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Lactate Dehydrogenase Isoenzymes 1 and 5: Differential Expression by Neoplastic and Stromal Cells in Non-Small Cell Lung Cancer and Other Epithelial Malignant Tumors

Koukourakis M.I.a · Giatromanolaki A.b · Sivridis E.b
Departments of aRadiotherapy/Oncology and bPathology, Democritus University of Thrace, Alexandroupolis, Greece Tumor Biol 2003;24:199–202 (DOI:10.1159/000074430)

Abstract

Background/Aims: 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. Methods: 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. Results: 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-1α overexpression. Conclusion: 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.

 

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