RESUMO
Cystic fibrosis transport regulator is a cAMP-dependent chloride channel protein. Normal (non cystic fibrosis) human epidermis stained positive for cystic fibrosis transport regulator as densely as did the eccrine sweat gland when three monoclonal antibodies for R (regulatory) and C (C-terminus) domains of cystic fibrosis transport regulator were used. All the layers of the epidermis took up staining uniformly. A peptide for C-epitope completely blocked the staining with monoclonal antibodies for C. Nested reverse transcription polymerase chain reaction of freshly isolated human epidermal fragments and the eccrine sweat glands amplified the cystic fibrosis transport regulator mRNA sequence derived from exons 13 and 14 to comparable extents. The 526 base pair antisense, but not sense, RNA probe derived from exons 10-13 stained cystic fibrosis transport regulator mRNA in both the epidermis and the sweat gland to a similar extent. In the epidermis, the cytoplasm of basal cells, stratum spinosum cells, and granular layer cells were all stained uniformly, but not corneocytes in the stratum corneum. In the sweat secretory coils, both clear and dark cells were stained but not the myoepithelium, with the dark cells staining more densely than the clear cells as in a previous study. In the duct, both luminal and basal ductal cells took up cystic fibrosis transport regulator staining uniformly but luminal cytoplasm of luminal ductal cells was devoid of cystic fibrosis transport regulator mRNA. Although the function of cystic fibrosis transport regulator in the epidermis is totally unknown, its recently proposed role as a universal regulator of a variety of cellular and membrane functions necessitates further studies on its regulation and function in health and disease.