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.