Dystrophin and its isoforms in a sympathetic ganglion of normal and dystrophic mdx mice: immunolocalization by electron microscopy and biochemical characterization

Stefano, Maria Egle De; Zaccaria, Maria Letizia; Cavaldesi, Michaela; Petrucci, Tamara C.; Medori, Rossella; Paggi, Paola

doi:10.1016/s0306-4522(97)00003-1

Cited by 22 publications

(31 citation statements)

References 43 publications

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“…ß 2003 Dystrophin, a protein of molecular weight 427,000 Da, is encoded by a gene mapped on the X (locus p21) chromosome. By means of alternative promoters or differential splicing, the same gene also encodes for other shorter isoforms whose molecular weight ranges from 260,000 to 40,000 Da (Ahn and Kunkel, 1994;Fabbrizio et al, 1994;De Stefano et al, 1997;Rivier et al, 1997;Jancsik and Hajos, 1998), thus the largest isoform is also called full-length dystrophin.…”

mentioning

confidence: 99%

Synaptic vesicle morphology and recycling are altered in myenteric neurons of mice lacking dystrophin (mdx mice)

Vannucchi

Corsani

Faussone–Pellegrini

2003

Journal Cellular Physiology

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Several dystrophin isoforms are known. The full-length isoform is present in striated and smooth muscles and neurons and its lack causes Duchenne Muscular Dystrophy, a progressive myopathy accompanied by mild cognitive deficits and gastrointestinal dismotility. An ultrastructural study was undertaken in the colon of mice lacking full-length dystrophin and maintaining shorter isoforms (mdx mice) to ascertain whether myenteric neurons have an altered morphology. Results showed a significant increase in the size of synaptic vesicle and in the number of recycling vesicles. An enlargement of endoplasmic reticulum cisternae in a subpopulation of neurons was also seen. Immunohistochemistry confirmed that the shorter isoforms were expressed in mdx mice myenteric neurons. These findings indicate the presence of a neuropathy at the myenteric plexus which might justify the defective neuronal control of gastrointestinal motility reported for these animals and which might be correlated with full-length dystrophin loss, since the shorter isoforms are present.

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mentioning

confidence: 99%

Synaptic vesicle morphology and recycling are altered in myenteric neurons of mice lacking dystrophin (mdx mice)

Vannucchi

Corsani

Faussone–Pellegrini

2003

Journal Cellular Physiology

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“…In these studies, however, rapsyn immunoreactivity was not detected in ganglionic neurons (137,208). neurons (210)(211)(212)(213). In addition to the muscle type, a number of short forms of dystrophin-related gene products that still carry critical interaction domains with other D/UGC proteins have been identified in the nervous system, although functional roles of those are not clear (192,212,214,215).…”

Section: Rapsyn Is Not Required For Clustering Of Ganglionic Achrsmentioning

confidence: 84%

“…neurons (210)(211)(212)(213). In addition to the muscle type, a number of short forms of dystrophin-related gene products that still carry critical interaction domains with other D/UGC proteins have been identified in the nervous system, although functional roles of those are not clear (192,212,214,215). There exists some evidence that these different gene products are localized at different synaptic sites (212).…”

Section: Rapsyn Is Not Required For Clustering Of Ganglionic Achrsmentioning

confidence: 99%

Clustering of Nicotinic Acetylcholine Receptors: From the Neuromuscular Junction to Interneuronal Synapses

Huh

Fuhrer

2002

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Fast and accurate synaptic transmission requires high-density accumulation of neurotransmitter receptors in the postsynaptic membrane. During development of the neuromuscular junction, clustering of acetylcholine receptors (AChR) is one of the first signs of postsynaptic specialization and is induced by nerve-released agrin. Recent studies have revealed that different mechanisms regulate assembly vs stabilization of AChR clusters and of the postsynaptic apparatus. MuSK, a receptor tyrosine kinase and component of the agrin receptor, and rapsyn, an AChR-associated anchoring protein, play crucial roles in the postsynaptic assembly. Once formed, AChR clusters and the postsynaptic membrane are stabilized by components of the dystrophin/utrophin glycoprotein complex, some of which also direct aspects of synaptic maturation such as formation of postjunctional folds. Nicotinic receptors are also expressed across the peripheral and central nervous system (PNS/CNS). These receptors are localized not only at the pre-but also at the postsynaptic sites where they carry out major synaptic transmission. In neurons, they are found as clusters at synaptic or extrasynaptic sites, suggesting that different mechanisms might underlie this specific localization of nicotinic receptors. This review summarizes the current knowledge about formation and stabilization of the postsynaptic apparatus at the neuromuscular junction and extends this to explore the synaptic structures of interneuronal cholinergic synapses.

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“…This relationship may partially explain the changes in nNOS expression in the sarcolemma of mdx muscles, as we observed here, but cannot explain the decrease in nNOS in the presynaptic region. Dystrophin and Cterminal isoforms of dystrophin (particularly Dp116) are expressed in Schwann cells of the sciatic nerve (Byers et al 1993 ;Fabbrizio et al 1995) and of the mouse superior cervical ganglion (De Stefano et al 1997). However, the mutation in mdx mice apparently does not affect the expression of dystrophin and its isoforms, at least in the superior cervical ganglia (De Stefano et al 1997).…”

Section: mentioning

confidence: 99%

“…Dystrophin and Cterminal isoforms of dystrophin (particularly Dp116) are expressed in Schwann cells of the sciatic nerve (Byers et al 1993 ;Fabbrizio et al 1995) and of the mouse superior cervical ganglion (De Stefano et al 1997). However, the mutation in mdx mice apparently does not affect the expression of dystrophin and its isoforms, at least in the superior cervical ganglia (De Stefano et al 1997). We are therefore unsure how ' dystrophin deficient ' the presynaptic region of mdx mice really is.…”

Section: mentioning

confidence: 99%

Immunolocalisation of neuronal nitric oxide synthase at the neuromuscular junction of MDX mice: a confocal microscopy study

2001

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The distribution of nitric oxide synthase at the neuromuscular junction (NMJ) of normal, denervated and mdx mice was studied using a specific antibody against the neuronal isoform of nitric oxide synthase (nNOS). Fluorescence confocal microscopy demonstrated that nNOS immunoreactivity was localised mainly in the sarcolemma and presynaptic region covering acetylcholine receptor branches. The expression of presynaptic nNOS was greatly reduced in dystrophin-deficient muscles. In normal denervated muscles, nNOS was still present in the presynaptic region and there were no qualitative changes in the expression of this protein. These results suggest that the presynaptic distribution of nNOS is associated with terminal Schwann cells. The relationship between nNOS and the presynaptic components of the neuromuscular junction may open new perspectives for improving our understanding of the pathogenesis of dystrophic muscles.

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Dystrophin and its isoforms in a sympathetic ganglion of normal and dystrophic mdx mice: immunolocalization by electron microscopy and biochemical characterization

Cited by 22 publications

References 43 publications

Synaptic vesicle morphology and recycling are altered in myenteric neurons of mice lacking dystrophin (mdx mice)

Synaptic vesicle morphology and recycling are altered in myenteric neurons of mice lacking dystrophin (mdx mice)

Clustering of Nicotinic Acetylcholine Receptors: From the Neuromuscular Junction to Interneuronal Synapses

Immunolocalisation of neuronal nitric oxide synthase at the neuromuscular junction of MDX mice: a confocal microscopy study

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