Evaluation of Serum Pyruvate Kinase M2 and Key Glycolytic Signatures and Its Correlation with Phosphatidylinositol-3-kinase/Akt/Mammalian Target of Rapamycin Pathway in Women with Breast Carcinoma

Abstract

Abstract Background: A desired target for cancer therapy is a cancer-specific metabolism which is associated with innate or acquired therapeutic resistance, malignancies, and aggressive cancer growth. Nevertheless, these cells utilize manifold metabolic routes to prolong their mass explosion. Human hexokinase 2 (HK2), phosphofructokinase, muscle (PFKM), pyruvate kinase M2 (PKM2), and lactate dehydrogenase A (LDHA) are fundamental signature players of cancer glycolysis playing a role in cancer cell regulation. Reflecting their metabolic roles may be possible with a better grasp of the metabolism transition in the early onset and spread of cancer. This study was designed to assess the serum protein levels of HK2, PFKM, PKM2, and LDHA in women with breast carcinoma and its correlation with phosphatidylinositol-3-kinase (PI3K)/Akt and the mammalian target of rapamycin (mTOR) pathway. Methods: In the current research, case–control investigation was undertaken with breast cancer women (n = 30) and compatible healthy women (n = 30) visiting Justice K. S. Hegde Charitable Hospital, Deralakatte, Mangaluru, who were selected on the basis of inclusion and exclusion criteria. Baseline characteristics for the study population were marked down. The HK2, PFKM, PKM2, and LDHA levels within serum were estimated by means of sandwich enzyme-linked immunosorbent assay. Results: We observed a difference that was significant among the two groups with regard to age and postmenopausal status and also a difference in first-degree family history. The levels of PKM2 and key glycolytic enzymes in serum varied between the case and control groups. There was a positive correlation that was observed in breast carcinoma subjects with glycolytic proteins and signaling pathway (PI3K/Akt/mTOR). Conclusions: Nevertheless, assured processes that persuade the target enzymes remain vague and require further in-depth exploration. Overall, discovering anticancer therapeutics that target glycolytic enzymes involved in glucose metabolism remains a dilemma.