Abstract
Proteinase-activated receptor 2 (PAR-2) has been shown to elicit secretion in a variety of secretory epithelial cells by the transepithelial movement of chloride ions across the apical membrane. However, it is not known whether these receptors are present and/or functional in the secretory epithelial cells of the human eccrine sweat gland. To investigate this possibility mRNA analysis, Ca2+ microspectrofluorimetry and the short circuit current (Isc) technique were used to quantify electrolyte transport in a cell line (NCL-SG3) derived from human eccrine sweat gland secretory epithelia. The results provided molecular and functional evidence of the presence of PAR-2 receptors in the NCL-SG3 cells and show that these receptors can activate transepithelial Cl- secretion possibly via Ca2+-activated Cl- channels.
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