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Cited by 173

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 access
Wolf, Ronald, Howard, O M Zack, Dong, Hui-Fang, Voscopoulos, Christopher, Boeshans, Karen, Winston, Jason, Divi, Rao, Gunsior, Michele, Goldsmith, Paul, Ahvazi, Bijan, Chavakis, Triantafyllos, Oppenheim, Joost J, Yuspa, Stuart H·2008·The Journal of Immunology

Abstract

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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Crossref · 10.4049/jimmunol.181.2.1499

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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
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
The paper
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

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.