Evidence map›Paper›PMID 18606705›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)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.

Ronald Wolf, O M Zack Howard, Hui-Fang Dong, Christopher Voscopoulos, Karen Boeshans, Jason Winston, Rao Divi, Michele Gunsior, Paul Goldsmith, Bijan Ahvazi and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
5.4field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

92 citing papers in PubMed, 167 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Antimicrobial Peptide Signaling in Skin Diseases.JID innovations : skin science from molecules to population health · 2025
    Review
  9. Review
  10. Article
  11. The Central Roles of Keratinocytes in Coordinating Skin Immunity.The Journal of investigative dermatology · 2024
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Pathogenic role of S100 proteins in psoriasis.Frontiers in immunology · 2023
    Review
  19. RAGE Inhibitors for Targeted Therapy of Cancer: A Comprehensive Review.International journal of molecular sciences · 2022
    Review
  20. Review

32 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 4 institutions in 1 country.

Ronald WolfLaboratory of Cancer Biology and Genetics, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892, USA.
O M Zack Howard
Hui-Fang Dong
Christopher Voscopoulos
Karen Boeshans
Jason Winston
Rao Divi
Michele Gunsior
Paul Goldsmith
Bijan Ahvazi
Triantafyllos Chavakis
Joost J Oppenheim
Stuart H Yuspa
Cancer Genetics (United States) · USNational Cancer Institute · USCenter for Cancer Research · USNational Institutes of Health · US

Funding

Studies of Receptor Interactions and Effects of AlarminsZIABC009369 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI OPPENHEIM, JOOST J · 2009 to 2022
$16.5M
Pathways that Suppress or Accelerate Premalignant Progression of Squamous CancerZ01BC005445 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI YUSPA, STUART H. · 1996 to 2008
$2.3M
Regulation of Leukocyte Integrins in Inflammatory Cell RecruitmentZIABC010790 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI CHAVAKIS, TRIANTAFYLLOS · 2009 to 2010
$789k
Intramural NIH HHS Z99 CA999999
6 · The paper itself

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.

Indexed as

Chemotaxis, LeukocyteAnimalsCalcium-Binding ProteinsCell LineHumansInflammationKeratinocytesLymphocyte SubsetsMiceMice, KnockoutReceptor for Advanced Glycation End ProductsReceptors, G-Protein-CoupledReceptors, ImmunologicS100 Calcium Binding Protein A7S100 ProteinsCalcium-Binding ProteinsReceptor for Advanced Glycation End ProductsReceptors, G-Protein-CoupledReceptors, ImmunologicS100A7A protein, humanS100A7 protein, humanS100 Calcium Binding Protein A7S100 Proteins

Identifiers

PMID18606705
PMCPMC2435511
OpenAlexW2148833203

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.