myotonic dystrophy/phosphatase

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Caenorhabditis elegans LET-502 is related to Rho-binding kinases and human myotonic dystrophy kinase and interacts genetically with a homolog of the regulatory subunit of smooth muscle myosin phosphatase to affect cell shape.

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We have identified two genes associated with the hypodermal cell shape changes that occur during elongation of the Caenorhabditis elegans embryo. The first gene, called let-502, encodes a protein with high similarity to Rho-binding Ser/Thr kinases and to human myotonic dystrophy kinase (DM-kinase).

Myotonic dystrophy protein kinase phosphorylates the myosin phosphatase targeting subunit and inhibits myosin phosphatase activity.

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Myotonic dystrophy protein kinase (DMPK) and Rho-kinase are related. An important function of Rho-kinase is to phosphorylate the myosin-binding subunit of myosin phosphatase (MYPT1) and inhibit phosphatase activity. Experiments were carried out to determine if DMPK could function similarly. MYPT1

Coiled-coil interactions modulate multimerization, mitochondrial binding and kinase activity of myotonic dystrophy protein kinase splice isoforms.

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The myotonic dystrophy protein kinase polypeptide repertoire in mice and humans consists of six different splice isoforms that vary in the nature of their C-terminal tails and in the presence or absence of an internal Val-Ser-Gly-Gly-Gly motif. Here, we demonstrate that myotonic dystrophy protein

Abnormal liver test results in myotonic dystrophy.

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Myotonic dystrophy (DM) is an autosomal dominant multisystem disorder. Little evidence suggests the existence of liver damage in a small number of patients. We have prospectively evaluated liver and gallbladder function in 53 patients with DM in relation to clinical and genetic parameters. None of

Erythrocyte alkaline phosphatase in patients with myotonic muscle disorders.

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The allosteric behaviour of the p-nitrophenyl-phosphatase (E.C.3.1.3.1.) from membrane erythrocytes was investigated in the following multisystemic diseases: myotonic dystrophy, limb-girdle muscular dystrophy, Charcot-Marie-Tooth and juvenile spinal muscular atrophy; in myotonia congenita, which is

Individual nonobese diabetic mice exhibit unique patterns of CD8+ T cell reactivity to three islet antigens, including the newly identified widely expressed dystrophia myotonica kinase.

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Spontaneous autoimmune diabetes development in NOD mice requires both CD8(+) and CD4(+) T cells. Three pathogenic CD8(+) T cell populations (represented by the G9C8, 8.3, and AI4 clones) have been described. Although the Ags for G9C8 and 8.3 are known to be insulin and islet-specific

Analysis of trinucleotide repeats in myotonic dystrophy.

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Myotonic dystrophy is a genetic disorder characterized in 99% of clinically diagnosed families by an unstable CTG repeat in the 3-untranslated region of a gene encoding a serine-threonine protein kinase. There is no one method to detect the entire range of expansion sizes possible in affected

Skeletal muscle in preterm infants with congenital myotonic dystrophy. Morphologic and histochemical study.

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The skeletal muscle in 3 preterm infants (27, 34, 37 weeks gestation age) born to mothers with myotonic dystrophy showed a syncytial pattern at 27 weeks and a decreasing percentage of satellite cells and central nuclei at 34 and 37 weeks gestation. The fiber type differentiation was observed only at

Muscle maturation delay in infantile myotonic dystrophy.

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Specimens of the quadriceps femoris muscle from four infants with neonatal myotonic dystrophy had features of muscle fiber immaturity. Delayed establishment of major fiber subtypes and persistent myotubes, seen in the youngest infant, resolved in a repeated specimen obtained at the age of 4 months.

Erythrocyte membrane abnormalities in human myotonic dystrophy.

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Membrane-bound enzyme activities and cardiac glycoside binding were determined in red blood cell membrane preparations from patients with myotonic dystrophy and in age matched controls. Na+-K+-activated ATPase activity was significantly increased in myotonic patients. [3H]Ouabain binding to

Lymphocyte abnormality in human myotonic dystrophy and experimental drug-induced myotonia.

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In the cytoplasm of peripheral blood lymphocytes in 3 of 13 patients with myotonic dystrophy, myelin-like structures were observed electronmicroscopically. Some were connected to the cytoplasmic membranes, and some were surrounded by a limiting membrane possessing acid phosphatase activity. These

Deficiency of Na+/K(+)-ATPase and sarcoplasmic reticulum Ca(2+)-ATPase in skeletal muscle and cultured muscle cells of myotonic dystrophy patients.

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Since defective regulation of ion transport could initiate or contribute to the abnormal cellular function in myotonic dystrophy (MyD), Na+/K(+)-ATPase and sarcoplasmic reticulum (SR) Ca(2+)-ATPase were examined in skeletal muscle and cultured skeletal muscle cells of controls and MyD patients.

Abnormal splicing of NEDD4 in myotonic dystrophy type 2: possible link to statin adverse reactions.

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Myotonic dystrophy type 2 (DM2) is a multisystemic disorder caused by a (CCTG)n repeat expansion in intron 1 of CNBP. Transcription of the repeats causes a toxic RNA gain of function involving their accumulation in ribonuclear foci. This leads to sequestration of splicing factors and alters pre-mRNA

Intrinsic Myogenic Potential of Skeletal Muscle-Derived Pericytes from Patients with Myotonic Dystrophy Type 1.

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Pericytes are multipotent, vessel-associated progenitors that exhibit high proliferative capacity, can cross the blood-muscle barrier, and have the ability to home to muscle tissue and contribute to myogenesis. Consequently, pericyte-based therapies hold great promise for muscular dystrophies. A

Phosphorylation of a novel myosin binding subunit of protein phosphatase 1 reveals a conserved mechanism in the regulation of actin cytoskeleton.

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The myotonic dystrophy kinase-related kinases RhoA binding kinase and myotonic dystrophy kinase-related Cdc42 binding kinase (MRCK) are effectors of RhoA and Cdc42, respectively, for actin reorganization. Using substrate screening in various tissues, we uncovered two major substrates, p130 and p85,

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