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Colony Forming Cell (CFC) Assay for Human Hematopoietic Cells

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pp60c-src activation in human colon carcinoma.

C A Cartwright¹, M P Kamps, A I Meisler

¹Molecular Biology and Virology Laboratory, Salk Institute, San Diego, California 92138.

The Journal of Clinical Investigation

|June 1, 1989

Summary

The protein-tyrosine kinase pp60c-src shows significantly elevated activity in human colon carcinoma cell lines and tumors. This increased activity suggests a role for activated pp60c-src in colon cancer development.

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Area of Science:

Oncology
Molecular Biology
Biochemistry

Background:

The protein-tyrosine kinase pp60c-src is involved in cell growth and differentiation.
Dysregulation of pp60c-src activity has been implicated in various cancers.

Purpose of the Study:

To investigate the in vitro protein-tyrosine kinase activity of pp60c-src in human colon carcinoma.
To determine if elevated pp60c-src activity correlates with colon cancer development.

Main Methods:

Measurement of pp60c-src in vitro kinase activity using enolase phosphorylation and autophosphorylation assays.
Immunoblotting with anti-phosphotyrosine antibodies to detect tyrosine-phosphorylated proteins.

Main Results:

pp60c-src activity was significantly higher (5-8 fold) in 6/9 colon carcinoma cell lines and 13/21 primary colon carcinomas compared to normal colonic mucosa.
Elevated pp60c-src activity was not solely due to increased protein levels, indicating enhanced specific activity.
Colon carcinoma cells exhibited increased in vivo tyrosine phosphorylation of proteins, correlating with elevated pp60c-src kinase activity.

Conclusions:

The specific activity of pp60c-src kinase is elevated in colon carcinoma cells and tumors.
Activated protein-tyrosine kinase(s), likely including pp60c-src, are present in colon cancer.
These findings suggest a potential role for pp60c-src in the pathogenesis of colon cancer.