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A study of protein synthesis in cells cultured from involved psoriatic skin
Author(s) -
Easty David J.,
Patel Ketan,
Otto William R.,
Dunn Michael J.,
Kiil J.,
Evans David J.
Publication year - 1991
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150120718
Subject(s) - psoriasis , keratin , epidermis (zoology) , keratinocyte , in vitro , downregulation and upregulation , biology , skin equivalent , cellular differentiation , polyacrylamide gel electrophoresis , microbiology and biotechnology , basal (medicine) , chemistry , biochemistry , immunology , enzyme , anatomy , genetics , endocrinology , gene , insulin
Using histochemical techniques an abnormal programme of epidermal differentiation has been well documented in psoriasis. In order to characterise further the biochemistry of this process we have cultured dermal fibroblasts and epidermal keratinocytes from involved psoriatic skin. This has facilitated metabolic radiolabelling of skin cells and analysis of protein synthesis by two‐dimensional polyacrylamide gel electrophoresis. The expression of keratin and differentiation markers was identical to that of normal keratinocytes, suggesting that psoriatic epidermal differentiation is not truncated in vitro as has been postulated to be the case in vivo . Low molecular mass components (5–8.5 kDa), previously shown to be upregulated in suprabasal keratinocytes, were detected in epidermal fractions from psoriatic skin enriched for basal cells. Of especial interest was a component of 26 kDa, p I 5.9, which was highly upregulated in psoriatic as compared to normal cultured keratinocytes and was not detected in fibroblasts. These findings are in accord with a qualitatively abnormal pattern of differentiation for keratinocytes in the involved psoriatic epidermis.