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From the Department of Dermatology (I.M., G.H., J.-H.S., G.S.), University Hospital, Geneva, Switzerland; the Department of Biochemistry (T.H. Van K., J.H.V.), University of Nijmegen (the Netherlands); the Institute of Medical Biochemistry (P.M.), Aarhus (Denmark) University; and the Department of Morphology (M.S.P.), University Medical Center, Geneva, Switzerland.
Correspondence to Dr Georges Siegenthaler, Clinique de Dermatologie, Hopital Universitaire, CH-1211 Geneve 14, Suisse. E-mail siegenth{at}cmu.unige.ch
Abstract Epidermal fatty acidbinding protein (E-FABP), previously characterized in human keratinocytes, is a cytoplasmic protein of 15 kD that specifically binds fatty acids (FAs). Previous PAGE-immunoblotting studies indicated that several human tissues display an immunoreactive band with an electrophoretic mobility identical to that of E-FABP. The aim of this study was to determine in which cells, other than keratinocytes, E-FABP might be expressed. By immunohistochemistry, we show that E-FABP is expressed in endothelial cells of the microvasculature of the placenta, heart, skeletal muscle, small intestine, lung, and renal medulla. Interestingly, in lung, a tissue of endodermal origin, E-FABP staining was also localized to secretory cells, ie, Clara cells, goblet cells, and probably a subpopulation of pneumocytes. RNA isolated from cultured human umbilical vein and normal human dermal microvascular endothelial cells was analyzed by reverse-transcriptase polymerase chain reaction (RT-PCR). Southern blotting and sequencing of the cloned RT-PCR products demonstrate that endothelial E-FABP is identical to keratinocyte E-FABP. These data suggest that E-FABPmediated FA transport occurs at the level of the microvasculature in several FA target organs.
Key Words: fatty acid blood vessel heart placenta lung
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