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Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein
Published on: January 16, 2020
Increased farnesyltransferase activity in human colorectal cancer: relationship with clinicopathological features and
M G Caruso1, M Notarnicola, M Bifulco
1Laboratory of Biochemistry, Institute for Digestive Diseases, Castellana Grotte, Bari, Italy.
Background:
The enzyme farnesyltransferase has emerged as an important target for anti-cancer therapies. Farnesyltransferase inhibitors have been introduced in clinical trials of subjects with colorectal cancer. We investigated Farnesyltransferase activity, beta-subunit Farnesyltransferase protein expression and its mRNA in patients with colorectal cancer and its relationship with clinicopathological features and K-ras mutation.
Methods:
Farnesyltransferase activity was determined by Farnesyltransferase [3H] SPA enzyme assay. Beta-subunit Farnesyltransferase protein expression was investigated by Western blotting and its mRNA by reverse transcriptase-polymerase chain reaction. K-ras mutation was detected by polymerase chain reaction amplification and restriction enzyme analysis. Multiple linear regression analysis was used to analyse relationships among age, sex, site of tumour, Dukes' stage, histological differentiation, K-ras mutation and Farnesyltransferase activity in normal mucosa and cancer.
Results:
The levels of Farnesyltransferase activity and beta-subunit Farnesyltransferase protein expression were significantly higher in cancer than in normal mucosa. Moreover, tumours located on the right side, with mucinous histological differentiation and with K-ras mutation showed higher levels of Farnesyltransferase activity.
Conclusions:
Our findings suggest that Farnesyltransferase activity may be a potential marker of tumourigenicity. The differences in Farnesyltransferase activity in relation to histological grading, tumour location and K-ras mutation described here may constitute a starting point for investigating the causes of this variation within the large bowel.
Insights
Farnesyltransferase activity and protein expression are elevated in colorectal cancer, particularly with K-ras mutations and specific tumor characteristics. This suggests Farnesyltransferase may indicate tumor development.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Farnesyltransferase is a key target in anti-cancer drug development.
- Farnesyltransferase inhibitors are in clinical trials for colorectal cancer.
- Investigating Farnesyltransferase in colorectal cancer is crucial for therapeutic advancements.
Purpose of the Study:
- To assess Farnesyltransferase activity, protein, and mRNA levels in colorectal cancer patients.
- To explore the relationship between Farnesyltransferase and clinicopathological features, including K-ras mutation.
Main Methods:
- Enzyme activity assays (Farnesyltransferase [3H] SPA).
- Protein expression analysis (Western blotting).
- mRNA analysis (RT-PCR) and K-ras mutation detection (PCR, restriction enzyme analysis).
- Statistical analysis (multiple linear regression).
Main Results:
- Significantly higher Farnesyltransferase activity and beta-subunit protein expression in cancer tissue compared to normal mucosa.
- Elevated Farnesyltransferase activity correlated with right-sided tumors, mucinous differentiation, and K-ras mutations.
Conclusions:
- Farnesyltransferase activity may serve as a biomarker for colorectal cancer tumorigenicity.
- Variations in Farnesyltransferase activity linked to histological grade, tumor location, and K-ras mutation warrant further investigation.
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