Elevated phosphorylase kinase activity in psoriatic epidermis: correlation with increased phosphorylation and psoriatic activity

Br J Dermatol. 1994 Mar;130(3):298-306. doi: 10.1111/j.1365-2133.1994.tb02924.x.


To determine whether abnormal activity of a calmodulin-containing enzyme which catalyses phosphorylation reactions may play a pathogenetic role in psoriasis, the presence and activity of phosphorylase kinase (PK) in human epidermis were determined in patients with untreated/active psoriasis (n = 10), treated/resolving psoriasis (n = 10), and non-psoriatic controls (n = 10). Biopsies were taken from involved and uninvolved skin for PK, organic phosphorus, and inorganic phosphate estimation, and light and electron microscopy. The enzyme was present in involved and uninvolved skin of every patient in the study. PK activity (units/mg protein) was significantly higher in active psoriasis than in resolving psoriasis and controls. PK activity correlated directly with organic phosphorus levels, and inversely with the extent of cellular glycogenolysis measured by the depletion of glycogen granules within the keratinocytes. The study demonstrates that PK is present in both psoriatic and normal epidermis, with significantly higher levels in active psoriasis. Furthermore, higher levels of PK activity, glycogenolysis and phosphorylation are associated with increased clinical psoriatic activity. We conclude that PK, a calmodulin-containing enzyme, is involved in regulating calcium-dependent phosphorylation events in human epidermis, and disturbance of its activity may play a key role in the clinical manifestations of psoriasis.

MeSH terms

  • Cytoplasmic Granules
  • Cytosol / chemistry
  • Glycogen / analysis
  • Humans
  • Keratinocytes / chemistry
  • Male
  • Phosphorus / analysis
  • Phosphorylase Kinase / metabolism*
  • Phosphorylation
  • Psoriasis / drug therapy
  • Psoriasis / enzymology*
  • Psoriasis / pathology
  • Skin / enzymology*


  • Phosphorus
  • Glycogen
  • Phosphorylase Kinase