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Potential intracellular target proteins of the anticarcinogenic Bowman Birk protease inhibitor identified by affinity

P C Billings1, W St Clair, A J Owen

  • 1Department of Cancer Biology, Harvard School of Public Health, Boston, Massachusetts 02115.

Cancer Research
|April 1, 1988
PubMed

Insights

Soybean Bowman Birk inhibitor (BBI) targets cellular enzymes involved in cancer prevention. Researchers identified 50- and 60-kilodalton proteins in mouse and human cells that interact with BBI, suggesting potential intracellular roles.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • The soybean-derived Bowman Birk inhibitor (BBI) demonstrates anti-carcinogenic properties in various models.
  • Protease inhibitors, including BBI, have been observed to reduce chromosomal aberrations in Bloom syndrome fibroblasts.

Purpose of the Study:

  • To investigate specific cellular enzyme interactions with BBI using affinity chromatography.
  • To identify potential intracellular targets of BBI within C3H/10T1/2 cells.

Main Methods:

  • Affinity chromatography utilizing a BBI-conjugated column.
  • Analysis of protein binding to the BBI column.
  • Cell fractionation to localize identified proteins.

Main Results:

  • Three proteins with masses of approximately 70, 60, and 50 kilodaltons were identified as interacting with BBI.
  • The 60- and 50-kilodalton proteins were localized to the lysosomal/Golgi fraction of C3H/10T1/2 cell homogenates.
  • Similar 60- and 50-kilodalton proteins were found to bind the BBI column in Bloom syndrome fibroblasts.

Conclusions:

  • The 50- and 60-kilodalton proteins identified are present in both mouse and human cells.
  • These proteins represent potential intracellular targets for BBI's cancer-inhibiting effects.

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