Effects of tinoridine on stability of rat liver and kidney lysosomes, and liver parenchymal cells

Abstract

The stabilizing activity of tinoridine hydrochloride on biomembranes was estimated by means of determining the rate of release of acid phosphatase and aryl sulfatase from lysosomes, or of transaminases from liver parenchymal cells. Tinoridine hydrochloride (10–100 μM), benzydamine hydrochloride (10–100 μM) and phenylbutazone (1–100 μM) stabilized significantly intact lysosomes (700–3500 g fraction), while indomethacin and prednisolone showed only moderate activity. The lysosomes treated with 0.3% hydrogen peroxide were stabilized by tinoridine hydrochloride, phenylbutazone and indomethacin, but not by benzydamine in the concentration range of 1–100 μM. On the fragile liver lysosomes prepared from rats pretreated with carbon tetrachloride and on kidney lysosomes (650–3500 g), only tinoridine hydrochloride had marked stabilizing activity at 1–100 μM among the tested nonsteroidal anti-inflammatory drugs. Prednisolone showed the same activity on these lysosomes as tinoridine hydrochloride. Both tinoridine hydrochloride and prednisolone also stabilized the liver parenchymal cells at 10–100 μM. The elevation of the free activity of lysosomal enzymes in the liver fraction of rats caused by the intraperitoneal injection of carbon tetrachloride (0.5 ml/kg) was really inhibited by the oral treatment with tinoridine hydrochloride (100 mg/kg).