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A pyruvate kinase variant in different mouse transplanted tumors
E Marchut1, M Gumińska, T Kedryna
1Institute of Medical Biochemistry, Nicolaus Copernicus Academy of Medicine, Cracow, Poland.
Experientia
|January 15, 1988
Summary
Researchers identified a specific pyruvate kinase (PK) variant in mouse tumors that is sensitive to L-cysteine. This tumor-specific PK variant could serve as a potential biomarker for neoplastic transformation.
Area of Science:
- Biochemistry
- Oncology
- Enzymology
Background:
- Normal tissues and transplanted mouse tumors exhibit distinct pyruvate kinase (PK) enzyme characteristics.
- Pyruvate kinase activity and sensitivity to inhibitors vary between normal and cancerous cells.
Purpose of the Study:
- To characterize the pyruvate kinase (PK) variants present in mouse tumors and normal tissues.
- To identify a potential tumor-specific PK variant that could serve as a biomarker for cancer.
Main Methods:
- Separation of pyruvate kinase (PK) fractions from normal mouse tissues (liver) and tumor samples (Ehrlich ascites tumor) using ammonium sulfate precipitation.
- Enzyme assays to determine the sensitivity of PK fractions to L-cysteine and saturated fatty acids.
Main Results:
- Two main PK fractions, A and B, were identified based on their ammonium sulfate saturation levels.
- Fraction B, predominant in skeletal muscle and Ehrlich ascites tumor, displayed sensitivity to L-cysteine inhibition, unlike fraction A found in normal liver.
- This L-cysteine-sensitive fraction B from tumors appears to be a tumor-specific pyruvate kinase (PK) variant.
Conclusions:
- A tumor-specific pyruvate kinase (PK) variant, characterized by L-cysteine sensitivity, exists in mouse experimental tumors.
- This variant may function as a valuable marker for detecting neoplastic transformation across various mouse tumor models.