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Tumour Biol. 2003 Aug-Sep;24(4):199-202.

Lactate dehydrogenase isoenzymes 1 and 5: differential expression by neoplastic and stromal cells in non-small cell lung cancer and other epithelial malignant tumors.

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Department of Radiotherapy/Oncology, Democritus University of Thrace, Alexandroupolis, Greece.



Lactate dehydrogenase-5 (LDH-5), an isoenzyme composed of 4 M-polypeptide chains, catalyzes the conversion of pyruvate to lactate with an unparalleled efficiency (anaerobic oxidation), but this function of LDH gradually fades away as the number of H over M chains increases. Thus, LDH-1, another component isoenzyme made up of 4 H-polypeptide chains, favors aerobic oxidation of pyruvate by pyruvate dehydrogenase.


Using immunohistochemistry in this study, we explored the expression of LDH-1 and LDH-5 in a variety of normal and malignant tissues, including lung, breast, endometrium, urinary bladder and large intestine.


LDH-1 was consistently expressed in all living cells, normal and malignant, epithelial and stromal, including endothelium and lymphocytes. In contrast, LDH-5 was expressed preferentially in tumor cells, while normal tissues were devoid of LDH-5 or expressed it only faintly, and the cellular population of the tumor-supporting stroma showed LDH-5 activity in a small percentage of cases. Interestingly, LDH-5-positive stromal cells were associated with hypoxia-inducible factor-1alpha overexpression.


It is concluded that normal tissues utilize aerobic oxidation as a means of energy production, while tumor cells are turned to anaerobic glycolysis, a phenomenon which is rarely followed by the mesenchymal cells of the tumor-supporting stroma.

[Indexed for MEDLINE]

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