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New knowledge about muscular dystrophy
Date:5/5/2014

The most common form of muscular dystrophy among adults is dystrophia myotonica type 1 (DM1), where approximately 1 in every 8000 is affected by the disease. The severity of the disease varies from mild forms to severe congenital forms. It is dominantly inherited and accumulates through generations, gaining increased severity and lowered age of onset. DM1 is characterised by accumulating toxic aggregates of ribonucleic acids (RNA) from a specific mutated gene (see figure 1).

When this RNA, which contains thousands of CUG nucleotide repeats, builds up in the cell, it attracts several cellular proteins, including muscleblind 1 (MBNL1) (see figure 2, left). This binding inhibits the normal function of MBNL1, which means that the cellular level of a number of specific proteins becomes deregulated and the disease develops.

Enzyme characterisation in muscular dystrophy patients

The researchers work at the Department of Molecular Biology and Genetics and the Department of Biomedicine, Aarhus University, where they characterised an enzyme called DDX6, found in both normal cells and cells from muscular dystrophy patients.

The enzyme constantly tries to disperse the toxic aggregates and release MBNL1 in cells from muscular dystrophy patients, which means that the protein can carry out its normal function (see figure 2, right). The enzyme is found in many different cell types, where it performs a number of vital functions. The researchers showed that an artificial increase in the level of DDX6 in muscular dystrophy cells reduces the number of RNA aggregates, while more are formed when DDX6 is removed from the cells.

DDX6 belongs to a class of enzymes called helicases, which can change RNA structure and also regulate the ability of proteins to bind RNA. By purifying DDX6 from human cells, the researchers succeeded in getting the enzyme to bind and carry out an enzymatic reaction outside the cell, thus changing the struct
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Contact: Christian K. Damgaard
cd@mb.au.dk
45-29-70-05-99
Aarhus University
Source:Eurekalert  

Page: 1 2

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