Abstract
A phospholipase A2 (PLA2) enzyme degrades glycerophospholipids to release lysophospholipids and fatty acids. The expression of PLA2 has been observed in breast, ovarian, and prostate cancers, and it reduces cell proliferation and mortality in vitro in cancer cells. Therefore, PLA2 may be a novel target for chemotherapy. Despite this, the 19 enzymes in the PLA2 family are heterogeneous. There are various subfamilies within the phospholipase A2 (PLA2) superfamily, such as cytosolic (cPLA2), calcium-independent (iPLA2), secretory (sPLA2), lysosomal (sPLA2), platelet-activating factor (PAF) acetyl hydrolases (aPLA), and adipocyte-specific (aPLA2). Depending on where in the cell they are located and in which tissues they are expressed, different PLA2s can select for phospholipids in different ways. Most malignancies are characterized by high levels of expression and activation of PLA2s, which are downstream regulators of the arachidonic acid cascade. Therefore, they can be biomarkers for cancer detection and potential drug targets. The comprehensive data presented in this chapter may help us understand how PLA2s affect cancer. This may lead to the development of more effective methods and medications to prevent and treat tumors. However, there is still a lack of understanding regarding the role that specific sPLA2 isoforms play in these tumors and their role in other cancer types. Following that, we will discuss innovative technologies that can provide insight into how specific PLA2 enzymes function in lung cancer. In addition, we will discuss drugs that can be used to treat inflammation and lipid metabolism, such as small molecule inhibitors and traditional Chinese medicines.
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