The proteins of living psoriatic epidermis.

Psoriatic epidermis has a rapid rate of turnover and produces a stratum corneum with an abnormal tonofilament composition. One polypeptide chain, (Mr 70,000) is absent or greatly decreased in relative amount and two other chains, (Mr 63,000 and 55,000), which are normally modified in the living cells, persists into the stratum corneum. Increasing the turnover of normal epidermis has been shown to cause the persistence of 63 and 55 kilodalton chains in the stratum corneum but does not affect the relative amount of 70 kilodalton chain. It has, therefore, been suggested that, in psoriasis, the deficiency of the 70 kilodalton chain may occur prior to or simultaneously with the induction of increased tissue turnover. In the present study, the polypeptide chain composition of living psoriatic epidermis has been examined. It is shown that the relative amounts of 70 kilodalton chain in psoriatic stratum corneum and involved living epidermis from the same site are not significantly different. The abnormality is, therefore, already present in the living cells and it appears that, in psoriasis, the synthesis of the 70 kilodalton chain is defective. The uninvolved epidermis of psoriatics is intermediate between normal and involved psoriatic epidermis both in the ability to synthesise the 70 kilodalton chain and to modify the 63 and 55 kilodalton chains. Comparisons of amino acid compositions of proteins containing different proportions of 70 kilodalton chain suggest that it has a considerably higher content of glycine and serine than the other tonofilament chains. These studies suggest that the 70 kilodalton chain may be functionally different from the other tonofilament chains. The defect in its synthesis in psoriasis is a relatively early event and may be involved with the induction of increased tissue turnover or induced by the same abnormal conditions as the increased tissue turnover.