Pyruvate carboxylase (PC) is a mitochondrial enzyme catalyzing the ATP-dependent reaction of pyruvate prolongation with bicarbonate ion to oxaloacetate. The synthesis of oxaloacetate by PC, an intermediate of the Krebs cycle, is recently recognized as a significant anaplerotic reaction that supports the biosynthetic capability, growth, aggressiveness, and even viability of several cancer cell types. PC expression was confirmed in several types of cancer cells and tumors. To evaluate the possibility that prostate tumor-forming cells are also exploiting the anaplerotic role of PC, we applied immunoblotting analysis to estimate its presence. Our results revealed that PC is present among the lysate proteins derived from prostate cancer and benign prostatic hyperplasia samples. The expression of PC in cells of prostate tumors and benign prostatic hyperplasia supposes that PC could facilitate the formation of oxaloacetate in situ and enhance the autonomy of their biosynthetic metabolism from the availability of extracellular substrates by increasing the cellular anaplerotic capability (Tab. 1, Fig. 1, Ref. 30). Keywords: pyruvate carboxylase, prostate cancer, cancer metabolism, anaplerosis.