Sentences with phrase «built.without dystrophin»

The inherited condition, most common in boys, results from a lack of dystrophin, a protein that's essential for healthy muscles.

As it turned out, viruses were too small to carry that gene, so Sweeney began searching for a smaller gene that would at least mimic dystrophin.

Children with muscular dystrophy lack the gene required to regulate dystrophin, a protein for muscle growth and stability.

Duchenne muscular dystrophy is caused by problems with the body's ability to produce dystrophin, a long protein chain that binds the interior of a muscle fiber to its surrounding support structure.

Gersbach and his team first delivered the therapy directly to a leg muscle in an adult mouse, resulting in the restoration of functional dystrophin and an increase in muscle strength.

In the study, researchers worked with a mouse model that has a debilitating mutation on one of the exons of the dystrophin gene.

Without enough dystrophin, muscle cells atrophy, wither, and die.

Sweeney's plan was to introduce the dystrophin gene by hitching it to the DNA of a virus that can transport genes into cells.

There's no way to cram the dystrophin gene into a virus to do traditional replacement gene therapy, but researchers have found that turning on other genes can compensate and bulk up muscles.

Duchenne muscular dystrophy is caused by mutations in a huge gene called dystrophin.

The result was the largest deletion ever observed in the dystrophin gene using CRISPR / Cas9, and the study was the first to create corrected human iPS cells that could directly restore functional muscle tissue affected by Duchenne.

Bottom row: skeletal muscle with restored dystrophin after application of the CRISPR / Cas9 platform.

Dystrophin appears yellow in overlay image.

To test the platform, they obtained skin cells from consenting patients at the Center for Duchenne Muscular Dystrophy, all of whom had mutations that fell within the dystrophin gene hot spot.

Once the UCLA researchers had produced iPS cells that were free from Duchenne mutations, they differentiated the iPS cells into cardiac muscle and skeletal muscle cells and then transplanted the skeletal muscle cells into mice that had a genetic mutation in the dystrophin gene.

Duchenne mutations cause abnormally low production of the dystrophin protein, which in turn causes muscles to degenerate and become progressively weaker.

They had been working with a worm model of Duchenne muscular dystrophy, a severe form of the disease that strikes young boys and is caused by mutations in the gene that encodes the dystrophin protein.

«We took patient - derived cells that had the most common mutation responsible for Duchenne muscular dystrophy and we corrected them in vitro to restore production of the missing dystrophin protein in the cells.

Like the dystrophin - defective animals, the new mutants couldn't control their muscles when they slithered backward.

Duchenne typically occurs through one mutation in a gene called dystrophin, which makes a protein with the same name.

«CRISPR - Cpf1 gene - editing can be applied to a vast number of mutations in the dystrophin gene.

«This work demonstrates the feasibility of using a single gene editing platform, plus the regenerative power of stem cells to correct genetic mutations and restore dystrophin production for 60 percent of Duchenne patients,» said Pyle, associate professor of microbiology, immunology and molecular genetics and member of the Broad Stem Cell Research Center.

Left to right: skeletal muscle nuclei (blue), skeletal muscle (red), dystrophin (green), Overlay of all three images to the left.

In people without the disease, the dystrophin protein helps strengthen and connect muscle fibers and cells.

Top row: skeletal muscle without dystrophin.

Mice treated with antisense RNA (bottom) produced more dystrophin — colored red in this image — than did control mice (top).

That was enough for the muscle to carry some weight, and one injection produced dystrophin for 3 months, the group reports in the 6 July online Nature Medicine.

Like most genes, the RNA for the dystrophin protein undergoes a process called splicing, in which stretches of so - called «junk» are clipped out.

But that's difficult because the dystrophin gene is enormous and unwieldy.

So Sweeney began searching for a smaller gene that would fit inside a virus and at least mimic dystrophin.

It's important to remember that we're not going after the primary cause of the disease, dystrophin deficiency.»

Patients suffering from Duchenne muscular dystrophy are unable to produce dystrophin.

In normal mice, stem cells (pink) express dystrophin (green) and are able to easily generate new muscle fibers, but in the disease model, there is no dystrophin and the stem cells lose their sense of direction and have trouble generating new muscle fibers.

For many years, dystrophin was thought to be a simple structural protein only found in muscle fibres.

«Muscle stem cells that lack dystrophin can not tell which way is up and which way is down,» said Dr. Rudnicki.

In the current study, Dr. Rudnicki and his team discovered that muscle stem cells also express the dystrophin protein, and without this protein, they produce ten-fold fewer muscle precursor cells, which in - turn generate fewer functional muscle fibres.

Researchers at the University of Michigan Health System have identified a new way of triggering the role of the muscle protein dystrophin, which is found in the muscles used for movement and in cardiac muscle cells.

Using isolated heart cells from dystrophin - deficient mice, the team of Dan Michele, Ph.D., and Joanne Garbincius, of the University of Michigan Department of Molecular & Integrative Physiology, found an explanation for this debilitating protein malfunction — and a potential way to bypass it.

«Our work suggests that AMPK signaling may be one of the links between the loss of dystrophin and the impaired nNOS function that is seen in muscular dystrophy,» says Michele, senior study author and professor of molecular & integrative physiology and internal medicine at the University of Michigan.

Experiments have shown treatment with sildenafil significantly improved heart function in mice missing the dystrophin protein.

Unlike skeletal muscle, where nNOS physically binds to the dystrophin, nNOS does not directly bind to dystrophin.

Lack of dystrophin makes the muscle cell plasma membrane more vulnerable to injury.

This balance can be disrupted in diseases such as Duchenne muscular dystrophy, which is caused by the lack of a muscle - specific protein, dystrophin.

Their study published online ahead of print in PNAS Early Edition suggests a new therapeutic strategy for patients with Duchene muscular dystrophy, a progressive neuromuscular condition, caused by a lack of dystrophin, that usually leaves patients unable to walk on their own by age 10 - 15.

Manipulating proteins in the body to compensate for the lack of dystrophin is one of many strategies being investigated to halt or reverse the muscle damage caused by DMD.

«AMPK normally helps to turn on nNOS function in muscle cells, for instance when we exercise, and when dystrophin is lost, AMPK does not turn on appropriately.»

Pictured are isolated adult mouse cardiomyocytes labeled for dystrophin (red), neuronal nitric oxide synthase (nNOS)(green), and nuclei (blue).

DMD is a rare disease affecting primarily boys and is caused by defects in the gene that makes the dystrophin protein.

Normally, the dystrophin protein helps strengthen muscle fibers.

These splice sites instruct the genetic machinery to build abnormal dystrophin molecules, but once the gene is successfully edited it expresses a much - improved dystrophin protein product, enhancing the function of the muscle tissue.