Exertional rhabdomyolysis in a patient with calcium adenosine triphosphatase deficiency.

Poels, P.J.E.; Wevers, Ron A.; Braakhekke, J. P.; Benders, A.A.G.M.; Veerkamp, J.H.; Joosten, E.M.G.

doi:10.1136/jnnp.56.7.823

Cited by 30 publications

(32 citation statements)

References 15 publications

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“…107,122,125,152,153 Inherited metabolic myopathies may present with myoglobinuria, triggered by physical stresses such as exercise, fasting, or infection, even in adult life. 16,18,39,70,77,87,104,105,114,115,125,139,140,151 The inherited causes of rhabdomyolysis are classified in Table 2 according to the step in myocyte metabolism that they disrupt. Combined defects have been described in several patients.…”

Section: Inherited Metabolic Myopathiesmentioning

confidence: 99%

“…The steps of ␤-oxidation are detailed in Figure 3. scription of idiopathic paroxysmal myoglobinuria is credited to Meyer-Betz, 102 and many cases have been reported. 9,29,45,125,128,136,153 An autosomal recessive pattern of inheritance may be evident. 29,45,128,135 Cases can be broadly classified according to whether attacks are triggered by exertion (the more common scenario) or infection, often with starvation.…”

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confidence: 97%

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Rhabdomyolysis: A review

2002

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Rhabdomyolysis, a syndrome of skeletal muscle breakdown with leakage of muscle contents, is frequently accompanied by myoglobinuria, and if sufficiently severe, acute renal failure with potentially life-threatening metabolic derangements may ensue. A diverse spectrum of inherited and acquired disorders affecting muscle membranes, membrane ion channels, and muscle energy supply causes rhabdomyolysis. Common final pathophysiological mechanisms among these causes of rhabdomyolysis include an uncontrolled rise in free intracellular calcium and activation of calcium-dependent proteases, which lead to destruction of myofibrils and lysosomal digestion of muscle fiber contents. Recent advances in molecular genetics and muscle enzyme histochemistry may enable a specific metabolic diagnosis in many patients with idiopathic recurrent rhabdomyolysis.

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Section: Inherited Metabolic Myopathiesmentioning

confidence: 99%

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confidence: 97%

Rhabdomyolysis: A review

2002

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“…Brody disease, a rare inherited disorder, is characterized by exercise-induced delay in skeletal muscle relaxation, which is most pronounced in the legs, arms, and eyelids (Benders et al 1994;Brody 1969;Danon et al 1988;Karpati et al 1986;Poels et al 1993;Taylor et al 1988;Wevers et al 1992). The muscles stiffen during sustained strenuous muscular activities, leading to painless or only mildly painful cramping.…”

Section: Introductionmentioning

confidence: 98%

The mutation of Pro789 to Leu reduces the activity of the fast-twitch skeletal muscle sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA1) and is associated with Brody disease

et al. 2000

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Brody disease is a rare inherited disorder of fast-twitch skeletal muscle function and is characterized by a lifelong history of exercise-induced impairment of skeletal muscle relaxation, stiffness, and cramps. The autosomal recessive inheritance of mutations in ATP2A1, the gene encoding SERCA1, which is the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+ ATPase, has been associated with Brody disease in three of six Brody families in which ATP2A1 has been sequenced. In the present analysis of the ATP2A1 gene in four unrelated families with autosomal recessive inheritance of Brody disease, three mutations were found in two families, leading to premature stop codons and truncated SERCA1. In a third family, the homozygous substitution of T for C2366 led to the missense mutation of Pro789 to Leu. The Pro789 to Leu mutant was readily expressed in HEK-293 cells, but it demonstrated an almost complete loss of Ca2+ transport activity because of reduced Ca2+ affinity. In a fourth family, the heterozygous substitution of T for C2455, mutating Arg819 to Cys, was identified. This mutation was also readily expressed in HEK-293 cells and shown to have near normal Ca2+ transport activity, indicating that it is not causal for Brody disease. These results confirm the genetic heterogeneity of Brody disease and emphasize the importance of a functional test for mutant SERCA1; immunostaining of skeletal muscle to detect the loss of SERCA1a protein is not adequate for the diagnosis of ATP2A1-linked Brody disease.

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“…Serum creatine kinase (CK) is normal or slightly increased, needle electromyography (EMG) records no myotonic and pseudomyotonic discharges during the exercise-induced muscle stiffness ("silent cramps") and percussion myotonia is absent [5,[8][9][10][11]. At present, no treatment is available for patients even though dantrolene and verapamil turned out to be useful for reduction of muscle stiffness and thus for improving exercise tolerance [6,10].…”

Section: Introductionmentioning

confidence: 99%

“…Ultrastructural abnormalities include increased number of membranous bodies within sarcoplasmic reticulum (SR) vesicles, enlargement of lateral cisternae with proliferation of the tubular SR elements and presence of swollen mitochondria [11,12].…”

Section: Introductionmentioning

confidence: 99%

Transfection efficiency in rat soleus and SERCA1b expression in human skeletal muscles

Kósa¹

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Keywords:Brody disease Sarcoplasmic/endoplasmic reticulum Ca Therefore it has been proposed to distinguish patients with ATP2A1 mutations, Brody disease (BD), from patients without mutations, Brody syndrome (BS). We performed a detailed study of SERCA1 protein expression in muscle of patients with BD and BS, and evaluated the alternative splicing of SERCA1 in primary cultures of normal human muscle and in infant muscle. SERCA1 reactivity was observed in type 2 muscle fibers of patients with and without ATP2A1 mutations and staining intensity was similar in patients and controls. Immunoblot analysis showed a significant reduction of SERCA1 band in muscle of BD patients. In addition we demonstrated that the wild type and mutated protein exhibits similar solubility properties and that RIPA buffer improves the recovery of the wild type and mutated SERCA1 protein. We found that SERCA1b, the SERCA1 neonatal form, is the main protein isoform expressed in cultured human muscle fibers and infant muscle. Finally, we identified two novel heterozygous mutations within exon 3 of the ATP2A1 gene from a previously described patient with BD.

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Exertional rhabdomyolysis in a patient with calcium adenosine triphosphatase deficiency.

Cited by 30 publications

References 15 publications

Rhabdomyolysis: A review

Rhabdomyolysis: A review

The mutation of Pro789 to Leu reduces the activity of the fast-twitch skeletal muscle sarco(endo)plasmic reticulum Ca2+ ATPase (SERCA1) and is associated with Brody disease

Transfection efficiency in rat soleus and SERCA1b expression in human skeletal muscles

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