Variant cathepsin L activity from gastric cancer tissue

Japanese Journal of Cancer Research : Gann
S M Chung

Abstract

Cathepsin L activity was partially purified by S-Sepharose 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 cathepsin 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 degrees C for 60 min. The molecular weight of cathepsin L from gastric cancer tissue was estimated as 115 kD by gel filtration or 110 kD by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme showed a different affinity for wheat germ agglutinin-Sepharose than cathepsin L from gastric normal mucosa. These results suggest that cathepsin 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.

References

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Jun 5, 1981·Science·B F SloaneK V Honn

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Citations

Jun 1, 1996·Cancer Biotherapy & Radiopharmaceuticals·M SiewinskiW Mikulewicz
Oct 14, 2011·Nutrition Research and Practice·Ha-Neul ChoiJung-In Kim

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Methods Mentioned

BETA
electrophoresis

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