Review Article

Amino Acids

, Volume 41, Issue 4, pp 789-796

First online:

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

  • Ronald WolfAffiliated withLaboratory of Cancer Biology and Genetics, Center for Cancer Research, National Cancer InstituteDepartment of Dermatology, Ludwig-Maximilian University Munich Email author 
  • , Thomas RuzickaAffiliated withDepartment of Dermatology, Ludwig-Maximilian University Munich
  • , Stuart H. YuspaAffiliated withLaboratory of Cancer Biology and Genetics, Center for Cancer Research, National Cancer Institute

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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 protein S100 Koebnerisin Psoriasin Evolution Paralogs RAGE Innate immunity Inflammation Cancer