An alternative dystrophin transcript specific to peripheral nerve

Byers, Timothy J.; Lidov, Hart G.W.; Kunkel, Louis M.

doi:10.1038/ng0593-77

Cited by 260 publications

(177 citation statements)

References 40 publications

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“…In rabbit sciatic nerve extracts, these antibodies stained a 400 kDa band corresponding to utrophin, and a 116 kDa single band corresponding to Dpll6 (Fig. 1B, lane 4), in agreement with previous studies [12,29,30]. The same monoclonal antibodies identified three proteins in Torpedo electrocyte nerve extracts, a 400 kDa protein band and two Mr 116 kDa proteins migrating as a doublet band (Fig.…”

Section: Comparative Western Blot Analyses Of Torpedo and Rabbitsupporting

confidence: 91%

“…1 D, lane 4). This 400 kDa rabbit protein corresponded to utrophin, in agreement with the protein content in rabbit sciatic nerve extracts [12,29,30].…”

Section: Comparative Western Blot Analyses Of Torpedo and Rabbitsupporting

confidence: 82%

“…In addition to the full-length 400 kDa dystrophin, four short dystrophin products (Dps) called Dp71 [11], Dp 116 [12], Dp 140 [13,14] and Dp260 [13,15] have been identified. Their transcripts are derived from the 3' part of the DMD gene using four different internal promoters [11][12][13][14][15]. These short dystrophin products have lost the N-terminal actin binding domain and most of the long spectrin-like rod region of dystrophin, but they retain the cystein-rich and highly conserved C-terminal domains of dystrophin (for review see refs.…”

Section: Introductionmentioning

confidence: 99%

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Presence of long and short dystrophin and/or utrophin products in Torpedo marmorata peripheral nerves

et al. 1996

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Peripheral nerves from rabbit and Torpedo marmorata were comparatively analyzed for the presence of short dystrophin products. Western blot analyses of Torpedo marmorata peripheral nerve extracts revealed the existence of three proteins belonging to the dystrophin family: a M, 400 kDa protein band detected with dystrophin/utrophin, dystrophin-specific and Torpedo utrophin-specific antibodies, a molecule identified as Dpll6 and, for the frst time at the protein level, a new protein probably corresponding to Upll6. All of these products were carefully identified according to the specificities of the monoclonal antibodies used. In immunofluorescence studies, clear staining of the thin rim surrounding each Schwann cell-axon unit was observed in both Torpedo marmorata and rabbit peripheral nerves, showing colocalization of all of these molecules. Their potential functions were discussed in comparison to similar products found in rabbit peripheral nerves.

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Section: Comparative Western Blot Analyses Of Torpedo and Rabbitsupporting

confidence: 91%

“…1 D, lane 4). This 400 kDa rabbit protein corresponded to utrophin, in agreement with the protein content in rabbit sciatic nerve extracts [12,29,30].…”

Section: Comparative Western Blot Analyses Of Torpedo and Rabbitsupporting

confidence: 82%

Section: Introductionmentioning

confidence: 99%

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Presence of long and short dystrophin and/or utrophin products in Torpedo marmorata peripheral nerves

et al. 1996

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“…There are slightly different forms of dystrophin mRNA in different tissues due to different transcription start sites and alternative splicing. [13][14][15] Dystrophin's exact function is not known, but it may be important in maintaining muscle membrane stability. Patients with DMD have very little or no detectable dystrophin whereas BMD patients have dystrophin of altered size and/or less quantity.…”

Section: Gene Studiesmentioning

confidence: 99%

Experience and Strategy for the Molecular Testing of Duchenne Muscular Dystrophy

Prior

Bridgeman

2005

The Journal of Molecular Diagnostics

130

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Mutations in the dystrophin gene result in both Duchenne and Becker muscular dystrophies (DMD and BMD). Approximately two-thirdsDuchenne and Becker muscular dystrophies (DMD and BMD) are X-linked, allelic, neuromuscular diseases characterized by progressive muscular weakness and degeneration of skeletal muscle. DMD is the most common X-linked recessive lethal disease with an incidence of ϳ1 in 3500 newborns, and it has been estimated that approximately one third of the cases result from new mutations.

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“…Several dystrophin and utrophin full-length and shorter isoforms are generated by different promoters and alternative splicing (Fig. 1A) (Feener et al, 1989;Gorecki et al, 1992;Byers et al, 1993;Lidov et al, 1995;Wilson et al, 1999;Jimenez-Mallebrera et al, 2003). Diverse functions of the variants stem from their ability to organize related but distinct membrane-bound glycoprotein complexes consisting of isoforms of syntrophin, dystroglycan, sarcoglycan, and dystrobrevin (Kramarcy et al, 1994;Yang et al, 1995;Rivier et al, 1999;Banks et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Dystrophin and utrophin isoforms are expressed in glia, but not neurons, of the avian parasympathetic ciliary ganglion

2008

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Muscular dystrophy patients often show cognitive impairment, in addition to muscle degeneration caused by dystrophin gene defects. The cognitive impairments lead to speculation that the dystrophin protein family may play a key role at neuronal synapses. Dystrophin regulates the stability of selected GABA A receptor subtypes and α3-containing nicotinic acetylcholine receptors (nAChRs) at a subset of central GABAergic and peripheral sympathetic nicotinic neuron synapses. Similarly, utrophin, the autosomal homologue of dystrophin, is not required for clustering but indirectly stabilizes muscletype nAChRs at the neuromuscular junction. We examined dystrophin and utrophin expression and localization in the avian parasympathetic ciliary ganglion (CG) to determine whether these proteins play a general role at neuronal nicotinic synapses. We have determined that full-length utrophin and dystrophin and the short dystrophin isoform Dp116 are the major isoforms expressed in the CG based on immunoblotting and immunolabeling. Unexpectedly, the cytoskeletal proteins were not detected at nicotinic synapses or in CG neurons. They are expressed in myelinating and non-myelinating Schwann cells. Further, utrophin expression developmentally precedes that of dystrophin. The proteins show partially overlapping distributions, but also differential accumulation along the surface membrane of Schwann cells adjacent to neuronal somata versus axonal processes. Our findings are consistent with reports that dystrophin protein family members function in the maintenance of cellcell interactions and myelination by anchoring the Schwann cell surface membrane to the basal lamina. In contrast, our results differ from those in skeletal muscle and a subset of sympathetic neurons where utrophin and dystrophin localize at nicotinic synapses.

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An alternative dystrophin transcript specific to peripheral nerve

Cited by 260 publications

References 40 publications

Presence of long and short dystrophin and/or utrophin products in Torpedo marmorata peripheral nerves

Presence of long and short dystrophin and/or utrophin products in Torpedo marmorata peripheral nerves

Experience and Strategy for the Molecular Testing of Duchenne Muscular Dystrophy

Dystrophin and utrophin isoforms are expressed in glia, but not neurons, of the avian parasympathetic ciliary ganglion

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