Amino Acids

, Volume 41, Issue 4, pp 789–796

Novel S100A7 (psoriasin)/S100A15 (koebnerisin) subfamily: highly homologous but distinct in regulation and function

Authors

    • Laboratory of Cancer Biology and Genetics, Center for Cancer ResearchNational Cancer Institute
    • Department of DermatologyLudwig-Maximilian University Munich
  • Thomas Ruzicka
    • Department of DermatologyLudwig-Maximilian University Munich
  • Stuart H. Yuspa
    • Laboratory of Cancer Biology and Genetics, Center for Cancer ResearchNational Cancer Institute
Review Article

DOI: 10.1007/s00726-010-0666-4

Cite this article as:
Wolf, R., Ruzicka, T. & Yuspa, S.H. Amino Acids (2011) 41: 789. doi:10.1007/s00726-010-0666-4

Abstract

S100A7 (psoriasin) and S100A15 (koebnerisin) were first identified in inflamed psoriatic skin. They are of major interest because of their putative functional roles in innate immunity, epidermal cell maturation, and epithelial tumorigenesis. Human S100A7 and S100A15 have lately evolved by gene duplications within the epidermal differentiation complex (chromosome 1q21) during primate evolution forming a novel S100 subfamily. Therefore, S100A7 and S100A15 are almost identical in sequence (>90%) and are difficult to discriminate. Despite their high homology, S100A7 and S100A15 are distinct in tissue distribution, regulation, and function, and thus, exemplary for the diversity within the S100 family. Their different properties are compelling reasons to discriminate S100A7 (psoriasin) and S100A15 (koebnerisin) in epithelial homeostasis, inflammation, and cancer.

Keywords

Calcium-binding proteinS100KoebnerisinPsoriasinEvolutionParalogsRAGEInnate immunityInflammationCancer

Abbreviations

UTR

Untranslated region

EDC

Epidermal differentiation complex

S100A15-L

Long human S100A15 transcript

S100A15-S

Short human S100A15 transcript

TLR

Toll-like receptor

RAGE

Receptor of advanced glycated end products

Copyright information

© Springer-Verlag 2010