TRPCs: Influential Mediators in Skeletal Muscle

Choi, Jun Hee; Jeong, Seong-Hae; Oh, Mi Ri; Allen, Paul D.; Lee, Eun Hui

doi:10.3390/cells9040850

Cited by 27 publications

(26 citation statements)

References 198 publications

(230 reference statements)

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“…The presence of SOCE in skeletal muscle was first identified in 2001 122 . There are several differences between SOCE in skeletal muscle cells and general SOCE in another cell types [5][6][7] . First, the SR or t-tubule in skeletal muscle corresponds to the ER or plasma membrane, respectively.…”

Section: A Reverse-directional Signal From Casq1 To Socementioning

confidence: 99%

“…Cytosolic [Ca 2+ ] at rest (nM range) rises to the μM range during skeletal muscle contraction 4 . To establish the Ca 2+ increase, in addition to the Ca 2+ from the SR, extracellular Ca 2+ entry via Ca 2+ channels in the t-tubule membrane, such as Orai1 or transient receptor potential canonical type (TRPC), also participates in the cytosolic Ca 2+ increase, especially for skeletal muscle contraction during tetanic stimulation or fatigue [5][6][7] . The relaxation of skeletal muscle involves the reuptake of Ca 2+ from the cytosol to the SR to reset the resting cytosolic Ca 2+ level and replenish SR Ca 2+ .…”

Section: Introductionmentioning

confidence: 99%

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Calsequestrin: a well-known but curious protein in skeletal muscle

et al. 2020

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Calsequestrin (CASQ) was discovered in rabbit skeletal muscle tissues in 1971 and has been considered simply a passive Ca2+-buffering protein in the sarcoplasmic reticulum (SR) that provides Ca2+ ions for various Ca2+ signals. For the past three decades, physiologists, biochemists, and structural biologists have examined the roles of the skeletal muscle type of CASQ (CASQ1) in skeletal muscle and revealed that CASQ1 has various important functions as (1) a major Ca2+-buffering protein to maintain the SR with a suitable amount of Ca2+ at each moment, (2) a dynamic Ca2+ sensor in the SR that regulates Ca2+ release from the SR to the cytosol, (3) a structural regulator for the proper formation of terminal cisternae, (4) a reverse-directional regulator of extracellular Ca2+ entries, and (5) a cause of human skeletal muscle diseases. This review is focused on understanding these functions of CASQ1 in the physiological or pathophysiological status of skeletal muscle.

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Section: A Reverse-directional Signal From Casq1 To Socementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Calsequestrin: a well-known but curious protein in skeletal muscle

et al. 2020

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“…ATP-driven Ca 2+ pumps pump out Ca 2+ from the cytoplasm, including the sarcoplasmic reticulum (SR) Ca 2+ ATPase that pumps it back into the SR and the plasma membrane Ca 2+ -ATPase ( Brini and Carafoli, 2009 ) that pumps it out of the cytoplasm into the extracellular space. Furthermore [Ca 2+ ] i is also regulated by Ca 2+ influx through TRPC channels ( Choi et al, 2020 ), store-operated Ca 2+ channels ( Lyfenko and Dirksen, 2008 ), the bidirectional and electrogenic Na + /Ca 2+ exchanger in the plasma membrane ( Cifuentes et al, 2000 ; Fraysse et al, 2001 ; Blaustein, 2013 ) and by passive leak from the SR through the ryanodine receptor ( Yang et al, 2007 ; Eltit et al, 2010 ; Andersson et al, 2011 ; Lamboley et al, 2016 ).…”

Section: Discussionmentioning

confidence: 99%

Senescence Is Associated With Elevated Intracellular Resting [Ca2 +] in Mice Skeletal Muscle Fibers. An in vivo Study

2021

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Aging causes skeletal muscles to become atrophied, weak, and easily fatigued. Here, we have tested the hypothesis that normal aging in skeletal muscle cells is associated with Ca2+ intracellular dyshomeostasis and oxidative stress. Intracellular Ca2+ concentration ([Ca2+]i), resting intracellular Na+ concentration ([Na+]i) and reactive oxygen species (ROS) production were measured in vivo (superficial gastrocnemius fibers) using double-barreled ion-selective microelectrodes, and in vitro [isolated single flexor digitorum brevis fibers] using fluorescent ROS sensor CM-H2DCFDA in young (3 months of age), middle-aged (12 months of age), and aged (24 months of age) mice. We found an age-related increase in [Ca2+]i from 121 ± 4 nM in young muscle cells which rose to 255 ± 36 nM in middle-aged and to 409 ± 25 nM in aged cells. [Na+]i also showed an age-dependent elevation, increasing from 8 ± 0.5 mM in young muscle fibers, to 12 ± 1 mM in middle-aged and to 17 ± 1 mM in old muscle fibers. Using the fluorescent ROS sensor CM-H2DCFDA we found that these increases in intracellular cation concentrations were associated with significantly increased basal ROS production as demonstrated by age related increases in the rate of dichlorodihydrofluorescein fluorescence. To determine is this could be modified by reducing ROS and/or blocking sarcolemmal Ca2+ influx we administered flufenamic acid (FFA), a non-steroidal anti-inflammatory drug which is also a non-selective blocker of the transient receptor potential canonical channels (TRPCs), for 4 weeks to determine if this would have a beneficial effect. FFA treatment reduced both basal ROS production and muscle [Ca2+]i and [Na+]i in middle-aged and aged muscle fibers compared to fibers and muscles of untreated 12 and 24-months old mice. [Ca2+]i was reduced to 134 ± 8 nM in middle-aged muscle and to 246 ± 40 nM in muscle from aged mice. Likewise [Na+]i was reduced to 9 ± 0.7 mM in middle-aged muscles and to 13 ± 1 mM in muscle from aged mice. FFA treatment also reduced age associated increases in plasma interleukin 6 and tumor necrosis factor-alpha (TNF-α) concentrations which were elevated in 12 and 24-months old mice compared to young mice and decreased age-related muscle damage as indicated by a reduction in serum creatine kinase (CK) activity. Our data provides a direct demonstration that normal aging is associated with a significant elevation [Ca2+]i, [Na+]i, and intracellular ROS production in skeletal muscle fibers. Furthermore, the fact that FFA reduced the intracellular [Ca2+], [Na+], and ROS production as well as the elevated IL6, TNF-α, and CK levels, led us to suggest that its pharmacological effect may be related to its action both as a TRPC channel blocker and as an anti-inflammatory.

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“…It has been recently suggested that SACs might undergo functional inactivation during unloading, possibly contributing to atrophy establishment [ 218 ]. Among SACs, the stretch-activated and Ca 2+ permeable TRPC1 channel is expressed in skeletal muscle and interacts with α-1-syntrophin PDZ domain and caveolin-3 [ 219 , 220 , 221 , 222 , 223 ]. This channel has been found to be responsible for anomalous extracellular Ca 2+ entry in dystrophic muscle fibers [ 220 , 222 , 223 ].…”

Section: Master Regulators Of Muscle Atrophymentioning

confidence: 99%

“…Among SACs, the stretch-activated and Ca 2+ permeable TRPC1 channel is expressed in skeletal muscle and interacts with α-1-syntrophin PDZ domain and caveolin-3 [ 219 , 220 , 221 , 222 , 223 ]. This channel has been found to be responsible for anomalous extracellular Ca 2+ entry in dystrophic muscle fibers [ 220 , 222 , 223 ]. Downregulation of TRPC1 in adult mouse muscles induces atrophy per se, pointing to a relevant role of this channel in muscle mass regulation [ 224 ].…”

Section: Master Regulators Of Muscle Atrophymentioning

confidence: 99%

Master Regulators of Muscle Atrophy: Role of Costamere Components

Gorza

Sorge

Seclì

et al. 2021

Cells

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The loss of muscle mass and force characterizes muscle atrophy in several different conditions, which share the expression of atrogenes and the activation of their transcriptional regulators. However, attempts to antagonize muscle atrophy development in different experimental contexts by targeting contributors to the atrogene pathway showed partial effects in most cases. Other master regulators might independently contribute to muscle atrophy, as suggested by our recent evidence about the co-requirement of the muscle-specific chaperone protein melusin to inhibit unloading muscle atrophy development. Furthermore, melusin and other muscle mass regulators, such as nNOS, belong to costameres, the macromolecular complexes that connect sarcolemma to myofibrils and to the extracellular matrix, in correspondence with specific sarcomeric sites. Costameres sense a mechanical load and transduce it both as lateral force and biochemical signals. Recent evidence further broadens this classic view, by revealing the crucial participation of costameres in a sarcolemmal “signaling hub” integrating mechanical and humoral stimuli, where mechanical signals are coupled with insulin and/or insulin-like growth factor stimulation to regulate muscle mass. Therefore, this review aims to enucleate available evidence concerning the early involvement of costamere components and additional putative master regulators in the development of major types of muscle atrophy.

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TRPCs: Influential Mediators in Skeletal Muscle

Cited by 27 publications

References 198 publications

Calsequestrin: a well-known but curious protein in skeletal muscle

Calsequestrin: a well-known but curious protein in skeletal muscle

Senescence Is Associated With Elevated Intracellular Resting [Ca2 +] in Mice Skeletal Muscle Fibers. An in vivo Study

Master Regulators of Muscle Atrophy: Role of Costamere Components

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