Neuron
ArticleDevelopmental regulation of highly active alternatively spliced forms of agrin
References (32)
- et al.
Agrin mediates cell contact-induced acetylcholine receptor clustering
Cell
(1991) - et al.
RNA splicing regulates agrin-mediated acetylcholine receptor clustering activity on cultured myotubes
Neuron
(1992) - et al.
Basal lamina components are concentrated in premuscle masses and at early acetylcholine receptor clusters in chick embryo hindlimb muscles
Dev. Biol.
(1988) - et al.
Glycosaminoglycan variants in the C2 muscle cell line
Dev. Biol.
(1989) - et al.
Synaptic structure and development: the neuromuscular junction
Cell
(1993)et al.Synaptic structure and development: the neuromuscular junction
Neuron
(1993) - et al.
Muscle-derived agrin in cultured myotubes: expression in the basal lamina and at induced acetylcholine receptor clusters
Dev. Biol.
(1992) - et al.
Motor neurons contain agrin-like molecules
J. Cell Biol.
(1988) - et al.
Agrin-like molecules at synaptic sites in normal, denervated, and damaged skeletal muscles
J. Cell Biol.
(1987) - et al.
On the mechanism of acetylcholine receptor accumulation at newly formed synapses of chick myotubes
J. Neurosci.
(1985) - et al.
Structure and expression of a rat agrin
Neuron
(1991)
Structure and chromosomal localization of the mammalian agrin gene
J. Neurosci.
Agrin-induced specializations contain cytoplasmic, membrane, and extracellular matrix-associated components of the postsynaptic apparatus
J. Neurosci.
Redistribution of acetylcholine receptors on developing rat myotubes
J. Neurosci.
Neurotransmitter synthesis by neuroblastoma clones
Nerve-induced and spontaneous redistribution of acetylcholine receptors on cultured muscle cells
J. Physiol.
Differentiated rat glial cell strain in tissue culture
Science
Cited by (182)
A first-in-human phase I/IIa gene transfer clinical trial for Duchenne muscular dystrophy using rAAVrh74.MCK.GALGT2
2022, Molecular Therapy Methods and Clinical DevelopmentCitation Excerpt :The rAAVrh74.MCK.GALGT2 vector contains a transgene encoding human GALGT2—alternatively called B4GALNT2—expressed under control of the skeletal and cardiac muscle-specific MCK promoter. In adult skeletal muscle, the GALGT2 protein acts as a β1,4 N-acetylgalactosaminyltransferase to glycosylate α-dystroglycan,10,11,12,13,14,15,16,17,18 and it expression is normally confined to the neuromuscular and myotendinous junctions, analogous to the similar domain-restricted expression of other synaptic dystroglycan-binding proteins, such as utrophin, plectin 1f, laminin α4, laminin α5, and agrin, in adult skeletal muscle.19,20,21,22,23,24 Multiple lines of evidence provide a rationale for its use in DMD patients.
rAAVrh74.MCK.GALGT2 Demonstrates Safety and Widespread Muscle Glycosylation after Intravenous Delivery in C57BL/6J Mice
2019, Molecular Therapy Methods and Clinical DevelopmentCitation Excerpt :In adult skeletal muscle, expression of GALGT2 is confined to the neuromuscular and myotendinous junction, and its expression is also very low in the heart.10–12 The confinement of GALGT2 to specialized subdomains of the skeletal myofiber, which contains hundreds of nuclei, is similar to that of other synaptic dystroglycan-binding proteins, including utrophin, plectin 1f, laminin α4, laminin α5, and agrin.13–18 When overexpressed in skeletal muscle, GALGT2 induces glycosylation of α dystroglycan and increases the ectopic expression of its normally synaptic binding partners, many of which can inhibit the development of muscular dystrophy when overexpressed.1,12,19,20
Alternative Splicing and the Intracellular Domain Mediate TM-agrin's Ability to Differentially Regulate the Density of Excitatory and Inhibitory Synapse-like Specializations in Developing CNS Neurons
2019, NeuroscienceCitation Excerpt :In the present study, we provide evidence that the effects of TM-agrin on excitatory and inhibitory synapse-like specializations are mediated by distinct regions within the TM-agrin protein and that presynaptic specializations are similarly affected. At the NMJ, only agrin isoforms that contain a peptide insert of 8, 11 or 19 amino acids at splice site z are synaptogenic through their direct high-affinity binding to Lrp4 (Ruegg et al., 1992; Hoch et al., 1993; Gesemann et al., 1996; Zong et al., 2012). Likewise, TM-agriny4z8 is able to induce AChR aggregates in cultured myotubes (Neumann et al., 2001), suggesting that the appropriate TM-agrin isoform can also interact with Lrp4.
Agrin requires specific proteins to selectively activate γ-aminobutyric acid neurons for pain suppression
2014, Experimental NeurologyAcetylcholinesterase and agrin: Different functions, similar expression patterns, multiple roles
2013, Chemico-Biological Interactions