UQ Diamantina Institute researcher Dr Pascal Duijf said the discovery could be the foundation for improved cancer diagnosis, new treatments and better assessment of a patient’s prognosis.

“My team has discovered excessively high levels of the protein EMI1 in cancer samples, including the aggressive brain cancer glioblastoma and tumours of the bone,” Dr Duijf said.

“High levels of EMI1 promote tumour development, increase the tendency of cancer cells to spread, and change immune responses, which fuel cancer progression,”

“This is associated with poor patient prognosis, particularly in breast cancer.”

Dr Duijf, a National Breast Cancer Foundation Career Development Fellow, said high levels of EMI1 disrupted normal cell division leading to new cells with abnormal chromosome numbers.

“This process, referred to as chromosome instability, accelerates cancer progression and allows cancer cells to become resistant to cancer therapies.”

“Our findings indicate that high EMI1 levels are one of the strongest indicators of chromosome instability identified to date.”

Dr Duijf said the discovery was an exciting step forward. The next step was to determine whether tumours had to maintain high levels of EMI1 to survive.

“If that is the case, it could present a promising anti-cancer target,” he said.

The study is published in the Nature journal Oncogene.

Explore further: Breast cancer prognosis associated with oncometabolite accumulation

More information: S Vaidyanathan et al. In vivo overexpression of Emi1 promotes chromosome instability and tumorigenesis, Oncogene (2016). DOI: 10.1038/onc.2016.94

 

 

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From Wiki:

EMI1 / YDR512C Overview

Emi1 is a mitotic regulator that interacts with Cdc20 and inhibits the anaphase promoting complex.

Emi1 protein accumulation implicates misregulation of the anaphase promoting complex/cyclosome pathway in ovarian clear cell carcinoma.

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Enzymes

Enzymes /ˈɛnzaɪmz/ are macromolecular biological catalysts. Enzymes accelerate, or catalyze, chemical reactions. The molecules at the beginning of the process are called substrates and the enzyme converts these into different molecules, called products. Almost all metabolic processes in the cell need enzymes in order to occur at rates fast enough to sustain life.^[1]:8.1 The set of enzymes made in a cell determines which metabolic pathways occur in that cell. The study of enzymes is called enzymology.

Enzymes are known to catalyze more than 5,000 biochemical reaction types.^[2] Most enzymes are proteins, although a few are catalytic RNA molecules. Enzymes’ specificity comes from their unique three-dimensional structures.

Like all catalysts, enzymes increase the rate of a reaction by lowering its activation energy. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5′-phosphate decarboxylase, which allows a reaction that would otherwise take millions of years to occur in milliseconds.^[3][4] Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, nor do they alter the equilibrium of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. An enzyme’s activity decreases markedly outside its optimal temperature and pH.

Some enzymes are used commercially, for example, in the synthesis of antibiotics. Some household products use enzymes to speed up chemical reactions: enzymes in biological washing powders break down protein, starch or fat stains on clothes, and enzymes in meat tenderizer break down proteins into smaller molecules, making the meat easier to chew.