Anne McArdle

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Anne McArdle
Alma mater University of Liverpool
Scientific career
Institutions University of Liverpool
Thesis Mechanisms skeletal muscle damage in the dystrophin-deficient MDX mouse  (1993)
Website www.liverpool.ac.uk/ageing-and-chronic-disease/staff/anne-mcardle/

Anne McArdle is a physiologist at the University of Liverpool. [1]

Contents

Education

McArdle graduated with a Bachelor's in Biochemistry from the University of Liverpool in 1988 and completed her PhD [2] studying muscle damage using the mdx mouse model of Duchenne muscular dystrophy. [1]

Career and research

McArdle undertook postdoctoral training at the University of Michigan in the laboratories of John Faulkner and was awarded a Research into Ageing Fellowship in 1998 working on sarcopenia. She was appointed as Professor at the University of Liverpool in 2007 and has served as Head of the Department of musculoskeletal biology.

Related Research Articles

Glycogen storage disease type V Human disease caused by deficiency of a muscle enzyme

Glycogen storage disease type V, also known as McArdle's disease, is a metabolic disorder, more specifically a muscle glycogen storage disease, caused by a deficiency of myophosphorylase. Its incidence is reported as one in 100,000, roughly the same as glycogen storage disease type I.

Rhabdomyolysis Human disease (condition) in which damaged skeletal muscle breaks down rapidly

Rhabdomyolysis is a condition in which damaged skeletal muscle breaks down rapidly. Symptoms may include muscle pains, weakness, vomiting, and confusion. There may be tea-colored urine or an irregular heartbeat. Some of the muscle breakdown products, such as the protein myoglobin, are harmful to the kidneys and may lead to kidney failure.

Trochlear nerve

The trochlear nerve, also called the fourth cranial nerve or CN IV, is a motor nerve that innervates just one muscle: the superior oblique muscle of the eye, which operates through the pulley-like trochlea.

Dystrophin Rod-shaped cytoplasmic protein

Dystrophin is a rod-shaped cytoplasmic protein, and a vital part of a protein complex that connects the cytoskeleton of a muscle fiber to the surrounding extracellular matrix through the cell membrane. This complex is variously known as the costamere or the dystrophin-associated protein complex (DAPC). Many muscle proteins, such as α-dystrobrevin, syncoilin, synemin, sarcoglycan, dystroglycan, and sarcospan, colocalize with dystrophin at the costamere. It has a molecular weight of 427 kDa

Phosphorylase Enzymes which catalyze the addition of phosphate groups to molecules

In biochemistry, phosphorylases are enzymes that catalyze the addition of a phosphate group from an inorganic phosphate (phosphate+hydrogen) to an acceptor.

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Myoglobinuria Medical condition

Myoglobinuria is the presence of myoglobin in the urine, which usually results from rhabdomyolysis or muscle injury. Myoglobin is present in muscle cells as a reserve of oxygen.

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Myophosphorylase Muscle enzyme involved in glycogen breakdown

Myophosphorylase or glycogen phosphorylase, muscle associated (PYGM) is the muscle isoform of the enzyme glycogen phosphorylase and is encoded by the PYGM gene. This enzyme helps break down glycogen into glucose-1-phosphate, so it can be used within the muscle cell. Mutations in this gene are associated with McArdle disease, a glycogen storage disease of muscle.

McArdle Laboratory

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The mdx mouse is a popular model for studying Duchenne muscular dystrophy (DMD). The mdx mouse has a point mutation in its DMD gene, changing the amino acid coding for a glutamine to STOP codon. This causes the muscle cells to produce a small, nonfunctional dystrophin protein. As a result, the mouse has a mild form of DMD where there is increased muscle damage and weakness.

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References

  1. 1 2 Wray, Susan; Tansey, Elizabeth, eds. (2015). Women phsysiologists : centenary celebrations and beyond (PDF). London: The Physiological Society. ISBN   9780993341007. OCLC   922032986.
  2. McArdle, Anne. (1993). Mechanisms skeletal muscle damage in the dystrophin-deficient MDX mouse (PhD thesis). University of Liverpool. OCLC   53496566. EThOS   uk.bl.ethos.385144.