Modulation of acetylcholine receptor function in TE671 (rhabdomyosarcoma) cells by non-AChR ligands: possible relevance to seronegative myasthenia gravis

Li, Zhuyi; Forester, Nerys; Vincent, Angela

doi:10.1016/0165-5728(95)00169-7

Cited by 31 publications

(16 citation statements)

References 27 publications

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“…The second highest ranking protein was cAMP-dependent protein kinase catalytic subunit alpha isoform 1 (PRKACA). This protein is known to phosphorylate and inhibit acetylcholine receptor functioning and affect the disease (Li et al, 1996;Plested et al, 2002). LGALS3BP INSR HLA-B PEX6 ZMYM2 PRKACA INSR GJA1 PPP1R2 CD46 GUCY2C HLA-A POU4F2 CD46 CALCOCO1 ITGAL EBF1 GRLF1 ZDHHC4 GATA3 GYS1…”

Section: Application To Myasthenia Gravismentioning

confidence: 99%

A Network-Based Method for Predicting Disease-Causing Genes

Karni

Soreq

Sharan

2009

Journal of Computational Biology

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A fundamental problem in human health is the inference of disease-causing genes, with important applications to diagnosis and treatment. Previous work in this direction relied on knowledge of multiple loci associated with the disease, or causal genes for similar diseases, which limited its applicability. Here we present a new approach to causal gene prediction that is based on integrating protein-protein interaction network data with gene expression data under a condition of interest. The latter are used to derive a set of disease-related genes which is assumed to be in close proximity in the network to the causal genes. Our method applies a set-cover-like heuristic to identify a small set of genes that best "cover" the disease-related genes. We perform comprehensive simulations to validate our method and test its robustness to noise. In addition, we validate our method on real gene expression data and on gene specific knockouts. Finally, we apply it to suggest possible genes that are involved in myasthenia gravis.

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Section: Application To Myasthenia Gravismentioning

confidence: 99%

A Network-Based Method for Predicting Disease-Causing Genes

Karni

Soreq

Sharan

2009

Journal of Computational Biology

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“…Thymoma is present in 15% of MG patients [44]. AChR antibodies impair neuromuscular transmission by complement-mediated postsynaptic membrane damage, direct blockade of ligand-receptor interaction, and/or by cross-linking of AChR and increased degradation [41,45]. Antibodies to muscle-specific kinase (MuSK) are observed in a minority of MG patients [46,47].…”

Section: Serum Levels Of Mmps In Mgmentioning

confidence: 99%

Serum Levels of Matrix Metalloproteinases: Implications in Clinical Neurology

Romi

Helgeland²,

Gilhus³

2012

Eur Neurol

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Matrix metalloproteinases (MMPs) are zinc-dependent enzymes involved in remodeling extracellular matrix and cell-matrix interactions. A pathogenic role of MMPs in neurological disorders is likely. This paper focuses on serological clinical aspects only. In multiple sclerosis, higher serum MMP-3 is seen during relapses. Lower serum MMP-8 and -9 levels correlate with fewer contrast-enhanced T₂-weighted MRI lesions, and serum MMP-9 can be used in monitoring treatment. In myasthenia gravis, serum MMP-2, -3, and -9 levels are elevated in both generalized and ocular diseases. A proportion of the patients have markedly increased serum MMP-3. In acute stroke, higher serum MMP-9 correlates with larger infarct volume, stroke severity, and worse functional outcome, and serum MMP-3 is significantly lower than in several other neurological disorders and healthy controls. In amyotrophic lateral sclerosis, serum MMP-2 correlates with disease progression, and both serum MMP-1 and -2 are elevated. In Alzheimer’s disease, serum MMP-3, -9, and -10 are elevated. In migraine, serum MMP-2 is elevated, and also MMP-9 in those patients with migraine without aura. MMP-9 is implicated in the pathogenesis of experimental epilepsy. A pathogenic role of MMPs in these conditions could be related to their ability to degrade extracellular matrix. MMPs may also facilitate autoimmunity.

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“…10 On the other hand, recent evidence suggests that SNMG patients have antibodies against some other cell surface determinant that indirectly affects AChR function, and that this is likely to involve activation of a second messenger pathway and AChR phosphorylation. 8,9,11 If this is the case, one would expect SNMG IgG to bind to muscle cell lines but not necessarily to nonmuscle cell lines, even if the latter were induced to express AChR.…”

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confidence: 99%