Novel sarco(endo)plasmic reticulum proteins and calcium homeostasis in striated muscles

Divet, Alexandra; Paesante, Silvia; Bleunven, Christophe; Anderson, Ayuk A.; Treves, Susan; Zorzato, Francesco

doi:10.1007/s10974-005-9001-1

Cited by 11 publications

(6 citation statements)

References 71 publications

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“…, 1997). The SR, which is derived from the smooth endoplasmic reticulum and contains a Ca 2+ ‐ storage and ‐ releasing part (terminal cisterna), is enriched in the skeletal muscle cell (Divet et al. , 2005).…”

Section: Discussionmentioning

confidence: 99%

Lipid imaging of human skeletal muscle using TOF‐SIMS with bismuth cluster ion as a primary ion source

Magnusson

Friberg

Sjövall

et al. 2008

Clin Physio Funct Imaging

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SummaryIntramyocellular lipids are of importance in lipid-related diseases. The techniques in this field are limited because of a lack of adequate tools for localization of various lipids. The most usual methods for the localization of lipid distribution in the skeletal muscle are histochemistry and fluorescence probes. Different chromatography methods and mass spectrometry techniques have also been used for lipid identification. Our aim was to localize the spatial distribution of lipids in their native forms by using static time-of-flight secondary-ion mass spectrometry (TOF-SIMS). Human percutaneous skeletal muscle biopsies were obtained from the middle part of the lateral vastus muscle in the right leg of healthy adolescents with a body mass index >30. Samples were prepared by high-pressure freezing, freeze-fracturing and freeze-drying, and analysed by imaging TOF-SIMS equipped with a Bi 3 + cluster ion gun. In the positive spectra, we identified phosphocholine, cholesterol, diacylglycerol, phospholipids and triacylglycerol. Phosphocholine was localized to the edge of the fibre, representing the sarcoplasma or endomysium. Weak cholesterol signals were observed in the intracellular areas. High diacylglycerol and low triacylglycerol signal intensities were seen in intracellular spaces of the transversal area of the muscle fibre. In the negative spectra, we identified fatty acids. We observed co-localization of fatty acids and diacylglycerol, which may indicate lipid-storing parts of the skeletal muscle. Thus, TOF-SIMS imaging can be used to depict the heterogeneous localization of lipids in human skeletal muscle.

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Section: Discussionmentioning

confidence: 99%

Lipid imaging of human skeletal muscle using TOF‐SIMS with bismuth cluster ion as a primary ion source

Magnusson

Friberg

Sjövall

et al. 2008

Clin Physio Funct Imaging

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“…In addition to this DHPR-RyR1 signaling, the RyR1 Ca 2þ release channel is subject to different forms of both extrinsic and intrinsic modulation. For instance, a variety of intracellular factors (such as Ca 2þ , Mg 2þ , calmodulin, and S100A1) extrinsically modulates the RyR1 activity (12)(13)(14)(15)(16).…”

Section: Introductionmentioning

confidence: 99%

Effects of Conformational Peptide Probe DP4 on Bidirectional Signaling between DHPR and RyR1 Calcium Channels in Voltage-Clamped Skeletal Muscle Fibers

Olojo

Hernández‐Ochoa

Ikemoto

et al. 2011

Biophysical Journal

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In skeletal muscle, excitation-contraction coupling involves the activation of dihydropyridine receptors (DHPR) and type-1 ryanodine receptors (RyR1) to produce depolarization-dependent sarcoplasmic reticulum Ca²⁺ release via orthograde signaling. Another form of DHPR-RyR1 communication is retrograde signaling, in which RyRs modulate the gating of DHPR. DP4 (domain peptide 4), is a peptide corresponding to residues Leu²⁴⁴²-Pro²⁴⁷⁷ of the central domain of the RyR1 that produces RyR1 channel destabilization. Here we explore the effects of DP4 on orthograde excitation-contraction coupling and retrograde RyR1-DHPR signaling in isolated murine muscle fibers. Intracellular dialysis of DP4 increased the peak amplitude of Ca²⁺ release during step depolarizations by 64% without affecting its voltage-dependence or kinetics, and also caused a similar increase in Ca²⁺ release during an action potential waveform. DP4 did not modify either the amplitude or the voltage-dependence of the intramembrane charge movement. However, DP4 augmented DHPR Ca²⁺ current density without affecting its voltage-dependence. Our results demonstrate that the conformational changes induced by DP4 regulate both orthograde E-C coupling and retrograde RyR1-DHPR signaling.

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“…RyR1 also enriches the activity of the DHPR through a backward current [53]. RyR1 and RyR2 are also controlled luminally through interactions with calsequestrin, junctin, and triadin [54]. RyR3 was found to co-localize with lysosomes in the perinuclear region of cardiac muscle cells, whereas RyR1 and RyR2 also co-localize with lysosomes they are 2-fold lower and mainly in the sub-plasmalemmal and extra-perinuclear, respectively, where 4- and 60-fold less lysosomal co-localization occurs [55].…”

Section: Er/sr Mediated Calcium Signalingmentioning

confidence: 99%

“…The structure of this interface with associated proteins allows an immense amount of Ca 2+ to be released from the SR in response to action potentials, fueling E-C coupling [29,36,54] This large reservoir of Ca 2+ required to generate contractile force repetitively from a train of action potentials in skeletal muscle cells is maintained by the low affinity, high capacity Ca 2+ binding and release of calsequestrin (CASQ1) [74]. CASQ1 is concentrated in the SR TC where it forms long polymers near the opening of RyR1 in a Ca 2+ dependent manner [75,76].…”

Section: Local Domains Of Er/sr Calcium Releasementioning

confidence: 99%

Calcium Dynamics Mediated by the Endoplasmic/Sarcoplasmic Reticulum and Related Diseases

Reddish

Miller

Gorkhali

et al. 2017

IJMS

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The flow of intracellular calcium (Ca2+) is critical for the activation and regulation of important biological events that are required in living organisms. As the major Ca2+ repositories inside the cell, the endoplasmic reticulum (ER) and the sarcoplasmic reticulum (SR) of muscle cells are central in maintaining and amplifying the intracellular Ca2+ signal. The morphology of these organelles, along with the distribution of key calcium-binding proteins (CaBPs), regulatory proteins, pumps, and receptors fundamentally impact the local and global differences in Ca2+ release kinetics. In this review, we will discuss the structural and morphological differences between the ER and SR and how they influence localized Ca2+ release, related diseases, and the need for targeted genetically encoded calcium indicators (GECIs) to study these events.

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Novel sarco(endo)plasmic reticulum proteins and calcium homeostasis in striated muscles

Cited by 11 publications

References 71 publications

Lipid imaging of human skeletal muscle using TOF‐SIMS with bismuth cluster ion as a primary ion source

Lipid imaging of human skeletal muscle using TOF‐SIMS with bismuth cluster ion as a primary ion source

Effects of Conformational Peptide Probe DP4 on Bidirectional Signaling between DHPR and RyR1 Calcium Channels in Voltage-Clamped Skeletal Muscle Fibers

Calcium Dynamics Mediated by the Endoplasmic/Sarcoplasmic Reticulum and Related Diseases

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