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Basic Sciences

Human Fibroblasts Contain a Proteolytic Activity Which Is Inhibited by the Bowman-Birk Protease Inhibitor

Paul C. Billings, Joan M. Habres, David C. Liao and Stephen W. Tuttle
Paul C. Billings
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Joan M. Habres
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David C. Liao
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Stephen W. Tuttle
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DOI:  Published October 1991
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Abstract

The Bowman Birk protease inhibitor (BBI) has been shown to be an effective suppressor of carcinogenesis in vivo and in vitro. In this report we demonstrate that normal human fibroblasts and Bloom cells contain a BBI-inhibitable proteolytic activity. The enzyme cleaves gelatin, has a molecular mass of 43 kDa, and is located in the cytosol. This activity has maximal activity at pH 8 and was inhibited by diisopropylfluorophosphate but was not affected by EDTA or 1,10-phenanthroline, indicating that this enzyme is a serine protease. We have reported previously that a similar BBI-inhibitable activity is present in C3H/10T1/2 mouse embryo fibroblast cells. Our results suggest that a common “target enzyme” of the BBI is present in mouse and human cells.

Footnotes

  • ↵1 This work was supported by NIH Grant CA 45734.

  • Received February 22, 1991.
  • Accepted August 8, 1991.
  • ©1991 American Association for Cancer Research.
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October 1991
Volume 51, Issue 20
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Human Fibroblasts Contain a Proteolytic Activity Which Is Inhibited by the Bowman-Birk Protease Inhibitor
Paul C. Billings, Joan M. Habres, David C. Liao and Stephen W. Tuttle
Cancer Res October 15 1991 (51) (20) 5539-5543;

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Human Fibroblasts Contain a Proteolytic Activity Which Is Inhibited by the Bowman-Birk Protease Inhibitor
Paul C. Billings, Joan M. Habres, David C. Liao and Stephen W. Tuttle
Cancer Res October 15 1991 (51) (20) 5539-5543;
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