Epidermal Fatty-Acid-Binding Protein in Psoriasis, Basal and Squamous Cell Carcinomas: An Immunohistological Study

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Abstract
In human keratinocytes, we have recently characterized a low-molecular-weight cytosolic protein of 15 kD that specifically binds fatty acids (FAs) with high affinity, the epidermal FA-binding protein (E-FABP). The distribution of E-FABP in skin diseases is not known. To localize by immunohistochemistry the expression of E-FABP in psoriasis, basal and squamous cell carcinomas in order to obtain indirect information, at the cellular level, on the transport of the FAs. E-FABP was localized in the upper stratum spinosum and stratum granulosum in normal and non-lesional psoriatic skin. In contrast, lesional psoriatic epidermis strongly expressed E-FABP in all suprabasal layers, like nonkeratinized oral mucosa. The basal layer did not express E-FABP reactivity in any of these samples. Accordingly, basal cell carcinomas were E-FABP negative whereas only well-differentiated cells of squamous cell carcinomas expressed E-FABP. It is unlikely that E-FABP plays a significant role in FA uptake by basal cells. Our data rather indicate that E-FABP expression is related to the commitment of keratinocyte differentiation and that the putative role of E-FABP should not be restricted to the formation of the skin lipid barrier. Since the pattern of E-FABP expression mimics cellular FA transport, our results suggest that lesional psoriatic skin and oral mucosa have a higher metabolism/transport for FAs than normal and non-lesional psoriatic epidermis.

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