muscular dystrophies/phosphatase

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Mutations in INPP5K, Encoding a Phosphoinositide 5-Phosphatase, Cause Congenital Muscular Dystrophy with Cataracts and Mild Cognitive Impairment.

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Phosphoinositides are small phospholipids that control diverse cellular downstream signaling events. Their spatial and temporal availability is tightly regulated by a set of specific lipid kinases and phosphatases. Congenital muscular dystrophies are hereditary disorders characterized by hypotonia

Congenital muscular dystrophy syndromes distinguished by alkaline and acid phosphatase, merosin, and dystrophin staining.

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Congenital muscular dystrophy syndromes are characterized by congenital weakness, contractures, and dystrophic features on muscle biopsy. However, these syndromes are often difficult to diagnose precisely because their clinical and pathologic characteristics are not specific and resemble changes in

MAP kinase phosphatase-1 deficiency impairs skeletal muscle regeneration and exacerbates muscular dystrophy.

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In skeletal muscle, the mitogen-activated protein kinase (MAPK) phosphatase-1 (MKP-1) is a critical negative regulator of the MAPKs. Since the MAPKs have been reported to be both positive and negative for myogenesis, the physiological role of MKP-1 in skeletal muscle repair and regeneration has

4-Nitrophenylalkaline phosphatase inhibition in muscular dystrophy.

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The allosteric behaviour of 4-nitrophenylphosphatase from membrane erythrocytes was investigated in Duchenne muscular dystrophy (DMD) patients, in female carriers and in healthy controls. Cooperative type kinetics with a Hill coefficient of -2.19, -1.71 and -1.54 has been obtained from the

[A comparison of histochemical features of some specific phosphatases in progressive muscular dystrophy, in neurogenic myopathies in man and in the denervated rat muscle (author's transl)].

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Allosteric transition of erythrocyte alkaline phosphatase from Duchenne muscular dystrophy (DMD) patients and Duchenne muscular dystrophy carriers (Homo sapiens).

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1. The kinetic properties of the p-nitrophenylphosphatase (EC 3.1.3.1) from erythrocytes was investigated in DMD-patients and DMD-carriers. 2. A different allosteric behaviour in the p-nitrophenylphosphatase from DMD-patients and DMD-carriers compared to controls is supported by the following

Phosphatase activities in mice with hereditary muscular dystrophy.

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[Serum phosphatase activity in progressive muscular dystrophy].

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[Alkaline phosphatase of red blood cells in muscular dystrophy].

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Nitric oxide deficiency determines global chromatin changes in Duchenne muscular dystrophy.

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The present study provides evidence that abnormal patterns of global histone modification are present in the skeletal muscle nuclei of mdx mice and Duchenne muscular dystrophy (DMD) patients. A combination of specific histone H3 modifications, including Ser-10 phosphorylation, acetylation of Lys 9

Genetic mutations strengthen functional association of LAP1 with DYT1 dystonia and muscular dystrophy.

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Lamina-associated polypeptide 1 (LAP1) is a ubiquitously expressed integral protein of the inner nuclear membrane. It interacts physically with lamins, torsinA, emerin and protein phosphatase 1; potentially providing a pivotal mechanism for transducing signals across the inner nuclear membrane. In

Phosphoinositide 5-phosphatases SKIP and SHIP2 in ruffles, the endoplasmic reticulum and the nucleus: An update.

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Phosphoinositides (PIs) are phosphorylated derivatives of phosphatidylinositol. They act as signaling molecules linked to essential cellular mechanisms in eukaryotic cells, such as cytoskeleton organization, mitosis, polarity, migration or invasion. PIs are phosphorylated and dephosphorylated by a

PAI-1-regulated miR-21 defines a novel age-associated fibrogenic pathway in muscular dystrophy.

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Disruption of skeletal muscle homeostasis by substitution with fibrotic tissue constitutes the principal cause of death in Duchenne muscular dystrophy (DMD) patients, yet the implicated fibrogenic mechanisms remain poorly understood. This study identifies the extracellular PAI-1/urokinase-type

Mutations in INPP5K Cause a Form of Congenital Muscular Dystrophy Overlapping Marinesco-Sjögren Syndrome and Dystroglycanopathy.

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Congenital muscular dystrophies display a wide phenotypic and genetic heterogeneity. The combination of clinical, biochemical, and molecular genetic findings must be considered to obtain the precise diagnosis and provide appropriate genetic counselling. Here we report five individuals from four

Interpretation of acid α-glucosidase activity in creatine kinase elevation: A case of Becker muscular dystrophy.

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BACKGROUND Diagnosis of Pompe disease is sometimes challenging because it exhibits clinical similarities to muscular dystrophy. METHODS We describe a case of Becker muscular dystrophy (BMD) with a remarkable reduction in activity of the acid α-glucosidase (GAA) enzyme, caused by a combination of

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