McArdle Disease

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Continuing Education Activity

McArdle disease is a genetic disorder that mainly affects skeletal muscles. It occurs due to the deficiency or absence of an enzyme called myophosphorylase. Symptoms like painful muscle cramps, weakness, and fatigue manifest during periods of physical activity. To avoid the unpleasant symptoms associated with this condition and improve the quality of life, the disease requires prompt diagnosis and treatment. This activity reviews the evaluation and management of McArdle disease and highlights the role of the interprofessional team in improving the care of patients with this condition.


  • Outline the etiology of McArdle disease.
  • Summarize the appropriate steps in the evaluation of McArdle disease.
  • Describe the treatment options currently available for McArdle disease.
  • Identify and discuss interprofessional team strategies to improve patient care coordination and communication to manage McArdle disease and improve disease outcomes.


McArdle disease, also known as glycogen storage disorder (GSD) type V, is an inborn metabolic disorder characterized by a deficiency or complete absence of an enzyme called muscle glycogen phosphorylase (or myophosphorylase). This disease is inherited in an autosomal recessive pattern and mainly affects skeletal muscles. The enzyme responsible for this disease normally catalyzes reactions that cause the conversion of glycogen to glucose. The deficiency of this enzyme, in turn, results in the accumulation of glycogen in tissues. The clinical sequelae are usually systemic but the defect is limited to particular tissues in some cases. Glycolysis is only partially hindered in McArdle disease, as muscle fibers are able to convert glucose to glucose-6-phosphate (G6P) downstream of the metabolic block.[1]

Most GSDs present in childhood, however, McArdle disease is one of those that have adult-onset forms as well. Unfortunately, there have not been any established treatment options although diet therapy has been observed to be efficacious in reducing clinical manifestations. In some patients, a liver transplant becomes a viable option. 

McArdle disease was first reported in 1951 by Dr. Brian McArdle from London.[2] In 1959, it was described that the enzyme responsible for the affected step was myophosphorylase.[3][4] The underlying gene for myophosphorylase (PYGM) was first discovered in 1984.[5]


McArdle disease typically results from mutations involving the muscle-specific isoform of the glycogen phosphorylase enzyme (abbreviated as PGYM). This enzyme plays a key role in the first step of glycogenolysis that releases glucose-1-phosphate monomers in muscle fibers. As a result, the carbohydrate metabolism of the skeletal muscle is affected, and energy cannot be generated from the glycogen stores of muscles. The genetic mutations of the PYGM gene on 11q13 make the enzyme inactive.[6] Exons 1 and 17 particularly exhibit mutation hotspots, and half of the cases are nonsense mutations. The commonest mutation in White individuals is described as p.Arg50Stop or R50X.[7][8]

From the study of the genetics of McArdle disease, 179 variants have been identified that together affect the PYGM gene. Missense mutations have been found to be the commonest variants in European and US White populations (around 60% of all mutations). It has been reported that the majority of the patients do not have myophosphorylase, regardless of the type of mutation, such as missense, nonsense, insertion, deletion, and splicing.[9] This indicates the absence of myophosphorylase activity when there is a PYGM mutation, except for those rare cases where missense mutations result in preserved myophosphorylase activity and better phenotypes.[10]


The exact prevalence of McArdle disease is not precisely known and appears to range from 1 in 50,000 to 1 in 200,000 in the United States. The variation between the prevalence according to genetic data and the prevalence according to diagnosed cases is attributable to the delay in the making of a diagnosis. One study analyzed gene frequency and next-generation sequencing data to report the true prevalence of the disease among populations. The results of that study revealed that the disease is much more common than previously thought, and has a prevalence of 1 in 7,650 (95% confidence interval (CI) 1/5,362-1/11,108). An additional method used by the same study looked at the two most common mutations and recorded a prevalence of 1 in 42,355.[11][8]

In some areas of the USA, such as the Dallas/Fort Worth area, the prevalence of McArdle disease on the basis of the genetic data is reported to be 1/100000.[12] A study carried out in Spain reported a prevalence of diagnosed cases to be around 1/139543.[13]

In terms of gender, in McArdle disease the following ratios of men to women have been noted:

In terms of age, most McArdle disease cases present in the second or third decade of life. Wolfe et al report a unique precedent of McArdle disease manifesting in a 73 years old patient.[16]Felice and Pourmand also reported late presentations. Providers should consider the diagnosis of McArdle disease regardless of the age of presentation.[17][18]


Myophosphorylase is a key enzyme in the regulation of glucose metabolism in muscles. It detaches 1,4 glycosyl chains from glycogen and attaches inorganic phosphate to form glucose-1-phosphate. During glycogen breakdown, muscle cells generate glucose-1-phosphate in place of glucose, and due to the polar nature of the former molecule, it disintegrates intracellularly.

PYG is activated when phosphorylated by the enzyme phosphorylase kinase. Glucagon and adrenaline initiate the glycogenolysis in the liver, and they bind to G-protein coupled receptors first. The signaling pathway behind this process involves the following steps: GPCRs (G-protein coupled receptors) - AC (adenylate cyclase) – cAMP (cyclic adenosine monophosphate) – PKA (protein kinase A) – PK (phosphorylase kinase) causing PYG activation. In contrast, PYG becomes inactivated when dephosphorylated by a different enzyme called protein phosphatase 1 (PP1).[7]

There are several tissue-specific isoforms of phosphorylase. Myophosphorylase is found in cardiac myocytes and the brain, and it is the only variant present in skeletal muscle. Most patients with McArdle disease lack myophosphorylase activity therefore they are unable to produce energy in the form of glucose by breaking down glycogen stores in muscles.[19]

During aerobic activity, such as walking, jogging, gentle swimming, or cycling the skeletal muscle derives energy from free fatty acids by oxidizing them in the mitochondria via the beta-oxidation pathway to form acetyl-CoA. Acetyl-CoA is further metabolized via the Krebs cycle and the respiratory chain, leading to the production of adenosine triphosphate (ATP). During anaerobic activity, such as weightlifting or sprinting the myophosphorylase of the skeletal muscle breaks down glycogen to glucose, which then enters the glycolytic pathway yielding ATP anaerobically.[20]


To support the diagnosis, muscle tissue is biopsied and examined under a microscope. The hallmark findings suggestive of McArdle disease are glycogen deposits and absence of the enzyme myophosphorylase.[21]

Glycogen deposits appear under the sarcolemmal membrane at the periphery of myofibers. The collection of glycogen between myofibrils makes the myofibers look like vacuoles. The glycogen takes up periodic acid-Schiff (PAS). The absence of glycogen accumulation in muscle biopsy should not be taken as proof for the absence of McArdle disease as the glycogen could be washed out in tissue processing.

Myophosphorylase histochemistry is easier to perform and has a good negative predictive value. Its absence is diagnostic for McArdle disease. However, providers must specifically request the testing of myophosphorylase.

History and Physical

The most frequently reported symptom remains physical activity intolerance. Other symptoms include painful muscle cramps, weakness, and fatigue. Muscle pain and stiffness sometimes can lead to painful contractures. All these symptoms are much pronounced soon after starting activity and alleviated with exercise cessation. In cases of sudden, persistent muscle contraction during high-intensity exercise, severe muscle damage can occur resulting in a massive release of muscle proteins, i.e., creatinine kinase (typical level >1,000 U/l) and myoglobin in blood, as well as myoglobinuria (excretion of myoglobin in urine) presenting as dark-colored urine. In rare instances, acute renal failure and catastrophic hyperkalemia can ensue from an episode of rhabdomyolysis (muscle breakdown).[22]

A unique feature associated with this disorder called the “second-wind phenomenon” is seen in most patients and is characterized by improved symptoms after approximately 10 minutes of gentle aerobic activity.[8]

McArdle disease usually presents in the first or second decade of life. Patients more than 40 years of age complain of weakness and wasting of muscles.[23][24][8][7][21]

Clinical heterogeneity is widely seen in McArdle disease. Some patients present with very mild symptoms, such as tiredness without cramps. On the other hand, progressive weakness ensues in the 6th or 7th decade of life. Contrary to this, fatal infantile McArdle syndrome which is the severe and rapidly progressive form appears shortly after birth.

Seizures have been described in 4% of patients.

Classic McArdle disease presents with the following examination findings:

  • Proximal muscle weakness - most notable following exercise
  • Fixed limb weakness - usually in the proximal muscle groups
  • Muscle wasting

The fatal infantile variant can have the following examination findings:

  • Hypotonia
  • Diminished deep tendon reflexes


Initial assessment in suspected cases is done using a forearm exercise test. As the process of glycogenolysis is defective, no pyruvate and subsequent lactate are produced through normal pathways. Isometric rhythmic exercises are done for one minute and the levels of lactate and ammonia before and after are compared with one another.

During normal circumstances, a three-fold rise in lactate and ammonia occurs, but lactate rise is remarkably low in glycolytic and glycogenolytic disorders. The ischemic test making use of sphygmomanometer cuff is obsolete now, and there is a recent consensus upon the use of non-ischemic forearm exercise tests to avoid unfavorable outcomes like rhabdomyolysis and compartment syndrome.[25] The test has fairly high sensitivity and specificity, therefore a normal test result rules out the possibility of glycolytic/glycogenolytic defect. Nonischemic forearm testing is equally diagnostic with a lesser risk of compartment syndrome. These tests are performed in the same way but with no use of a blood pressure cuff.[26]The nonischemic test has a sensitivity of 100% and a specificity of 100% and 99.7%, respectively, as has been reported by a 2015 retrospective study.[27]

A characteristic feature of McArdle disease is the chronically elevated serum creatine kinase (CK) enzyme levels.

Graded exercise stress is done to demonstrate the second-wind phenomenon, often seen in patients with McArdle disease, and also to distinguish it from disorders of glycolytic pathways.

Muscle biopsy (vastus lateralis or biceps brachialis) shows periodic acid Schiff-positive vacuoles of high glycogen content and absence of myophosphorylase. Genetic testing includes options of specific mutation analysis (most commonly R50X in the White population), and next-generation PYGM gene sequencing panels or myopathy panels or whole-exome sequencing for particular glycogen-storage diseases. Typically patients are diagnosed based on whether they are homozygous or compound heterozygous for PYGM pathogenic mutations. A study aimed to formulate a less invasive approach to diagnose the disease and found out PYGM expression in white blood cells by using antibodies.

Other tests done to support the findings are serum uric acid levels (high in about half of the cases), urinalysis for detecting pigmenturia, and electromyography that often yields normal findings.[8][28][26][6][21]

Treatment / Management

The treatment is mostly geared towards avoiding lifestyle activities that exacerbate the symptoms. Patients may adapt to avoiding physical activity but this may worsen the disease because serum CK rises with loss of aerobic fitness. It may also result in the decreased capacity of muscles to utilize alternate fuels to overcome the block in glycogenolysis. Moreover, there is a marked reduction in the expression of proteins needed for metabolism and calcium hemostasis in non-exercising muscles.

There is evidence proving the beneficial effects of moderate-intensity graded aerobic exercise therapy. Patients reported less significant exercise intolerance and earlier appearance of second wind with this intervention. A balanced weight-lifting approach also lessens the severity of symptoms in some patients.

Howell et al proposed that sodium valproate could cause the up-regulation of the myophosphorylase enzyme. The findings of that study suggested that sodium valproate could be a potential management option for McArdle disease; however, more randomized trials are needed.[29]

It has been noted that creatine may improve ATP storage and exercise tolerability. However, in a trial, high-dose creatine monohydrate resulted in poor exercise tolerance and a significant increase in exercise-induced myalgia. The investigators proposed an explanation that inadequate adaptation to better electromechanical efficacy results in excess muscle contractility during exercise and thus a resultant worsening of symptoms.[30]

Certain dietary interventions which confer favorable effects include taking a sugary meal before planned exercise—for example, having a drink containing 37 g sucrose 5 minutes before exercise reduces initial symptoms of exercise intolerance. A diet rich in carbohydrates results in much better outcomes in comparison to a protein-rich diet. Other nutritional agents that were helpful for some patients but could not yield convincing outcomes during actual experimental studies include branched-chain amino acids, depot glucagon preparations, verapamil, dantrolene sodium, vitamin B6, high dose D-ribose, and high-dose creatine ingestion.[31][24][22][32][8][33]

Differential Diagnosis

It is essential to distinguish McArdle disease from other glycogen storage disorders as well as other diseases inducing myopathy, particularly fatty acid oxidation defects, and mitochondrial myopathies.

McArdle disease demonstrates its symptoms at the very beginning of rigorous physical activity, whereas fatty acid oxidation defects (carnitine palmitoyltransferase II deficiency) and mitochondrial myopathies (Medium-chain acyl-CoA dehydrogenase deficiency) show symptoms much later with a longer duration of the exercise. Moreover, fatty acid oxidation defects manifest their symptoms under stressful states such as fasting, fever, and infections.

A noteworthy phenomenon occurring with McArdle disease is the second wind phenomenon (lesser perception of discomfort), and it does not occur in other conditions mimicking McArdle disease.

Patients with McArdle disease have chronically high serum creatine kinase levels. This enzyme may or may not be elevated in other glycogen storage diseases, fatty acid oxidation defects, and mitochondrial myopathies.

In general, a carbohydrate-rich meal before exercise decreases the symptom severity in McArdle disease and fatty acid oxidation defects but does not prove helpful in mitochondrial myopathies and worsens symptoms in the glycolytic pathway disorder.

Muscle biopsy and genetic testing further delineate the difference between the disorders mentioned above. On biopsy, McArdle disease shows high glycogen content, carnitine palmitoyltransferase II deficiency shows increased lipids, and a mitochondrial myopathy shows ragged red fibers and cytochrome oxidase negative fibers. Specific mutation analysis reveals the most common mutations to be R50X, S113L, and m.3243A>G in McArdle disease, fatty acid oxidation disorders, and mitochondrial defects, respectively.[21]


Most of the patients affected with McArdle disease lead a normal life, and it does not affect life expectancy. Rhabdomyolysis is to be avoided as it can lead to acute renal failure which may potentially become life-threatening. Patients exploit the second wind phenomenon and adjust to the disease itself. Only a minority of patients have known to experience progressive worsening of symptoms with advancing age and wasting, especially over the shoulder girdle and back muscles.[24]

More recent studies report heterogeneity in the clinical severity, such as 8% of patients are asymptomatic in daily life and 21% show limitations in the activities of daily living and fixed muscle weakness.[13]The evidence also reiterates acquiring an active lifestyle, which is critical in patients with McArdle disease.[13]

It has also been reported in various studies that the disease does not adversely alter the course of pregnancy or childbirth.[22]


Rhabdomyolysis is an established complication of McArdle disease.[34] Acute renal failure may result from myoglobinuria after vigorous exercise. As with any patient having rhabdomyolysis, the patients with McArdle disease should be monitored for the possible complications of electrolyte abnormalities, compartment syndrome, and metabolic encephalopathy.[35]


In McArdle disease, rhabdomyolysis may be followed by acute renal failure, necessitating consultation with a renal physician. Renal function should be monitored in all McArdle disease cases.

Deterrence and Patient Education

Upon diagnosis of the condition, it is essential to refer the patient to a clinical geneticist/genetic counselor. Annual surveillance includes routine physical examination and diet checks. Counseling consists of avoiding certain exercises, e.g., sustained hand grips exercises, weight lifting unless under specialists supervision, competitive ball games, running, exercises involving excessive jumping, strenuous swimming, and cycling.[23][13][8][24]

Limitation or adaptation of physical activity to avoid symptoms is necessary as rhabdomyolysis is a life-threatening condition.

There is a mild risk of acute muscle necrosis secondary to certain general anesthetics, such as muscle relaxants and inhaled anesthetic agents. This should be taken care of while treating patients with McArdle disease to avoid rhabdomyolysis.[36]

Enhancing Healthcare Team Outcomes

GSD type V is an autosomal recessive disease, and patients should be made aware of its inheritance pattern and risk in future generations. Homozygous persons are symptomatic, while heterozygous individuals carry affected genes and transmit them to their offspring.

A consultation with a genetic specialist is critical in such circumstances. Optional genetic testing could be offered to the relatives (particularly siblings) of an affected individual. The autosomal recessive inheritance means that the parents are the carriers of the disease and have mild symptoms to no symptoms at all. Each sibling carries a 1 in 4 chance of being affected, a 1 in 2 chance of being a carrier, and a 1 in 4 chance of being unaffected and non-carrier.

Appropriate family planning is necessary for affected individuals, carriers, or individuals at high risk of being carriers. All available options require collaborative exploration with the patient, including information about prenatal testing and preimplantation genetic testing before becoming pregnant.[23]

Article Details

Article Author

Zoia E. Khattak

Article Editor:

Muddasir Ashraf


5/22/2022 11:36:16 PM

PubMed Link:

McArdle Disease



Santalla A,Nogales-Gadea G,Ørtenblad N,Brull A,de Luna N,Pinós T,Lucia A, McArdle disease: a unique study model in sports medicine. Sports medicine (Auckland, N.Z.). 2014 Nov     [PubMed PMID: 25028051]


McARDLE B, Myopathy due to a defect in muscle glycogen breakdown. Clinical science. 1951 Feb     [PubMed PMID: 24540673]


Mommaerts WF,Illingworth B,Pearson CM,Guillory RJ,Seraydarian K, A FUNCTIONAL DISORDER OF MUSCLE ASSOCIATED WITH THE ABSENCE OF PHOSPHORYLASE. Proceedings of the National Academy of Sciences of the United States of America. 1959 Jun     [PubMed PMID: 16590445]


SCHMID R,MAHLER R, Chronic progressive myopathy with myoglobinuria: demonstration of a glycogenolytic defect in the muscle. The Journal of clinical investigation. 1959 Nov     [PubMed PMID: 14442994]


Lebo RV,Gorin F,Fletterick RJ,Kao FT,Cheung MC,Bruce BD,Kan YW, High-resolution chromosome sorting and DNA spot-blot analysis assign McArdle's syndrome to chromosome 11. Science (New York, N.Y.). 1984 Jul 6     [PubMed PMID: 6587566]


de Luna N,Brull A,Lucia A,Santalla A,Garatachea N,Martí R,Andreu AL,Pinós T, PYGM expression analysis in white blood cells: a complementary tool for diagnosing McArdle disease? Neuromuscular disorders : NMD. 2014 Dec;     [PubMed PMID: 25240406]


Llavero F,Arrazola Sastre A,Luque Montoro M,Gálvez P,Lacerda HM,Parada LA,Zugaza JL, McArdle Disease: New Insights into Its Underlying Molecular Mechanisms. International journal of molecular sciences. 2019 Nov 25;     [PubMed PMID: 31775340]


Nogales-Gadea G,Godfrey R,Santalla A,Coll-Cantí J,Pintos-Morell G,Pinós T,Arenas J,Martín MA,Lucia A, Genes and exercise intolerance: insights from McArdle disease. Physiological genomics. 2016 Feb;     [PubMed PMID: 26465709]


García-Consuegra I,Asensio-Peña S,Ballester-Lopez A,Francisco-Velilla R,Pinos T,Pintos-Morell G,Coll-Cantí J,González-Quintana A,Andreu AL,Arenas J,Lucia A,Nogales-Gadea G,Martín MA, Missense mutations have unexpected consequences: The McArdle disease paradigm. Human mutation. 2018 Oct     [PubMed PMID: 30011114]


Vissing J,Duno M,Schwartz M,Haller RG, Splice mutations preserve myophosphorylase activity that ameliorates the phenotype in McArdle disease. Brain : a journal of neurology. 2009 Jun     [PubMed PMID: 19433441]


De Castro M,Johnston J,Biesecker L, Determining the prevalence of McArdle disease from gene frequency by analysis of next-generation sequencing data. Genetics in medicine : official journal of the American College of Medical Genetics. 2015 Dec;     [PubMed PMID: 25741863]


Haller RG, Treatment of McArdle disease. Archives of neurology. 2000 Jul     [PubMed PMID: 10891971]


Santalla A,Nogales-Gadea G,Encinar AB,Vieitez I,González-Quintana A,Serrano-Lorenzo P,Consuegra IG,Asensio S,Ballester-Lopez A,Pintos-Morell G,Coll-Cantí J,Pareja-Galeano H,Díez-Bermejo J,Pérez M,Andreu AL,Pinós T,Arenas J,Martín MA,Lucia A, Genotypic and phenotypic features of all Spanish patients with McArdle disease: a 2016 update. BMC genomics. 2017 Nov 14;     [PubMed PMID: 29143597]


Bruno C,Cassandrini D,Martinuzzi A,Toscano A,Moggio M,Morandi L,Servidei S,Mongini T,Angelini C,Musumeci O,Comi GP,Lamperti C,Filosto M,Zara F,Minetti C, McArdle disease: the mutation spectrum of PYGM in a large Italian cohort. Human mutation. 2006 Jul;     [PubMed PMID: 16786513]


Quinlivan R,Buckley J,James M,Twist A,Ball S,Duno M,Vissing J,Bruno C,Cassandrini D,Roberts M,Winer J,Rose M,Sewry C, McArdle disease: a clinical review. Journal of neurology, neurosurgery, and psychiatry. 2010 Nov     [PubMed PMID: 20861058]


Wolfe GI,Baker NS,Haller RG,Burns DK,Barohn RJ, McArdle's disease presenting with asymmetric, late-onset arm weakness. Muscle & nerve. 2000 Apr     [PubMed PMID: 10716777]


Felice KJ,Schneebaum AB,Jones HR Jr, McArdle's disease with late-onset symptoms: case report and review of the literature. Journal of neurology, neurosurgery, and psychiatry. 1992 May     [PubMed PMID: 1602316]


Pourmand R,Sanders DB,Corwin HM, Late-onset Mcardle's disease with unusual electromyographic findings. Archives of neurology. 1983 Jun;     [PubMed PMID: 6573876]


Dimaur S,Andreu AL,Bruno C,Hadjigeorgiou GM, Myophosphorylase deficiency (glycogenosis type V; McArdle disease). Current molecular medicine. 2002 Mar     [PubMed PMID: 11949935]


Godfrey R,Quinlivan R, Skeletal muscle disorders of glycogenolysis and glycolysis. Nature reviews. Neurology. 2016 Jul     [PubMed PMID: 27231184]


Tarnopolsky MA, Metabolic Myopathies. Continuum (Minneapolis, Minn.). 2016 Dec;     [PubMed PMID: 27922496]


Lucia A,Ruiz JR,Santalla A,Nogales-Gadea G,Rubio JC,García-Consuegra I,Cabello A,Pérez M,Teijeira S,Vieitez I,Navarro C,Arenas J,Martin MA,Andreu AL, Genotypic and phenotypic features of McArdle disease: insights from the Spanish national registry. Journal of neurology, neurosurgery, and psychiatry. 2012 Mar;     [PubMed PMID: 22250184]


Martín MA,Lucia A,Arenas J,Andreu AL, Glycogen Storage Disease Type V 1993;     [PubMed PMID: 20301518]


Quinlivan R,Martinuzzi A,Schoser B, Pharmacological and nutritional treatment for McArdle disease (Glycogen Storage Disease type V). The Cochrane database of systematic reviews. 2014 Nov 12;     [PubMed PMID: 25391139]


Lucia A,Nogales-Gadea G,Pérez M,Martín MA,Andreu AL,Arenas J, McArdle disease: what do neurologists need to know? Nature clinical practice. Neurology. 2008 Oct     [PubMed PMID: 18833216]


Kazemi-Esfarjani P,Skomorowska E,Jensen TD,Haller RG,Vissing J, A nonischemic forearm exercise test for McArdle disease. Annals of neurology. 2002 Aug;     [PubMed PMID: 12210784]


Hogrel JY,van den Bogaart F,Ledoux I,Ollivier G,Petit F,Koujah N,Béhin A,Stojkovic T,Eymard B,Voermans N,Laforêt P, Diagnostic power of the non-ischaemic forearm exercise test in detecting glycogenosis type V. European journal of neurology. 2015 Jun     [PubMed PMID: 25740218]


Hanisch F,Eger K,Bork S,Lehnich H,Deschauer M,Zierz S, Lactate production upon short-term non-ischemic forearm exercise in mitochondrial disorders and other myopathies. Journal of neurology. 2006 Jun;     [PubMed PMID: 16619130]


Howell JM,Dunton E,Creed KE,Quinlivan R,Sewry C, Investigating sodium valproate as a treatment for McArdle disease in sheep. Neuromuscular disorders : NMD. 2015 Feb     [PubMed PMID: 25455802]


Vorgerd M,Zange J,Kley R,Grehl T,Hüsing A,Jäger M,Müller K,Schröder R,Mortier W,Fabian K,Malin JP,Luttmann A, Effect of high-dose creatine therapy on symptoms of exercise intolerance in McArdle disease: double-blind, placebo-controlled crossover study. Archives of neurology. 2002 Jan     [PubMed PMID: 11790236]


Andersen ST,Vissing J, Carbohydrate- and protein-rich diets in McArdle disease: effects on exercise capacity. Journal of neurology, neurosurgery, and psychiatry. 2008 Dec;     [PubMed PMID: 19010947]


Nogales-Gadea G,Consuegra-García I,Rubio JC,Arenas J,Cuadros M,Camara Y,Torres-Torronteras J,Fiuza-Luces C,Lucia A,Martín MA,García-Arumí E,Andreu AL, A transcriptomic approach to search for novel phenotypic regulators in McArdle disease. PloS one. 2012;     [PubMed PMID: 22347505]


Santalla A,Munguía-Izquierdo D,Brea-Alejo L,Pagola-Aldazábal I,Díez-Bermejo J,Fleck SJ,Ara I,Lucia A, Feasibility of resistance training in adult McArdle patients: clinical outcomes and muscle strength and mass benefits. Frontiers in aging neuroscience. 2014;     [PubMed PMID: 25566067]


Satoh A,Hirashio S,Arima T,Yamada Y,Irifuku T,Ishibashi H,Motoda A,Sueda Y,Masaki T, Novel Asp511Thr mutation in McArdle disease with acute kidney injury caused by rhabdomyolysis. CEN case reports. 2019 Aug     [PubMed PMID: 30900170]


Mull AB,Wagner JI,Myckatyn TM,Kells AF, Recurrent Compartment Syndrome Leading to the Diagnosis of McArdle Disease: Case Report. The Journal of hand surgery. 2015 Dec     [PubMed PMID: 26612634]


Bollig G, McArdle's disease (glycogen storage disease type V) and anesthesia--a case report and review of the literature. Paediatric anaesthesia. 2013 Sep     [PubMed PMID: 23565573]