Histochemistry in psoriasis. 5'-Nucleotidase in psoriatic parakeratotic horny layer.
The 5'-nucleotidase activity in psoriatic and normal human epidermis was studied in comparison to acid phosphatase activity. The optimum pH in normal human epidermis was about 5.0 at room temperature. The activity of both enzymes was found to be high in the transitional zone. Acid phosphatase (non-specific) activity was strongly positive in the psoriatic parakeratotic horny layers whereas 5'-nucleotidase activity in that area was completely absent. The results suggest that the enzyme which degrades nucleoside-5'-phosphate to nucleoside and inorganic phosphate is not acid phosphatase but 5'-nucleotidase. Nuclear preservation in psoriatic hyperkeratosis was attributed to absence or inactivation of specific enzymes of nuclear degradation, such as 5'-nucleotidase, rather than acid phosphatase.
D000135:Acid Phosphatase / Q000032:analysis; D000328:Adult; D004817:Epidermis / Q000032:analysis; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007642:Keratosis / Q000201:enzymology*; D009708:Nucleotidases / Q000032:analysis*; D010241:Parakeratosis / Q000201:enzymology*; D011565:Psoriasis / Q000201:enzymology*; D012867:Skin / Q000201:enzymology*
D009708:Nucleotidases; D000135:Acid Phosphatase