Topic
Triadin
About: Triadin is a research topic. Over the lifetime, 267 publications have been published within this topic receiving 15618 citations. The topic is also known as: CPVT5 & TDN.
Papers published on a yearly basis
Papers
TL;DR: Foot structures have been termed feet and are now commonly known as ryanodine receptor/Ca2+ release channels because of the presence of an intrinsic ci+ channel activity within the feet structures, and their ability to bind the plant.
Abstract: Current evidence suggests that excitable and nonexcitable cells may contain one or both of two intracellular Ca2+ release channels. Release of Ca2+ from intramembrane compartments can be triggered by the binding of the second messenger inositol I ,4,5-trisphosphate (lP3) to the IP3 receptor/Ca2+ release channel (for review, see 6). It also can be mediated by the ryanodine receptor (RyR)/Ca2+ release channel in response to a surface membrane action potential and/or a change in the concentration of a second messenger, by a mechanism referred to in musele as excitation-contraction (E-C) coupling. In striated muscle, rapid release of Ca2+ from the intracellular compart ment, sarcoplasmic reticulum (SR), is initiated by a surface membrane action potential that is communicated to the SR at specialized areas where the junctional SR comes in close contact with the surface membrane or tubular infoldings of the surface membrane (T-tubule); at these areas large protein structures are present that span the gap between the two membrane systems. These structures have been termed feet (see C rranzini-Armstrong & A Jorgensen, this volume) and are now commonly known as ryanodine receptor/Ca2+ release channels because of the presence of an intrinsic ci+ channel activity within the feet structures, and their ability to bind the plant
968 citations
TL;DR: Preliminary data indicate that the protein is unique to sarcoplasmic reticulum and that it is hydrophobically bonded on the interior of these vesicles, and the name Calsequestrin is suggested for the protein.
Abstract: An acidic protein has been extracted from sarcoplasmic reticulum with KCl and deoxycholate. The protein, which remains soluble after extraction, has been highly purified by fractionation on DEAE-cellulose, Sephadex, and hydroxylaptite. It has a molecular weight of 44,000 and contains 392 amino acid residues per molecule, of which 146 are either glutamic or aspartic acid. No phosphorus, sialic acid, or lipid has been detected in the preparation. The protein has been shown to bind up to 970 nmol of Ca++ per mg (43 mol/mol) at pH 7.5, with an apparent dissociation constant of 4 × 10-5 M. Preliminary data indicate that the protein is unique to sarcoplasmic reticulum and that it is hydrophobically bonded on the interior of these vesicles. The protein is believed to play a role in sequestering calcium within sarcoplasmic reticulum. The name Calsequestrin is suggested for the protein.
575 citations
TL;DR: The binding interactions between the cardiac forms of junctin, calsequestrin, triadin, and the ryanodine receptor form a quaternary complex that may be required for normal operation of Ca2+ release.
545 citations
TL;DR: Results suggest that a complex of CSQ, triadin 1, and junctin confer RyR luminal Ca sensitivity, whereas CSQ apparently serves as a luminals Ca sensor that inhibits the channel at low luminal [Ca], whereasTriadin 1 and/or junctIn may be required to mediate interactions of CS Q with RyR.
473 citations
TL;DR: It is shown that Casq2-null mice are viable and display normal SR Ca2+ release and contractile function under basal conditions and phenocopied the human arrhythmias.
Abstract: Cardiac calsequestrin (Casq2) is thought to be the key sarcoplasmic reticulum (SR) Ca2+ storage protein essential for SR Ca2+ release in mammalian heart. Human CASQ2 mutations are associated with catecholaminergic ventricular tachycardia. However, homozygous mutation carriers presumably lacking functional Casq2 display surprisingly normal cardiac contractility. Here we show that Casq2-null mice are viable and display normal SR Ca2+ release and contractile function under basal conditions. The mice exhibited striking increases in SR volume and near absence of the Casq2-binding proteins triadin-1 and junctin; upregulation of other Ca2+-binding proteins was not apparent. Exposure to catecholamines in Casq2-null myocytes caused increased diastolic SR Ca2+ leak, resulting in premature spontaneous SR Ca2+ releases and triggered beats. In vivo, Casq2-null mice phenocopied the human arrhythmias. Thus, while the unique molecular and anatomic adaptive response to Casq2 deletion maintains functional SR Ca2+ storage, lack of Casq2 also causes increased diastolic SR Ca2+ leak, rendering Casq2-null mice susceptible to catecholaminergic ventricular arrhythmias.
462 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2022 | 1 |
| 2021 | 9 |
| 2020 | 6 |
| 2019 | 1 |
| 2018 | 4 |
| 2017 | 10 |