Variant Cathepsin L Activity from Gastric Cancer Tissue

Publisher Website
Google Scholar
Abstract
Cathespin L activity was partially purified by S-epharose FF chromatography, concanavalin-A Sepharose chromatography, phenyl-Superose column chromatography, Mono S column chromatography, and TSK G3000SWXL column chromatography from gastric cancer tissue. The optimal pH of cathespin L from gastric cancer tissue was 7.4, and the activity was retained even at alkaline pH. Heat stability tests showed that cathepsin L from gastric cancer tissue was heat stable; that is, 65% activity was retained after incubation at 56.degree.C for 60 min. The molecular weight of cathepsin L from gastric cancer tissue was estimated as 115 kD gel filtration or 110 kD by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme showed a different affinity of wheat germ agglutinin-Sepharose than cathepsin L from gastric normal mocosa. These results suggest that cathespin L from gastric cancer tissue may play an important role in gastric cancer invasion through the destruction of the surrounding extracellular matrix by its proteolytic activity.

This publication has 18 references indexed in Scilit: