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Related Experiment Videos

Pericellular cathepsin B and malignant progression.

Stefanie Roshy1, Bonnie F Sloane, Kamiar Moin

  • 1Program in Cancer Biology, Barbara Ann Karmanos Cancer Institute, Wayne State University, Detroit, MI 48201, USA.

Cancer Metastasis Reviews
|June 6, 2003
PubMed
Summary

Cathepsin B, a protease upregulated in tumors, is secreted and binds to the cell surface. This localization may initiate proteolytic cascades involved in cancer progression.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Cathepsin B is a lysosomal cysteine protease.
  • In cancer, cathepsin B expression is upregulated, secreted, and cell-surface associated.
  • Its normal lysosomal trafficking involves mannose 6-phosphate receptors (MPRs).

Purpose of the Study:

  • To investigate the role and mechanisms of cathepsin B secretion and cell-surface association in tumors.
  • To explore the interaction of secreted cathepsin B with the annexin II heterotetramer.
  • To hypothesize the involvement of pericellular cathepsin B in proteolytic cascades.

Main Methods:

  • Analysis of cathepsin B expression and secretion in tumor cells.
  • Investigation of procathepsin B binding to the annexin II heterotetramer (p11).

Related Experiment Videos

  • Cellular fractionation to isolate caveolae and assess protein colocalization.

    • Main Results:

    • Tumor cells secrete both inactive procathepsin B and active cathepsin B.
    • Secreted procathepsin B binds to the tumor cell surface via p11, facilitating its activation.
    • Cathepsin B and annexin II heterotetramer colocalize in caveolae.

    Conclusions:

    • Tumor-associated cathepsin B is secreted and actively processed on the cell surface.
    • The annexin II heterotetramer (p11) mediates cell-surface binding and activation of procathepsin B.
    • Pericellular cathepsin B, localized in caveolae with other proteases, may initiate tumor-promoting proteolytic cascades.