Steroid sulfatase activity in human lung tissue and in endothelial pulmonary cells in culture.

The conversion of tritium-labeled estrone sulfate to [3H]estrone was evaluated in human lung tissue in vitro. Under standardized conditions, the rate of hydrolysis of [3H] estrone sulfate to [3H]estrone was linear with time of incubation up to 4 h and with wet tissue weight up to 400 mg/ml. The apparent Km of sulfatase for estrone sulfate was 9 microM, and the maximum velocity was 1.4 nmol substrate hydrolyzed/100 mg lung . h. The lung tissue also metabolized the primary metabolite of [3H]estrone sulfate, [3H]estrone, to 17 beta-[3H]estradiol. The hydrolysis of [3H]dehydroisoandrosterone sulfate to [3H]dehydroisoandrosterone by human lung tissue was also measured. Sulfatase activity with this substrate was linear as a function of wet tissue weight up to 800 mg/ml. The apparent Km of sulfatase for dehydroisoandrosterone sulfate was 7 microM, and the maximum velocity was 1.0 nmol substrate hydrolyzed/100 mg lung . h. The highest specific activity of lung sulfatase for [3H]dehydroisoandrosterone sulfate was found in a microsomal fraction of lung homogenate. The primary metabolite, [3H]dehydroisoandrosterone, was metabolized further by lung tissue to [3H]androstenedione and [3H]5-androstene-3 beta, 17 beta-diol. Although isolated segments of human pulmonary arteries also metabolized both [3H] estrone sulfate and [3H]dehydroisoandrosterone sulfate, cultures of pulmonary arterial endothelial cells lacked sulfatase activity. The cell(s) source of sulfatase activity in human lung tissue and isolated arteries has not yet been identified. Our findings suggest that the metabolism of sulfated steroids by the lung should be considered in evaluating homeostasis.