The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Chemotactic Activity of S100A7 (Psoriasin) Is Mediated by the Receptor for Advanced Glycation End Products and Potentiates Inflammation with Highly Homologous but Functionally Distinct S100A15
Open accessAbstract
Human S100A7 (psoriasin) is overexpressed in inflammatory diseases. The recently discovered, co-evolved hS100A15 is almost identical in sequence and up-regulated with hS100A7 during cutaneous inflammation. The functional role of these closely related proteins for inflammation remains undefined. By generating specific Abs, we demonstrate that hS100A7 and hS100A15 proteins are differentially expressed by specific cell types in the skin. Although highly homologous, both proteins are chemoattractants with distinct chemotactic activity for leukocyte subsets. We define RAGE (receptor for advanced glycation end products) as the hS100A7 receptor, whereas hS100A15 functions through a Gi protein-coupled receptor. hS100A7-RAGE binding, signaling, and chemotaxis are zinc-dependent in vitro, reflecting the previously reported zinc-mediated changes in the hS100A7 dimer structure. When combined, hS100A7 and hS100A15 potentiate inflammation in vivo. Thus, proinflammatory synergism in disease may be driven by the diverse biology of these almost identical proteins that have just recently evolved. The identified S100A7 interaction with RAGE may provide a novel therapeutic target for inflammation.
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Cites
RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain
Deane, R., Du Yan, S., Submamaryan, R. K., LaRue, B., Jovanovic, S., Hogg, E., Welch, D., Manness, L., Lin, C., Yu, J., et al. (2003) · Nature Medicine · doi:10.1038/nm890 · Cited by 1,426
Immune cell migration in inflammation: present and future therapeutic targets
Luster, A. D., Alon, R., & von Andrian, U. H. (2005) · Nature Immunology · doi:10.1038/ni1275 · Cited by 1,313
Understanding RAGE, the receptor for advanced glycation end products
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Self-citationBlockade of RAGE-amphoterin signalling suppresses tumour growth and metastases
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Intracellular and extracellular roles of S100 proteins
Donato, R. (2003) · Microscopy Research and Technique · doi:10.1002/jemt.10296 · Cited by 974
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
S100A7 (Psoriasin) – Mechanism of Antibacterial Action in Wounds
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S100A15, an Antimicrobial Protein of the Skin: Regulation by E. coli through Toll-Like Receptor 4
Büchau, A. S., Hassan, M., Kukova, G., Lewerenz, V., Kellermann, S., Würthner, J. U., Wolf, R., Walz, M., Gallo, R. L., & Ruzicka, T. (2007) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700946 · Cited by 79
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Cited by
HMGB1 and RAGE in Inflammation and Cancer
Sims, G. P., Rowe, D. C., Rietdijk, S. T., Herbst, R., & Coyle, A. J. (2010) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132603 · Cited by 1,436
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Ehrchen, J. M., Sunderkötter, C., Foell, D., Vogl, T., & Roth, J. (2009) · Journal of Leukocyte Biology · doi:10.1189/jlb.1008647 · Cited by 846
Sparvero, L. J., Asafu-Adjei, D., Kang, R., Tang, D., Amin, N., Im, J., Rutledge, R., Lin, B., Amoscato, A. A., Zeh, H. J., et al. (2009) · Journal of Translational Medicine · doi:10.1186/1479-5876-7-17 · Cited by 622
The IL-23/T17 pathogenic axis in psoriasis is amplified by keratinocyte responses
Lowes, M. A., Russell, C. B., Martin, D. A., Towne, J. E., & Krueger, J. G. (2013) · Trends in Immunology · doi:10.1016/j.it.2012.11.005 · Cited by 537
Metadata
- Authors
- Wolf, R., Howard, O. M. Z., Dong, H.-F., Voscopoulos, C., Boeshans, K., Winston, J., Divi, R., Gunsior, M., Goldsmith, P., Ahvazi, B., Chavakis, T., Oppenheim, J. J., & Yuspa, S. H.
- Venue
- The Journal of Immunology
- Publisher
- Oxford University Press (OUP)
- Published
- 2008-07
- Volume
- 181
- Issue
- 2
- Pages
- 1499-1506
- ISSN
- 0022-1767 (ISSN-L)
- 1550-6606
- OpenAlex
- W2148833203
- Cited by
- 173
- References
- 8
- FWCI
- 4.84
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Chemotactic Activity of S100A7 (Psoriasin) Is Mediated by the Receptor for Advanced Glycation End Products and Potentiates Inflammation with Highly Homologous but Functionally Distinct S100A15. https://app.cochat.ai/papers/10.4049/jimmunol.181.2.1499
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- Wolf, R., Howard, O. M. Z., Dong, H.-F., Voscopoulos, C., Boeshans, K., Winston, J., Divi, R., Gunsior, M., Goldsmith, P., Ahvazi, B., Chavakis, T., Oppenheim, J. J., & Yuspa, S. H. (2008). Chemotactic Activity of S100A7 (Psoriasin) Is Mediated by the Receptor for Advanced Glycation End Products and Potentiates Inflammation with Highly Homologous but Functionally Distinct S100A15. The Journal of Immunology. https://doi.org/10.4049/jimmunol.181.2.1499
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