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The horse PYGM gene was broadly expressed in all tissues tested with the highest expression observed in skeletal muscle. It contains fewer mobile elements than its human ortholog, resulting in an increase in the structural stability of the gene sequence.
Results show that PYGM and RAC1 are altered in the dorsolateral prefrontal cortex in chronic schizophrenia and are controlled by NMDA signaling in the rodent cortex and cortical astrocytes suggesting an altered NMDA-dependent glycogenolysis in astrocytes in schizophrenia.
Data suggest that the irreversible inhibition of glycogen phosphorylase (GP) could represent one of the mechanisms that contribute to mercury-dependent muscle toxicity.
this is the first successful attempt to develop a genetically modified animal model of McArdle disease.
Data show that glycogen phosphorylase is irreversibly impaired by exposure to peroxynitrite, and suggest that the peroxynitrite-dependent inactivation of the enzyme could be due to the nitration of Tyr613 at the allosteric inhibitor site of the enzyme.
These results suggest that some conformational changes have taken place in the maltooligosaccharide-binding region of the GP catalytic site during allosteric regulation.
The formation of a complex between the denatured monomeric form of Phb and the dissociated forms of GroEL is detected during heating at 46 degrees C.
alpha-crystallin interacts with the intermediates of unfolding of the Phb molecule
This report expands the phenotype and genotype of McArdle disease and suggests that PYGM mutations should be looked for in patients with very late-onset myopathy with no previous history of exercise intolerance
Because the NMD mechanism does not seem to operate in nonspecific cells, PBMCs were more suitable than muscle biopsies for detecting the pathogenicity of some PYGM mutations, notably the silent mutation whose effect in the splicing of intron 6 was unnoticed in previous muscle transcriptomic studies
Variations in AMPD1, CPT2, and PGYM genes are not associated with the onset, susceptibility, or severity of chronic fatigue syndrome.
update of the reported mutations and polymorphisms in the PYGM gene [review]
study found that T lymphocytes expressed myophosphorylase in healthy donors, but expression was significantly lower in McArdle patients (p<0.001); PYGM mRNA levels were also lower in white blood cells from McArdle patients
biological significance of this PKCtheta;/alphaPIX/Rac 1 GTPase/PYGM signaling pathway seems to be the control of different cellular responses such as migration and proliferation
5 different PYGM mutations were found in 8 Brazilian families: 4 previously described (p.R50X, p.T692kfs30, p.K609K, and p.G455R), and one, pI513V, a novel heterozygous mutation.
a novel mutation, in the PYGM gene c.632delG, in three unrelated families of Jewish descent originating from the Caucasus region
a new role for Rac1 in cell signaling, showing that this GTPase triggers T-cell proliferation upon IL-2 stimulation by associating with PYGM and modulating its enzymatic activity.
No genotype-phenotype correlation is evident and that no gender effect is related to the phenotype of McArdle's disease (PYGM gene) in a cohort of 123 European McArdle's disease patients.
The current data add to the list of pathogenic mutations in the PYGM gene associated with McArdle disease
This study demonistrated that PYGM mutation in McArdle disease.
indicate that in both patients' and controls' cell cultures, unlike in skeletal muscle tissue, most of the protein and GP activities result from the expression of brain GP and liver GP genes
McArdle disease may be caused by a R269X nonsense mutation in this gene.
two new mutations in the myophosphorylase gene in Italian patients with McArdle's disease; both were compound heterozygous, with the common mutation at codon 49 (R49X) on the other allele
molecular genetic study of McArdle's disease in Yemenite-Jewish patients expands the already remarkable genetic heterogeneity of McArdle's disease and suggests the existence of ethnic or private mutations within this group.
In Mcardle's disease (deficiency of this enzyme) efferent muscle sympathetic nerve activity (MSNA) is attenuated.
the muscle subtype of glycogen phosphorylase mRNA level is up-regulated in preeclampsia in placenta
A new autosomal dominant gene mutation in McArdle disease.
Data indicate that a G/T mutation in exon 8 in muscle glycogen phosphorylase (PYGM) was identified and association analysis with meat quality traits showed that it was significantly associated with lean meat percentage(p<0.05).
This gene encodes a muscle enzyme involved in glycogenolysis. Highly similar enzymes encoded by different genes are found in liver and brain. Mutations in this gene are associated with McArdle disease (myophosphorylase deficiency), a glycogen storage disease of muscle. Alternative splicing results in multiple transcript variants.
, glycogen phosphorylase, muscle form
, phosphorylase, glycogen; muscle (McArdle syndrome, glycogen storage disease type V)
, phosphorylase, glycogen. muscle
, Phosphorylase glycogen
, Phosphorylase, glycogen; muscle (McArdle syndrome)
, muscle (McArdle syndrome)
, muscle glycogen phosphorylase
, glycogen myophosphorylase