Neuron
ArticleLocalization of the α1 and α2 subunits of the dihydropyridine receptor and ankyrin in skeletal muscle triads
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Cited by (83)
Calcium Influx and Release Cooperatively Regulate AChR Patterning and Motor Axon Outgrowth during Neuromuscular Junction Formation
2018, Cell ReportsCitation Excerpt :The voltage-gated calcium channel CaV1.1 (also called dihydropyridine receptor [DHPR]) functions as voltage sensor for EC coupling (Ríos and Pizarro, 1991). It is located in the triads—junctions between the sarcoplasmic reticulum (SR) and t-tubules—where CaV1.1 interacts with the SR calcium release channel (type 1 ryanodine receptor [RyR1]; Block et al., 1988; Franzini-Armstrong et al., 1999; Flucher et al., 1990). Upon membrane depolarization, conformational changes of CaV1.1 directly translate into the activation of the RyR1, thus triggering depolarization-induced calcium release from the SR (Melzer et al., 1995).
Kir2.6 Regulates the surface expression of Kir2.x inward rectifier potassium channels
2011, Journal of Biological ChemistryCitation Excerpt :Kir2.2 was present in transverse striations with a distribution that extended into the center of muscle fibers (Fig. 6B). Colabeling with antibodies to markers indicated that these striations corresponded to T-tubules (47); Kir2.2 labeling resolved as double transverse rows that colocalize with rows of DHPR (Fig. 6B, insets, arrowheads), that bracket the Z-line identified with anti-α-actinin (Fig. 6B), and that are slightly narrower than double rows of ryanodine receptor (not shown). Interestingly, the distribution of both Kir2.1 and Kir2.2 was punctate along the T-tubules and appeared adjacent to and with some overlap with DHPR, suggesting that the Kir2 channels and DHPR are spatially segregated in discrete clusters on the T-tubules.
RyRs: Their disposition, frequency, and relationships with other proteins of calcium release units
2010, Current Topics in MembranesCitation Excerpt :Surprisingly, the small bCaV1 subunit is also essential for the RyR1–Cav1.1 association (Schredelseker et al., 2005). In the absence of a1, the channel region of the complex, a2 fails to target to CRUs (Flucher, Morton, Froehner, & Daniels, 1990). The reverse is not true: in the absence of the a2 subunit, CaV1.1 are present in CRUs and they link to RyR1 forming tetrads (Gach et al., 2008).
Skeletal muscle tissue engineering: A maturation model promoting long-term survival of myotubes, structural development of the excitation-contraction coupling apparatus and neonatal myosin heavy chain expression
2009, BiomaterialsCitation Excerpt :This clustering of the AChR receptors, which are induced by the motoneuron protein agrin in vivo, are locations on the myotube where neuromuscular junction formation occurs and another indication of functional myotube formation. The presence of the ryanodine (RyR) receptor and dihydropyridine (DHPR) receptor clusters, as well as their colocalization in vivo, represents the development of excitation–contraction coupling apparatus in skeletal muscle myotubes [8,9,24]. The clustering of both RyR and DHPR receptors was observed on the myotubes after 30 days in culture (Fig. 5 A–D).
Molecular architecture of the sarcoplasmic reticulum and its role in the ECC
2009, NeurochirurgieImmunostaining of rat brain, spinal cord, sensory neurons and skeletal muscle for calcium channel alpha<inf>2</inf>-delta (α<inf>2</inf>-δ) type 1 protein
2008, NeuroscienceCitation Excerpt :Immunoblotting of various proteins was used to investigate the specificity of the α2-δ-1 monoclonal antibody (Sigma-Aldrich, St. Louis, MO, USA; catalog # D-219, anti-dihydropyridine receptor (α2 subunit) clone 20A). This antibody was derived from an antibody made in mice against α2-δ-1 protein purified from rabbit skeletal muscle (Flucher et al., 1990). Recombinant porcine α2-δ-1 and human α2-δ-2 proteins were stably expressed in Cos-7 and GKS07 mammalian cell lines (respectively), and harvested cell paste with high concentrations of the respective α2-δ subunits was used to provide relatively pure α2-δ subtype proteins, as previously described (Wang et al., 1999).
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Present address: Department of Pharmacology, University of Washington, Seattle, Washington, 98195.