl, T., Tenbrock, K., Ludwig, S., Leukert, N., Ehrhardt, C., van Zoelen, M. A. D., Nacken, W., Foell, D., van der Poll, T., Sorg, C., et al. (2007) · Nature Medicine · doi:10.1038/nm1638 · Cited by 1,418 · cited 5×
“One report indicates that S100A9 induces TNF- , IL-1 , IL-6 and IL-8 in macrophages via NF- B activation [228] whereas another claims that it principally activates neutrophils via TLR-4 [60] and S100A9 decreases phorbol-12-myristate-13-acetate-triggered peroxide production by BCG-activated macrophages [229].”
BackgroundInfluentialUnderstanding RAGE, the receptor for advanced glycation end products
Bierhaus, A., Humpert, P. M., Morcos, M., Wendt, T., Chavakis, T., Arnold, B., Stern, D. M., & Nawroth, P. P. (2005) · Journal of Molecular Medicine · doi:10.1007/s00109-005-0688-7 · Cited by 1,297
Antimicrobial psoriasin (S100A7) protects human skin from Escherichia coli infection
Gläser, R., Harder, J., Lange, H., Bartels, J., Christophers, E., & Schröder, J.-M. (2005) · Nature Immunology · doi:10.1038/ni1142 · Cited by 651
Peripheral blood proteins predict mortality in idiopathic pulmonary fibrosis
Richards, T. J., Kaminski, N., Baribaud, F., Flavin, S., Brodmerkel, C., Horowitz, D., Li, K., Choi, J., Vuga, L. J., Lindell, K. O., et al. (2012) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201101-0058oc · Cited by 381
Arumugam, T., Ramachandran, V., & Logsdon, C. D. (2006) · JNCI: Journal of the National Cancer Institute · doi:10.1093/jnci/djj498 · Cited by 159
Averill, M. M., Barnhart, S., Becker, L., Li, X., Heinecke, J. W., LeBoeuf, R. C., Hamerman, J. A., Sorg, C., Kerkhoff, C., & Bornfeldt, K. E. (2011) · Circulation · doi:10.1161/circulationaha.110.985523 · Cited by 155
Hyperzincaemia and hypercalprotectinaemia: a new disorder of zinc metabolism
Sampson, B., Fagerhol, M. K., Sunderkötter, C., Golden, B. E., Richmond, P., Klein, N., Kovar, I. Z., Beattie, J. H., Wolska-Kusnierz, B., Saito, Y., et al. (2002) · The Lancet · doi:10.1016/s0140-6736(02)11683-7 · Cited by 122
S100A7 (Psoriasin) – Mechanism of Antibacterial Action in Wounds
Lee, K. C., & Eckert, R. L. (2007) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700663 · Cited by 116
Hofmann Bowman, M. A., Gawdzik, J., Bukhari, U., Husain, A. N., Toth, P. T., Kim, G., Earley, J., & McNally, E. M. (2011) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/atvbaha.110.217745 · Cited by 111
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Peinado, H., Zhang, H., Matei, I. R., Costa-Silva, B., Hoshino, A., Rodrigues, G., Psaila, B., Kaplan, R. N., Bromberg, J. F., Kang, Y., et al. (2017) · Nature Reviews Cancer · doi:10.1038/nrc.2017.6 · Cited by 1,889
Verkhratsky, A., & Nedergaard, M. (2018) · Physiological Reviews · doi:10.1152/physrev.00042.2016 · Cited by 1,678
Pyroptosis versus necroptosis: similarities, differences, and crosstalk
Frank, D., & Vince, J. E. (2019) · Cell Death & Differentiation · doi:10.1038/s41418-018-0212-6 · Cited by 1,062
Decoding cell death signals in liver inflammation
Brenner, C., Galluzzi, L., Kepp, O., & Kroemer, G. (2013) · Journal of Hepatology · doi:10.1016/j.jhep.2013.03.033 · Cited by 1,022
Lu, H., Zhou, Q., He, J., Jiang, Z., Peng, C., Tong, R., & Shi, J. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00315-3 · Cited by 891
Metadata
- Authors
- Donato, R., R. Cannon, B., Sorci, G., Riuzzi, F., Hsu, K., J. Weber, D., & L. Geczy, C.
- Venue
- Current Molecular Medicine
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2013-01-01
- Volume
- 13
- Issue
- 1
- Pages
- 24-57
- ISSN
- 1566-5240 (ISSN-L)
- OpenAlex
- W2161888715
- Cited by
- 1,316
- References
- 13
- FWCI
- 19.28
- Type
- journal article
- Language
- en
- Open access
- green
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