Expression of a cardiac Ca2+-release channel isoform in mammalian brain

Lai, F. Anthony; Dent, Myrna A. R.; Wickenden, Colin; Xu, Le; Kumari, G.L.; Misra, Manoj; Lee, H. B.; Sar, Madhabananda; Meissner, Gerhard

doi:10.1042/bj2880553

Cited by 94 publications

(60 citation statements)

References 64 publications

(63 reference statements)

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“…Since we routinely used calcium concentrations up to 0 5 mM, we cannot discard the possibility that higher calcium c,,ncentrations will inhibit the calcium-stimulated channels of b ain cortex as well. It remains to be established whether this c tannel behavior reflects the presence in our isolated vesicles o'the ryanodine receptor-2 isoform, which is present in high d :nsity in rat brain cortex [9,11].…”

Section: Resultsmentioning

confidence: 99%

“…High conductance (= 100 pS) ryanodinesensitive calcium channels present in rat [10], bovine [11], and r~tbbit [5] brain have been studied after fusion with planar li~id bilayers; these channels are activated by millimolar *Corresponding author. Fax: (56) (2) 7776916.…”

Section: Introductionmentioning

confidence: 99%

“…ATP [5,10,11], caffeine [5] and micromolar IP3 [10,11]. Micromolar calcium activates a ryanodine receptor purified from bovine brain that corresponds to the cardiac isoform [11].…”

Section: Introductionmentioning

confidence: 99%

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Calcium dependence of ryanodine‐sensitive calcium channels from brain cortex endoplasmic reticulum

1996

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Calcium dependence of ryanodine‐sensitive calcium channels from brain cortex endoplasmic reticulum

1996

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“…In situ hybridization and immunolocalization studies have revealed a cell type-specific pattern of expression in the different regions of the central nervous system (37)(38)(39)(40). Several recent studies have provided evidence that RyRs are under strict …”

Section: Ortho-substituted Pcbs Alter Ca 2ϩ Regulation In Rat Brain Bmentioning

confidence: 99%

ortho-Substituted Polychlorinated Biphenyls Alter Microsomal Calcium Transport by Direct Interaction with Ryanodine Receptors of Mammalian Brain

Wong

Brackney

Pessah

1997

Journal of Biological Chemistry

105

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A stringent structure-activity relationship among polychlorinated biphenyls (PCBs) possessing two or more ortho-chlorine substituents is observed for activation of ryanodine receptors in mammalian brain, revealing an arylhydrocarbon receptor-independent mechanism through which non-coplanar PCBs disrupt neuronal Ca 2؉ signaling. Of the congeners assayed, noncoplanar PCB 95 exhibits the highest potency (EC 50 Along with the genetically related inositol 1,4,5-trisphosphate receptors (IP 3 Rs), 1 ryanodine receptors (RyRs) are Ca 2ϩ -selective ion channels which regulate the release of Ca 2ϩ from endoplasmic reticulum (ER) during cell activation. Mobilization of ER Ca 2ϩ is essential for determining the amplitude, spatial and temporal fluctuation of intracellular Ca 2ϩ , thereby providing important signaling information to the cell (1). In consonance with their fundamental role in cellular Ca 2ϩ signaling, skeletal (Ry 1 R) and brain (Ry 3 R) isoforms of RyRs possess a cytoskeletal binding motif which could confer a structural and functional association with L-type voltage-dependent Ca 2ϩ entry channels in skeletal muscle (2-5). Data supporting direct coupling of neuronal L-type voltage-dependent Ca 2ϩ entry and RyRs has been recently provided (6). Most significant is the finding that expression of Ry 1 R cDNA in dyspedic muscle cells, which lack constitutive expression of Ry 1 R, restores not only excitation-contraction coupling but also restores L-type voltage-dependent Ca 2ϩ entry (5). Thus mechanical coupling between RyRs and voltage-gated Ca 2ϩ channels within the surface membrane appears to confer reciprocal regulation, a finding that may have broad significance in neuronal cell functions.Polychlorinated biphenyls (PCBs), polychlorinated dibenzop-dioxins and polychlorinated dibenzofurans are commonly known as halogenated aromatic hydrocarbons (HAHs), a family of persistent and widely dispersed environmental contaminants. The unique chemical properties and low cost of producing PCBs have contributed to their extensive industrial use (7,8). The high lipophilicity and chemical stability of PCBs have further resulted in widespread environmental contamination, and there is significant evidence of PCBs accumulation in biota (9). PCBs are found in extracts of virtually all environmental samples as well as in human tissue and breast milk (10,11).Among the HAHs various congeners differentially confer ability to bind to a cytosolic receptor, the arylhydrocarbon receptor (AhR). 2,3,7, binds to the receptor with the highest affinity and confers the highest potency to induce certain toxic responses, such as wasting syndrome, immunosuppression, and teratogenicity. PCB congeners without ortho-chlorine substitutions are able to confer the coplanar structure similar to TCDD and elicit similar toxicity. PCB congeners with single ortho-chlorine slightly favor the non-coplanarity and behave as weak AhR agonists. PCB congeners with two or more ortho-chlorines highly favor the non-coplanar conformation; thus, this group of congene...

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“…Recently a splice variant of RyR2 was identified in the heart that increases susceptibility to apoptosis (Valdivia 2007). RyR2 is also expressed at high levels in Purkinje cells of cerebellum and cerebral cortex (Lai et al 1992;Nakanishi et al 1992;Sharp et al 1993;Furuichi et al 1994) and in low levels in stomach, kidney, adrenal glands, ovaries, thymus, and lungs Giannini et al 1995).…”

Section: Expression Of Ryanodine Receptorsmentioning

confidence: 99%

Ryanodine Receptors: Structure, Expression, Molecular Details, and Function in Calcium Release

Lanner¹,

Georgiou²,

Joshi³

et al. 2010

Cold Spring Harbor Perspectives in Biology

648

572

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Ryanodine receptors (RyRs) are located in the sarcoplasmic/endoplasmic reticulum membrane and are responsible for the release of Ca 2þ from intracellular stores during excitation-contraction coupling in both cardiac and skeletal muscle. RyRs are the largest known ion channels (.2MDa) and exist as three mammalian isoforms (RyR 1 -3), all of which are homotetrameric proteins that interact with and are regulated by phosphorylation, redox modifications, and a variety of small proteins and ions. Most RyR channel modulators interact with the large cytoplasmic domain whereas the carboxy-terminal portion of the protein forms the ion-conducting pore. Mutations in RyR2 are associated with human disorders such as catecholaminergic polymorphic ventricular tachycardia whereas mutations in RyR1 underlie diseases such as central core disease and malignant hyperthermia. This chapter examines the current concepts of the structure, function and regulation of RyRs and assesses the current state of understanding of their roles in associated disorders.

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Expression of a cardiac Ca2+-release channel isoform in mammalian brain

Cited by 94 publications

References 64 publications

Calcium dependence of ryanodine‐sensitive calcium channels from brain cortex endoplasmic reticulum

Calcium dependence of ryanodine‐sensitive calcium channels from brain cortex endoplasmic reticulum

ortho-Substituted Polychlorinated Biphenyls Alter Microsomal Calcium Transport by Direct Interaction with Ryanodine Receptors of Mammalian Brain

Ryanodine Receptors: Structure, Expression, Molecular Details, and Function in Calcium Release

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