We conclude that deregulation of Microcephalin and ASPM expression is significantly associated with tumourigenesis. The results from this study warrant the further investigation of Microcephalin and ASPM as potential biomarkers in EOC. Vast numbers of enzyme-catalysed biochemical transformations are dependent on cofactors, which are non-protein, chemical compounds that associate with enzymes and assist their biological activity. Coenzyme A is an essential and ubiquitous cofactor made from pantothenate, ATP, and cysteine. CoA acts as a carrier of acyl groups and transports biologically active carboxylic acids, including small organic acids and fatty acids, between different enzymatic reactions in the form of CoA thioesters. CoA thioesters are important intermediates and precursors in numerous metabolic pathways, including oxidation of glucose and fatty acids and biosynthesis of lipids. Acetyl CoA is a CoA thioester which is centrally placed at a junction of multiple catabolic and anabolic pathways. Mitochondrial acetyl CoA, derived from catabolism of glucose and beta-oxidation of fatty acids, can be further oxidised in the citric acid cycle for energy production, while cytosolic acetyl CoA is a precursor for lipid and cholesterol biosynthesis. Additionally, both mitochondrial and nucleocytoplasmic acetyl CoA serve as co-substrates for protein acetylation reactions, linking cellular metabolism to protein posttranslational modifications. Cellular levels of CoA and CoA thiosters are not constant and fluctuate significantly under conditions such as fasting/feeding, in response to nutrients and hormones and during energetic stress and cell growth. Such changes in CoA metabolites not only reflect a shift in the metabolic activity of a cell in response to different intracellular and extracellular stimuli, but can themselves act as a signal for regulating cellular processes. Notably, recent accumulating evidence suggests that cellular levels of acetyl CoA can directly influence cell growth, cell cycle, differentiation and apoptosis by affecting protein acetylation reactions and epigenetic modifications. Three forms of protein acetylation have been identified to date: O-linked, Ne-linked, and Na-linked acetylation. In all three types of acetylation reactions acetyl CoA donates the acetyl group to the acceptor protein, releasing free CoA. Ne-linked acetylation of histones and transcription factors has been recognised for many years as a post-translation modification important for regulation of gene transcription. It is generally accepted that this type of acetylation is dynamically regulated by a balance between histone acetyl transferases and histone deacetylases, which themselves are regulated by gene expression and posttranslational modifications, such as phosphorylation and acetylation. However, a number of recent studies have suggested that the level or availability of acetyl CoA.