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pp60c-src activation in lung adenocarcinoma.
T Masaki1, K Igarashi, M Tokuda
1Third Department of Internal Medicine, Kagawa Medical University, 1750-1 Ikenobe Miki-cho, Kagawa 761-0793, Japan.
European Journal of Cancer (Oxford, England : 1990)
|June 27, 2003
Summary
pp60c-src tyrosine kinase activity is elevated in non-small cell lung cancers (NSCLC), particularly adenocarcinomas. This activation, linked to dephosphorylation at Tyr 530, suggests a role in lung adenocarcinoma progression.
Area of Science:
- Oncology
- Molecular Biology
- Biochemistry
Background:
- Src family kinases are cytoplasmic or membrane-associated protein tyrosine kinases.
- Elevated pp60c-src tyrosine kinase activity correlates with cell transformation.
- The activation status of pp60c-src in non-small cell lung cancers (NSCLC) is not well understood.
Purpose of the Study:
- To investigate the activity level of pp60c-src in NSCLC.
- To determine the role of pp60c-src activation in lung adenocarcinoma progression.
Main Methods:
- Western blotting to measure pp60c-src expression.
- In vitro kinase assays to assess protein tyrosine kinase activity.
- Two-dimensional tryptic phosphopeptide mapping to evaluate pp60c-src phosphorylation.
Main Results:
- pp60c-src kinase activity was significantly activated in NSCLC, especially in adenocarcinomas.
- Activated pp60c-src kinase activity correlated positively with adenocarcinoma size.
- Dephosphorylation of pp60c-src at Tyr 530 was observed in adenocarcinomas.
Conclusions:
- pp60c-src is activated in NSCLC, particularly adenocarcinomas, partly due to Tyr 530 dephosphorylation.
- Activated pp60c-src may contribute to the progression of lung adenocarcinomas.