Medicine:Glycogen storage disease type V

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Short description: Human disease caused by deficiency of a muscle enzyme
Glycogen storage disease type V
Other namesMcArdle disease, muscle glycogen phosphorylase (myophosphorylase) deficiency
Vacuolar myopathy mcArdle type V glcogenosis.jpg
Muscle biopsy specimen showing vacuolar myopathy: The patient had a type V glycogenosis (McArdle disease)
SpecialtyNeuromuscular medicine
SymptomsExercise intolerance, inappropriate rapid heart rate response to exercise, exaggerated cardiorespiratory response to exercise, exercise-induced premature muscle fatigue and cramping, second wind phenomenon
ComplicationsPoor physical or mental health due to prolonged delay in diagnosis, misdiagnosis, or having been given inappropriate exercise advice. Rare complications include rhabdomyolysis with myoglobinuria requiring hospitalization, transient muscle contracture, and compartment syndrome.
Usual onsetChildhood-onset (median age of symptom onset 3 years)
CausesPathogenic autosomal recessive mutations in PYGM gene coding for myophosphorylase
Diagnostic methodGenetic testing (preferred), muscle biopsy. Supplemental tests: blood tests, exercise stress test, 12-Minute Walk Test, non-ischemic forearm test, EMG

Glycogen storage disease type V (GSD5, GSD-V),[1] also known as McArdle's disease,[2] is a metabolic disorder, one of the metabolic myopathies, more specifically a muscle glycogen storage disease, caused by a deficiency of myophosphorylase.[3][4] Its incidence is reported as one in 100,000, roughly the same as glycogen storage disease type I.[2]

The disease was first reported in 1951 by Dr. Brian McArdle of Guy's Hospital, London.[5]

Signs and symptoms

Onset of symptoms and diagnostic delay

The onset of this disease is usually noticed in childhood,[6][7][8] but often not diagnosed until the third or fourth decade of life, frequently due to misdiagnosis and dismissal of symptoms.[6][8] The median age of symptom onset is 3 years, with the median diagnostic delay being 29 years.[8] Misdiagnosis is overwhelmingly common, with approximately 90% of patients being misdiagnosed, and approximately 62% receiving multiple misdiagnoses before a correct diagnosis.[8] The prolonged diagnostic delay, misdiagnosis or multiple misdiagnoses, or being given inappropriate exercise advice (such as ignore pain or avoid exercise) severely impacts quality of life (QoL), physically and mentally.[6][8]

There is, however, a very rare adult-onset, limb–girdle phenotype that presents late in life (70+ years of age) due to recessive homozygous PYGM mutations resulting in severe upper and lower limb atrophy, with the possibility of ptosis (drooping eyelids) and camptocormia (stooped posture).[9]

Common signs and symptoms

The most prominent symptom is that of exercise intolerance which includes:

  • premature muscle fatigue (particularly for anaerobic activity and high-intensity aerobic activity, which may be described as inability to keep up with peers or reduced stamina);
  • exercise-induced painful cramps;
  • inappropriate rapid heart rate response to exercise;
  • exaggerated cardiorespiratory response to exercise (heavy or rapid breathing with inapprop. rapid HR);
  • second wind phenomenon (muscle fatigue and heart rate improves for aerobic activity after approximately 6–10 minutes).[2][10][11]

Heart rate during exercise is a key indicator as, unlike the symptoms of muscle fatigue and cramping, it is a medical sign (meaning that it is observable and measurable by a third party rather than felt subjectively by the patient). In regularly active individuals with McArdle disease, they may not feel the usual symptoms of muscle fatigue and cramping until they increase their speed to very brisk walking, jogging or cycling; however, they will still show an inappropriate rapid heart rate response to exercise, with a declining heart rate once second wind has been achieved.[12][13][14]

"In McArdle's, our heart rate tends to increase in what is called an 'inappropriate' response. That is, after the start of exercise it increases much more quickly than would be expected in someone unaffected by McArdle's."[11]

Other symptoms and comorbidities

Myoglobinuria (reddish-brown urine) may be seen due to the breakdown of skeletal muscle known as rhabdomyolysis (a condition in which muscle cells breakdown, sending their contents into the bloodstream).[15] In 2020, the largest study to-date of 269 GSD-V patients, 39.4% reported no previous episodes of myoglobinuria and 6.8% had normal CK (including those with fixed muscle weakness); so an absence of myoglobinuria and normal CK should not rule out the possibility of the disease.[16] Between 33-51.4% develop fixed muscle weakness, typically of the trunk and upper body, with the onset of muscle weakness usually occurring later in life (40+ years of age).[17][16]

Younger people may display unusual symptoms, such as difficulty in chewing, swallowing or utilizing normal oral motor functions.[18] A number of comorbidities were found in GSD-V individuals at a higher rate than found in the general population, including (but not limited to): hypertension (17%), endocrine diseases (15.7%), muskuloskeletal/rheumatic disease (12.9%), hyperuricemia/gout (11.6%), gastrointestinal diseases (11.2%), neurological disease (10%), respiratory disease (9.5%), and coronary artery disease (8.3%).[16] They may have a pseudoathletic appearance of muscle hypertrophy, particularly of the legs, and may have lower bone mineral content and density in the legs.[19][20][21]

Besides exercise-induced premature muscle fatigue, GSD-V individuals may also have comorbidities of mental fatigue, general fatigue, reduced motivation, sleep disturbances, anxiety and depression.[22]

As skeletal muscle relies predominantly on glycogenolysis for the first few minutes as it transitions from rest to activity, as well as throughout high-intensity aerobic activity and all anaerobic activity, individuals with GSD-V experience during exercise: sinus tachycardia, tachypnea, muscle fatigue and pain, during the aforementioned activities and time frames.[10][23] They may exhibit a “second wind” phenomenon, which is characterized by the individual's better tolerance for aerobic exercise such as walking and cycling after approximately 10 minutes.[24] This is attributed to the combination of increased blood flow and the ability of the body to find alternative sources of energy, like fatty acids, proteins, and increased blood glucose uptake.[6][10]

AMP is primarily produced from the myokinase (adenylate kinase) reaction,[25] which runs when the ATP reservoir is low. The myokinase reaction is one of three reactions in the phosphagen system (ATP-PCr), with the myokinase reaction occurring after phosphocreatine (creatine phosphate) has been depleted. In McArdle disease individuals, their muscle cells produce far more AMP than non-affected individuals as the reduced glycolytic flux from impaired glycogenolysis results in a chronically low ATP reservoir during exercise.[25] The muscle cells need ATP (adenosine triphosphate) as it provides energy for muscle contraction by actively transporting calcium ions into the sarcoplasmic reticulum before muscle contraction, and it is used during muscle contraction for the release of myosin heads in the sliding filament model during the cross-bridge cycle.

Along with the myokinase reaction, AMP is also produced by the purine nucleotide cycle, which also runs when the ATP reservoir in muscle cells is low, and is a part of protein metabolism. In the purine nucleotide cycle, three nucleotides: AMP (adenosine monophosphate), IMP (inosine monophosphate), and S-AMP (adenylosuccinate) are converted in a circular fashion; the byproducts are fumarate (which goes on to produce ATP via oxidative phosphorylation), ammonia (from the conversion of AMP into IMP), and uric acid (from excess AMP). GSD-V patients may experience myogenic hyperuricemia (exercise-induced accelerated breakdown of purine nucleotides in skeletal muscle).[26][27]

To avoid health complications, GSD-V patients need to get their ATP primarily from free fatty acids (lipid metabolism) rather than protein metabolism. Over-reliance on protein metabolism can be best avoided by not depleting their ATP reservoir, such as by not pushing through the pain and by not going too fast, too soon.[11][14]

"Be wary of pushing on when you feel pain start. This pain is a result of damaging muscles, and repeated damage will cause problems in the long term. But also this is counterproductive–it will stop you from getting into second wind. By pressing on despite the pain, you start your protein metabolism which then effectively blocks your glucose and fat metabolism. If you ever get into this situation, you need to stop completely for 30 minutes or more and then start the whole process again."[14]

Patients may present at emergency rooms with a transient contracture of the muscles and often severe pain (e.g. "clawed hand"). These require urgent assessment for rhabdomyolysis as in about 30% of cases this leads to acute kidney injury, which left untreated can be life-threatening. In a small number of cases compartment syndrome has developed, requiring prompt surgical referral.[17][28][29]

Genetics

Autosomal recessive inheritance

McArdle disease (GSD-V) is inherited in an autosomal recessive manner. If both parents are carriers (not having the disease, but each parent having one copy of the mutated allele), then each child of the couple will have a 25% chance of being affected (having McArdle disease), a 50% chance of being a carrier, and a 25% chance of being unaffected (neither a carrier nor diseased).[18]

Two autosomal recessive forms of this disease occur, childhood-onset and adult-onset. The gene for myophosphorylase, PYGM (the muscle-type of the glycogen phosphorylase gene), is located on chromosome 11q13. According to the most recent publications, 95 different mutations have been reported. The forms of the mutations may vary between ethnic groups. For example, the R50X (Arg50Stop) mutation (previously referred to as R49X) is most common in North America and western Europe, and the Y84X mutation is most common among central Europeans.[9]

The exact method of protein disruption has been elucidated in certain mutations. For example, R138W is known to disrupt to pyridoxal phosphate binding site.[30] In 2006, another mutation (c.13_14delCT) was discovered which may contribute to increased symptoms in addition to the common Arg50Stop mutation.[31]

Myophosphorylase

Structure

The myophosphorylase structure consists of 842 amino acids. Its molecular weight of the unprocessed precursor is 97 kDa. The three-dimensional structure has been determined for this protein. The interactions of several amino acids in myophosphorylase's structure are known. Ser-14 is modified by phosphorylase kinase during activation of the enzyme. Lys-680 is involved in binding the pyridoxal phosphate, which is the active form of vitamin B6, a cofactor required by myophosphorylase. By similarity, other sites have been estimated: Tyr-76 binds AMP, Cys-109 and Cys-143 are involved in subunit association, and Tyr-156 may be involved in allosteric control.[citation needed]

Function

Myophosphorylase is the form of the glycogen phosphorylase found in muscle that catalyses the following reaction:[32][33][34]

((1→4)-alpha-D-glucosyl) (n) + phosphate = ((1→4)-alpha-D-glucosyl) (n-1) + alpha-D-glucose 1-phosphate

Failure of this enzyme ultimately impairs the operation of ATPases. This is due to the lack of normal pH fall during exercise, which impairs the creatine kinase equilibrium and exaggerates the rise of ADP.[citation needed]

Pathophysiology

Myophosphorylase is involved in the breakdown of glycogen to glucose-1-phosphate for use in muscle. The enzyme removes 1,4 glycosyl residues from outer branches of glycogen and adds inorganic phosphate to form glucose-1-phosphate. Ordinarily, the removal of 1,4 glycosyl residues by myophosphorylase leads to the formation of glucose-1-phosphate during glycogen breakdown and the polar, phosphorylated glucose cannot leave the cell membrane and so is marked for intracellular catabolism. In McArdle's Disease, deficiency of myophosphorylase leads to accumulation of intramuscular glycogen and a lack of glucose-1-phosphate for cellular fuel.

Myophosphorylase comes in two forms: form 'a' is phosphorylated by phosphorylase kinase, form 'b' is not phosphorylated. Form 'a' is de-phosphorylated into form 'b' by the enzyme phosphoprotein phosphatase, which is activated by elevated insulin. Both forms have two conformational states: active (R or relaxed) and inactive (T or tense). When either form 'a' or 'b' are in the active state, then the enzyme converts glycogen into glucose-1-phosphate. Myophosphorylase-b is allosterically activated by elevated AMP within the cell, and allosterically inactivated by elevated ATP and/or glucose-6-phosphate. Myophosphorylase-a is active, unless allosterically inactivated by elevated glucose within the cell. In this way, myophosphorylase-a is the more active of the two forms as it will continue to convert glycogen into glucose-1-phosphate even with high levels of glycogen-6-phosphate and ATP. (See Glycogen phosphorylase§Regulation).

Diagnosis

There are some laboratory tests that may aid in diagnosis of GSD-V. A muscle biopsy will note the absence of myophosphorylase in muscle fibers. In some cases, abnormal accumulation of glycogen stained by periodic acid-Schiff can be seen with microscopy.[17][9]

Genetic sequencing of the PYGM gene (which codes for the muscle isoform of glycogen phosphorylase[35][36]) may be done to determine the presence of gene mutations, determining if McArdle's is present. This type of testing is considerably less invasive than a muscle biopsy.[18]

The physician can also perform an ischemic forearm exercise test as described above. Some findings suggest a nonischemic test could be performed with similar results.[37] The nonischemic version of this test would involve not cutting off the blood flow to the exercising arm. Findings consistent with McArdle's disease would include a failure of lactate to rise in venous blood and exaggerated ammonia levels. These findings would indicate a severe muscle glycolytic block.

Serum lactate may fail to rise in part because of increased uptake via the monocarboxylate transporter (MCT1), which is upregulated in skeletal muscle in McArdle disease. Lactate may be used as a fuel source once converted to pyruvate. Ammonia levels may rise given ammonia is a by-product of AMP deaminase which follows after the production of AMP by adenylate kinase, an alternative pathway for ATP production. In this pathway, adenylate kinase combines two ADP molecules to make ATP and AMP; AMP is then deaminated, producing inosine monophosphate (IMP) and ammonia (NH3) as part of purine nucleotide cycle.[38]

Physicians may also check resting levels of creatine kinase, which are moderately increased in 90% of patients.[10] In some, the level is increased by multitudes - a person without GSD-V will have a CK between 60 and 400IU/L, while a person with the syndrome may have a level of 5,000 IU/L at rest, and may increase to 35,000 IU/L or more with muscle exertion. This can help distinguish McArdle's syndrome from carnitine palmitoyltransferase II deficiency (CPT-II), a lipid-based metabolic disorder which prevents fatty acids from being transported into mitochondria for use as an energy source. Also, serum electrolytes and endocrine studies (such as thyroid function, parathyroid function and growth hormone levels) will also be completed. Urine studies are required only if rhabdomyolysis is suspected. Urine volume, urine sediment and myoglobin levels would be ascertained. If rhabdomyolysis is suspected, serum myoglobin, creatine kinase, lactate dehydrogenase, electrolytes and renal function will be checked.[citation needed]

Physicians may also conduct an exercise stress test to test for an inappropriate rapid heart rate (sinus tachycardia) in response to exercise. Due to the rare nature of the disease, the inappropriate rapid heart rate in response to exercise may be misdiagnosed as inappropriate sinus tachycardia (which is a diagnosis of exclusion). The 12 Minute Walk Test (12MWT) can be used to determine "second wind," which requires a treadmill (no incline), heart rate monitor, stop watch, pain scale, and that the patient has rested for 30 minutes prior to the test to ensure that "second wind" has stopped (that is, that increased ATP production primarily from free fatty acids has returned to resting levels).[12][39]

Electromyography (EMG) may show normal or myopathic results (short duration, polyphasic, small amplitude MUAPs).[9][40] Before exercise, a minority of GSD-V patients show myopathic results (5/25 patients); whereas after 5 minutes of high-intensity isometric exercise, the majority showed myopathic results (22/25 patients). The myopathic results were a decrease in CMAP amplitude, which was evident immediately after exercise and, after a plateau phase of a few minutes, reached its maximum after 30 minutes.[40]

Differential diagnoses

Dynamic symptoms of exercise intolerance (e.g. muscle fatigue and cramping) with or without fixed proximal muscle weakness:

  • Another glycogen storage disease that affects muscle (muscle GSD);
  • Metabolic myopathy other than glycogen storage disease;
  • Endocrine myopathy that affects carbohydrate metabolism secondary to the primary disease;
  • Inadequate blood flow (ischemia), particularly of the calves
  • Poor diet or malabsorption disease resulting in malnutrition of micronutrients essential for muscle glycogen metabolism.
  • Other rare myopathies, such as Brody disease, Rippling muscle disease, Erythrocyte lactate transporter defect, a small number of muscular dystrophies, Tubular aggregate myopathy (TAM), etc.

Exercise-induced muscle fatigue without cramping:

Fixed symptom of muscle weakness, predominantly of the proximal muscles:

  • Limb-girdle muscular dystrophy;
  • Inflammatory myopathy.

Allelic to McArdle disease (GSD-V) is a recently discovered disease that has a pathogenic autosomal dominant mutation on the PYGM gene. It impairs the ability of myophosphorylase to become phosphorylated, that is to be converted from myophosphorylase-b into myophosphorylase-a. Myophosphorylase-b can be activated to break down glycogen (glycogenolysis) by high levels of AMP, and as the amp-dependent activity was preserved, this disease does not have exercise intolerance (which is a prominent distinguishing feature from McArdle disease). The only symptom was adult-onset fixed muscle weakness. Muscle biopsy also showed accumulation of the intermediate filament desmin in the myofibres.[41][42]

Treatment

Supervised exercise programs have been shown in small studies to improve exercise capacity by several measures: lowering heart rate, lowering serum creatine kinase (CK), increasing the exercise intensity threshold before symptoms of muscle fatigue and cramping are experienced, and the skeletal muscles becoming aerobically conditioned.[43][44][21][6]

Oral sucrose treatment (for example a sports drink with 75 grams of sucrose in 660 ml.) taken 30 minutes prior to exercise has been shown to help improve exercise tolerance, including a lower heart rate and lower perceived level of exertion compared with placebo.[45] This is because the ingestion of a high-carbohydrate meal or drink causes transient hyperglycaemia, with the exercising muscle cells utilizing the high glucose in the blood for the glycolytic pathway. However, the ingestion of a high-carbohydrate meal or drink is problematic as a frequent form of treatment since it will increase the release of insulin, which inhibits the release of fatty acids[46] and subsequently will delay the ability to get into second wind.[11] The frequent ingestion of sucrose (e.g. sugary drinks), in order to avoid premature muscle fatigue and cramping, is also problematic in that it can lead to obesity as insulin will also stimulate triglyceride synthesis (develop body fat),[46] and obesity-related ill health (e.g. type II diabetes and heart disease).[11]

A low dosage treatment with creatine showed a significant improvement of muscle problems compared to placebo in a small clinical study, while other studies have shown minimal subjective benefit.[47][48] High dosage treatment of creatine has been shown to worsen symptoms of myalgia (muscle pain).[48]

A ketogenic diet has demonstrated beneficial for McArdle disease (GSD-V) as ketones readily convert to acetyl CoA for oxidative phosphorylation, whereas free fatty acids take a few minutes to convert into acetyl CoA.[49][50] Ketones are a part of fat metabolism,[46] the ketones can act as the main fuel before fatty acid catabolism takes over (second wind), during which the ketones would act as a supplementary fuel along side the fatty acids to produce adenosine triphosphate (ATP) by oxidative phosphorylation.

History

The deficiency was the first metabolic myopathy to be recognized, when the physician Brian McArdle described the first case in a 30-year-old man who always experienced pain and weakness after exercise. McArdle noticed this patient's cramps were electrically silent and his venous lactate levels failed to increase upon ischemic exercise. (The ischemic exercise consists of the patient squeezing a hand dynamometer at maximal strength for a specific period of time, usually a minute, with a blood pressure cuff, which is placed on the upper arm and set at 250 mmHg, blocking blood flow to the exercising arm.)

Notably, this is the same phenomenon that occurs when muscle is poisoned in vitro by iodoacetate, which inhibits the breakdown of glycogen into glucose and prevents the formation of lactate; as well as produces an electronically silent muscle contracture. Knowing what occurs to muscle poisoned by iodoacetate, helped McArdle speculate that a glycogenolytic block might be occurring when he first described the disease.[51] McArdle accurately concluded that the patient had a disorder of glycogen breakdown that specifically affected skeletal muscle. The associated enzyme deficiency was discovered in 1959 by W. F. H. M. Mommaerts et al.[52]

In animals

Naturally-occurring myophosphorylase deficiency (GSD-V; McArdle disease) has been found in Charolais cattle and Merino sheep.[53] The cattle were asymptomatic at rest, but when forced to exercise, would become noticeably fatigued and recumbent (having to lie down) for approximately 10 minutes before being able to resume exercise (the second wind phenomenon).[54][55]

Artificially-induced myophosphorylase deficiency was created in mice, by altering their embryonic DNA, for use in laboratory experiments.[53][56]

See also

References

  1. ↑ "Glycogen Storage Disease Type V (GSD V)". Syndromes: Rapid Recognition and Perioperative Implications (2nd ed.). New York, NY: McGraw-Hill Education. 2019. http://accesspediatrics.mhmedical.com/content.aspx?aid=1164071134. Retrieved 2021-12-12. 
  2. ↑ 2.0 2.1 2.2 "Inflammatory Diseases of Muscle and Other Myopathies". Kelley's Textbook of Rheumatology. 2013. pp. 1404–1430.e5. doi:10.1016/b978-1-4377-1738-9.00085-2. ISBN 978-1-4377-1738-9. 
  3. ↑ "A proposed molecular diagnostic flowchart for myophosphorylase deficiency (McArdle disease) in blood samples from Spanish patients". Human Mutation 28 (2): 203–204. February 2007. doi:10.1002/humu.9474. PMID 17221871. 
  4. ↑ "Skeletal Muscle Function". Clinical Biochemistry of Domestic Animals. 2008. pp. 459–484. doi:10.1016/b978-0-12-370491-7.00015-5. ISBN 978-0-12-370491-7. 
  5. ↑ Brian McArdle at Who Named It?
  6. ↑ 6.0 6.1 6.2 6.3 6.4 "Development of Continuum of Care for McArdle disease: A practical tool for clinicians and patients". Neuromuscular Disorders 33 (7): 575–579. July 2023. doi:10.1016/j.nmd.2023.05.006. PMID 37354872. 
  7. ↑ "McArdle's disease presenting with asymmetric, late-onset arm weakness". Muscle & Nerve 23 (4): 641–645. April 2000. doi:10.1002/(SICI)1097-4598(200004)23:4<641::AID-MUS25>3.0.CO;2-M. PMID 10716777. 
  8. ↑ 8.0 8.1 8.2 8.3 8.4 Scalco, Renata Siciliani; Morrow, Jasper M.; Booth, Suzanne; Chatfield, Sherryl; Godfrey, Richard; Quinlivan, Ros (September 2017). "Misdiagnosis is an important factor for diagnostic delay in McArdle disease". Neuromuscular Disorders 27 (9): 852–855. doi:10.1016/j.nmd.2017.04.013. ISSN 1873-2364. PMID 28629675. 
  9. ↑ 9.0 9.1 9.2 9.3 Chéraud, Chrystel; Froissart, Roseline; Lannes, Béatrice; Echaniz-Laguna, Andoni (January 2018). "Novel variant in the PYGM gene causing late-onset limb-girdle myopathy, ptosis, and camptocormia". Muscle & Nerve 57 (1): 157–160. doi:10.1002/mus.25588. ISSN 1097-4598. PMID 28120463. https://pubmed.ncbi.nlm.nih.gov/28120463/. 
  10. ↑ 10.0 10.1 10.2 10.3 "Clinical practice guidelines for glycogen storage disease V & VII (McArdle disease and Tarui disease) from an international study group". Neuromuscular Disorders 31 (12): 1296–1310. December 2021. doi:10.1016/j.nmd.2021.10.006. PMID 34848128. 
  11. ↑ 11.0 11.1 11.2 11.3 11.4 Living With McArdle Disease. IAMGSD. 2017. https://www.iamgsd.org/_files/ugd/c951b2_91a5802caa2144d5aedbb0489c1cf543.pdf. 
  12. ↑ 12.0 12.1 "The Second Wind in McArdle Patients: Fitness Matters". Frontiers in Physiology 12: 744632. 2021. doi:10.3389/fphys.2021.744632. PMID 34721068. 
  13. ↑ Perez, M.; Martin, M. A.; Rubio, J. C.; Maté-Muñoz, J. L.; Gómez-Gallego, F.; Foster, C.; Andreu, A. L.; Arenas, J. et al. (August 2006). "Exercise capacity in a 78 year old patient with McArdle's disease: it is never too late to start exercising". British Journal of Sports Medicine 40 (8): 725–726; discussion 726. doi:10.1136/bjsm.2006.026666. ISSN 1473-0480. PMID 16864568. 
  14. ↑ 14.0 14.1 14.2 101 Tips For A Good Life With McArdle Disease. AGSD-UK Ltd.. 2013. https://www.iamgsd.org/_files/ugd/c951b2_452b11293216448caedd2909082fd924.pdf. 
  15. ↑ "Rhabdomyolysis". StatPearls [Internet]. Treasure Island (FL): StatPearls Publishing. 10 August 2022. https://www.ncbi.nlm.nih.gov/books/NBK448168/. 
  16. ↑ 16.0 16.1 16.2 "Data from the European registry for patients with McArdle disease and other muscle glycogenoses (EUROMAC)". Orphanet Journal of Rare Diseases 15 (1): 330. November 2020. doi:10.1186/s13023-020-01562-x. PMID 33234167. 
  17. ↑ 17.0 17.1 17.2 Ph.D, Kathryn Elizabeth Birch (2011-07-01) (in en). The McArdle Disease Handbook: A guide to the scientific and medical research into McArdle Disease, explained in plain English.. AGSD-UK. ISBN 978-0-9569658-1-3. https://books.google.com/books?id=uHuQibxWcHgC. 
  18. ↑ 18.0 18.1 18.2 "Glycogen Storage Disease Type V". GeneReviews®. University of Washington, Seattle. 1993. http://www.ncbi.nlm.nih.gov/books/NBK1344/. 
  19. ↑ "Non-osteogenic muscle hypertrophy in children with McArdle disease". Journal of Inherited Metabolic Disease 41 (6): 1037–1042. November 2018. doi:10.1007/s10545-018-0170-7. PMID 29594644. 
  20. ↑ Rodríguez-Gómez, Irene; Santalla, Alfredo; Díez-Bermejo, Jorge; Munguía-Izquierdo, Diego; Alegre, Luis M.; Nogales-Gadea, Gisela; Arenas, Joaquin; Martín, Miguel Ángel et al. (January 2018). "A New Condition in McArdle Disease: Poor Bone Health—Benefits of an Active Lifestyle" (in en-US). Medicine & Science in Sports & Exercise 50 (1): 3–10. doi:10.1249/MSS.0000000000001414. ISSN 0195-9131. PMID 29251685. https://journals.lww.com/acsm-msse/fulltext/2018/01000/a_new_condition_in_mcardle_disease__poor_bone.2.aspx. 
  21. ↑ 21.0 21.1 Pietrusz, Aleksandra; Scalco, Renata S.; Quinlivan, Ros (2018). "Resistance Exercise Training in McArdle Disease: Myth or Reality?". Case Reports in Neurological Medicine 2018: 9658251. doi:10.1155/2018/9658251. ISSN 2090-6668. PMID 30363996Patient 1 had hypertrophy of calf, deltoid and bicep muscles before resistance training commenced, while living a sedentary lifestyle with an office job, walking short distances was difficult as was everyday tasks like vacuuming and cutting the grass. After four years of resistance training, pre-existing hypertrophy in deltoid muscles increased further and muscle bulk was gained in additional muscle groups (quadriceps, gluteus, pectoralis, and trapezius muscles). 
  22. ↑ Slipsager, Anna; Andersen, Linda Kahr; Voermans, Nicol Cornelia; Lucia, Alejandro; Karazi, Walaa; Santalla, Alfredo; Vissing, John; Løkken, Nicoline (2023-11-11). "Fatigue and associated factors in 172 patients with McArdle disease: An international web-based survey". Neuromuscular Disorders 34: 19–26. doi:10.1016/j.nmd.2023.11.003. ISSN 1873-2364. PMID 38042739. 
  23. ↑ "From exercise intolerance to functional improvement: the second wind phenomenon in the identification of McArdle disease". Arquivos de Neuro-Psiquiatria 72 (7): 538–541. July 2014. doi:10.1590/0004-282x20140062. PMID 25054987. 
  24. ↑ "A metabolic myopathy due to absence of muscle phosphorylase". The American Journal of Medicine 30 (4): 502–517. April 1961. doi:10.1016/0002-9343(61)90075-4. PMID 13733779. 
  25. ↑ 25.0 25.1 "Phenotype consequences of myophosphorylase dysfunction: insights from the McArdle mouse model". The Journal of Physiology 593 (12): 2693–2706. June 2015. doi:10.1113/JP270085. PMID 25873271. 
  26. ↑ "Myogenic hyperuricemia. A common pathophysiologic feature of glycogenosis types III, V, and VII". The New England Journal of Medicine 317 (2): 75–80. July 1987. doi:10.1056/NEJM198707093170203. PMID 3473284. 
  27. ↑ "Myogenic hyperuricemia: what can we learn from metabolic myopathies?". Muscle & Nerve. Supplement 3: S75–S81. 1995. doi:10.1002/mus.880181416. PMID 7603532. 
  28. ↑ Triplet, Jacob J.; Goss, David A.; Taylor, Benjamin (September 2017). "Spontaneous Compartment Syndrome in a Patient with McArdle Disease: A Case Report and Review of the Literature" (in en). JBJS Case Connector 7 (3): e49. doi:10.2106/JBJS.CC.16.00196. ISSN 2160-3251. PMID 29252879. https://journals.lww.com/01709767-201707030-00009. 
  29. ↑ Mull, Aaron B.; Wagner, Janelle I.; Mycktayn, Terence M.; Kells, Amy F. (December 2015). "Recurrent Compartment Syndrome Leading to the Diagnosis of McArdle Disease: Case Report". The Journal of Hand Surgery 40 (12): 2377–2379. doi:10.1016/j.jhsa.2015.09.015. ISSN 0363-5023. PMID 26612634. https://doi.org/10.1016/j.jhsa.2015.09.015. 
  30. ↑ "Molecular analysis of myophosphorylase deficiency in Dutch patients with McArdle's disease". Annals of Human Genetics 68 (Pt 1): 17–22. January 2004. doi:10.1046/j.1529-8817.2003.00067.x. PMID 14748827. 
  31. ↑ "Novel mutation in the PYGM gene resulting in McArdle disease". Archives of Neurology 63 (12): 1782–1784. December 2006. doi:10.1001/archneur.63.12.1782. PMID 17172620. 
  32. ↑ "PYGM - Glycogen phosphorylase, muscle form - Homo sapiens (Human) - PYGM gene & protein" (in en). https://www.uniprot.org/uniprot/P11217.  This article incorporates text available under the CC BY 4.0 license.
  33. ↑ "UniProt: the universal protein knowledgebase". Nucleic Acids Research 45 (D1): D158–D169. January 2017. doi:10.1093/nar/gkw1099. PMID 27899622. 
  34. ↑ "Reaction participants of glycogen phosphorylase" (in en). https://www.rhea-db.org/rhea/41732. 
  35. ↑ NCBI Gene ID 5837: PYGM phosphorylase, glycogen, muscle, https://www.ncbi.nlm.nih.gov/gene/5837, retrieved 22 May 2013 
  36. ↑ "PYGM", NLM Genetics Home Reference, http://ghr.nlm.nih.gov/gene/PYGM, retrieved 22 May 2013 
  37. ↑ "A nonischemic forearm exercise test for McArdle disease". Annals of Neurology 52 (2): 153–159. August 2002. doi:10.1002/ana.10263. PMID 12210784. 
  38. ↑ "McArdle Disease and Exercise Physiology". Biology 3 (1): 157–166. February 2014. doi:10.3390/biology3010157. PMID 24833339. 
  39. ↑ "IAMGSD | Training support" (in en). https://www.iamgsd.org/training-support. 
  40. ↑ 40.0 40.1 Semplicini, Claudio; Hézode-Arzel, Marianne; Laforêt, Pascal; Béhin, Anthony; Leonard-Louis, Sarah; Hogrel, Jean-Yves; Petit, François; Eymard, Bruno et al. (2018-01-19). "The role of electrodiagnosis with long exercise test in mcardle disease". Muscle & Nerve 58: 64–71. doi:10.1002/mus.26074. ISSN 1097-4598. PMID 29350794. https://pubmed.ncbi.nlm.nih.gov/29350794/. 
  41. ↑ Echaniz-Laguna, A.; Lornage, X.; Edelweiss, E.; Laforêt, P.; Eymard, B.; Vissing, J.; Laporte, J.; Böhm, J. (October 2019). "O.5 A new glycogen storage disorder caused by a dominant mutation in the glycogen myophosphorylase gene (PYGM)". Neuromuscular Disorders 29: S39. doi:10.1016/j.nmd.2019.06.023. ISSN 0960-8966. https://doi.org/10.1016/j.nmd.2019.06.023. 
  42. ↑ Echaniz-Laguna, Andoni; Lornage, Xavière; Laforêt, Pascal; Orngreen, Mette C.; Edelweiss, Evelina; Brochier, Guy; Bui, Mai T.; Silva-Rojas, Roberto et al. (August 2020). "A New Glycogen Storage Disease Caused by a Dominant PYGM Mutation" (in en). Annals of Neurology 88 (2): 274–282. doi:10.1002/ana.25771. ISSN 0364-5134. PMID 32386344. https://onlinelibrary.wiley.com/doi/10.1002/ana.25771. 
  43. ↑ "Can patients with McArdle's disease run?". British Journal of Sports Medicine 41 (1): 53–54. January 2007. doi:10.1136/bjsm.2006.030791. PMID 17000713. 
  44. ↑ "Aerobic conditioning: an effective therapy in McArdle's disease". Annals of Neurology 59 (6): 922–928. June 2006. doi:10.1002/ana.20881. PMID 16718692. 
  45. ↑ "The effect of oral sucrose on exercise tolerance in patients with McArdle's disease". The New England Journal of Medicine 349 (26): 2503–2509. December 2003. doi:10.1056/NEJMoa031836. PMID 14695410. 
  46. ↑ 46.0 46.1 46.2 Coffee, Carole J. (1999). Quick Look Medicine: Metabolism. Hayes Barton Press. ISBN 1-59377-192-4. 
  47. ↑ "Creatine therapy in myophosphorylase deficiency (McArdle disease): a placebo-controlled crossover trial". Archives of Neurology 57 (7): 956–963. July 2000. doi:10.1001/archneur.57.7.956. PMID 10891977. 
  48. ↑ 48.0 48.1 Quinlivan, Rosaline; Martinuzzi, Andrea; Schoser, Benedikt (2014-11-12). "Pharmacological and nutritional treatment for McArdle disease (Glycogen Storage Disease type V)". The Cochrane Database of Systematic Reviews 2014 (11): CD003458. doi:10.1002/14651858.CD003458.pub5. ISSN 1469-493X. PMID 25391139. 
  49. ↑ "Titrating a modified ketogenic diet for patients with McArdle disease: A pilot study". Journal of Inherited Metabolic Disease 43 (4): 778–786. July 2020. doi:10.1002/jimd.12223. PMID 32060930. 
  50. ↑ "Patient-Reported Experiences with a Low-Carbohydrate Ketogenic Diet: An International Survey in Patients with McArdle Disease". Nutrients 15 (4): 843. February 2023. doi:10.3390/nu15040843. PMID 36839201. 
  51. ↑ "McArdle's disease in the 1980s". The New England Journal of Medicine 312 (6): 370–371. February 1985. doi:10.1056/NEJM198502073120609. PMID 3855500. 
  52. ↑ "A Functional Disorder of Muscle Associated with the Absence of Phosphorylase". Proceedings of the National Academy of Sciences of the United States of America 45 (6): 791–797. June 1959. doi:10.1073/pnas.45.6.791. PMID 16590445. Bibcode: 1959PNAS...45..791M. 
  53. ↑ 53.0 53.1 DiMauro, Salvatore; Akman, Hasan Orhan (2015-01-01), Rosenberg, Roger N.; Pascual, Juan M., eds., "Chapter 54 - Glycogen Storage Diseases", Rosenberg's Molecular and Genetic Basis of Neurological and Psychiatric Disease (Fifth Edition) (Boston: Academic Press): pp. 607–614, doi:10.1016/b978-0-12-410529-4.00054-1, ISBN 978-0-12-410529-4, https://www.sciencedirect.com/science/article/pii/B9780124105294000541, retrieved 2023-11-11 
  54. ↑ Valberg, Stephanie J. (2008-01-01), Kaneko, J. Jerry; Harvey, John W.; Bruss, Michael L., eds., "Chapter 15 - Skeletal Muscle Function", Clinical Biochemistry of Domestic Animals (Sixth Edition) (San Diego: Academic Press): pp. 459–484, doi:10.1016/b978-0-12-370491-7.00015-5, ISBN 978-0-12-370491-7, https://www.sciencedirect.com/science/article/pii/B9780123704917000155, retrieved 2023-11-11 
  55. ↑ Valentine, Beth A. (2017-01-01), Zachary, James F., ed., "Chapter 15 - Skeletal Muscle1", Pathologic Basis of Veterinary Disease (Sixth Edition) (Mosby): pp. 908–953.e1, doi:10.1016/b978-0-323-35775-3.00015-1, ISBN 978-0-323-35775-3 
  56. ↑ Brull, Astrid; de Luna, Noemí; Blanco-Grau, Albert; Lucia, Alejandro; Martin, Miguel Angel; Arenas, Joaquin; Martí, Ramon; Andreu, Antoni L. et al. (2015-06-15). "Phenotype consequences of myophosphorylase dysfunction: insights from the McArdle mouse model". The Journal of Physiology 593 (12): 2693–2706. doi:10.1113/JP270085. ISSN 1469-7793. PMID 25873271. 

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