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Related Experiment Videos

Tumor cell membrane cathepsin B

K Moin1, L Cao, N A Day

  • 1Department of Pharmacology, Wayne State University School of Medicine, Detroit, MI 48201, USA.

Biological Chemistry
|October 29, 1998
PubMed
Summary

Cathepsin B, an enzyme involved in extracellular matrix degradation, was found on the surface of melanoma cells. Its altered forms in tumors suggest changes in glycosylation and trafficking.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Cancer Research

Background:

  • Cathepsin B is a lysosomal cysteine peptidase.
  • Its role in extracellular matrix degradation is proposed.
  • Association with plasma membrane/endosomal fractions of B16 amelanotic melanoma cells was investigated.

Purpose of the Study:

  • To investigate the localization and characterization of cathepsin B in B16 melanoma cells.
  • To compare cathepsin B from tumor cells with that from normal liver cells.

Main Methods:

  • Confocal microscopy with 3D image analysis.
  • Purification and partial characterization of cathepsin B.
  • SDS-PAGE under reducing conditions.
  • Isoelectric focusing (IEF) to determine isozymes.

Main Results:

  • Cathepsin B was localized to the external basal cell surface of B16 melanoma cells.
  • Tumor cathepsin B appeared as a single 31,000 Mr band, while liver cathepsin B showed 31,000 and 24,000 Mr bands.
  • B16 tumor cathepsin B exhibited four isozymes, whereas liver cathepsin B had five, with differences likely due to altered glycosylation in tumors.

Conclusions:

  • Cathepsin B's presence on the tumor cell surface supports its role in extracellular matrix degradation.
  • Differences in cathepsin B forms and isozymes between tumor and liver cells suggest tumor-specific modifications.
  • Retrograde trafficking from lysosome to endosome and exocytosis likely contribute to cathepsin B's association with the tumor cell membrane.

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