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Relationship between cell surface protease activity and doubling time in various normal and transformed cells
Biochimica Et Biophysica Acta
|December 21, 1976
Summary
This study introduces a new radioassay to measure cell surface protease activity. Transformed cells and cells undergoing mitosis show higher protease levels, suggesting a role in cell growth regulation.
Area of Science:
- Biochemistry
- Cell Biology
- Enzymology
Background:
- Cell surface proteases play roles in various biological processes.
- Quantifying cell surface protease activity is crucial for understanding cell behavior.
Purpose of the Study:
- To develop a sensitive method for measuring cell surface and secreted protease activity.
- To investigate the characteristics and regulation of cell surface proteases.
Main Methods:
- A radioassay using 3H-labelled casein as a substrate was developed.
- Proteolytic degradation products were measured as trichloracetic acid soluble peptides.
- Cell lines were cultured, synchronized, and their surface protease activity quantified.
Main Results:
- All cultured cell lines exhibited cell surface protease activity not secreted into the media.
- Transformed mouse epidermal cells showed significantly higher protease activity than normal cells.
- Surface protease activity increased during mitosis and correlated inversely with cell doubling times.
Conclusions:
- Cell surface proteases, distinct from plasminogen activator or plasmin, are present in cultured cells.
- Elevated surface protease activity in transformed cells and during mitosis suggests a role in cell proliferation.
- Cell surface proteases may be key regulators of cell growth rates in culture.