Prolonged exercise induces structural changes in SR Ca2+-ATPase of rat muscle

Luckin, Kristen A.; Favero, Terence G.; Klug, G. A.

doi:10.1016/0885-4505(91)90087-2

Cited by 62 publications

(87 citation statements)

References 47 publications

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“…Although a number of cytoplasmic regions of SERCA1a are sensitive to oxidants and are modified by exposure to ROS (16), numerous studies support the view that ROS can inactivate SERCAs by inducing structural alterations to the nucleotidebinding site (17,36,47,48,55). By using a FITC binding assay, we tested the hypothesis that modification of a region of the N domain containing the nucleotide-binding site is responsible for thermal inactivation of SERCA1a.…”

Section: Discussionmentioning

confidence: 99%

“…Inactivation of SERCA1a activity with oxidative stress has been associated with structural modification to the N domain as indicated by reductions in FITC binding capacity (17,18,36,47,48). Moreover, it has been shown that thermal inactivation of SERCA1a activity is because of denaturation of the N domain (11).…”

Section: Fitc Binding Capacity-fitc Covalently Labels Lysmentioning

confidence: 99%

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HSP70 Binds to the Fast-twitch Skeletal Muscle Sarco(endo)plasmic Reticulum Ca2+-ATPase (SERCA1a) and Prevents Thermal Inactivation

Tupling

Gramolini²,

Duhamel

et al. 2004

Journal of Biological Chemistry

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This study examined whether HSP70 could bind to and protect against thermal inactivation of SERCA1a, the SERCA isoform expressed in adult fast-twitch skeletal muscle. Sarcoplasmic reticulum vesicles prepared from rat gastrocnemius muscle were incubated with purified HSP70 at both 37 and 41°C for either 30, 60, or 120 min. Maximal SERCA1a activity (mol/g protein/min) in the absence of HSP70 was reduced progressively with time, with greater reductions occurring at 41°C compared with 37°C. HSP70 protected against thermal inactivation of SERCA1a activity at 37°C but not at 41°C and only at 30 and 60 min but not at 120 min. HSP70 also protected against reductions in binding capacity for fluorescein isothiocyanate, a fluorescent probe that binds to Lys 515 in the nucleotide binding domain of SERCA, at 30 and 60 min but not at 120 min, an effect that was independent of temperature. HEK-293 cells were cotransfected with cDNAs encoding rabbit SERCA1a and human HSP-EYFP and subjected to 40°C for 1 h. Immunohistochemistry revealed nearly complete co-localization of SERCA1a with HSP70 under these conditions. Co-immunoprecipitation showed physical interaction between HSP70 and SERCA1a under all thermal conditions both in vitro and in HEK-293 cells. Modeling showed that the fluorescein isothiocyanate-binding site of intact SERCA1a in the E2 form lies in its close proximity to a potential interaction site between SERCA1a and HSP70. These results indicate that HSP70 can bind to SERCA1a and, depending on the severity of heat stress, protect SERCA1a function by stabilizing the nucleotide binding domain. Sarco(endo)plasmic reticulum Ca2ϩ -ATPases (SERCAs) 1 are 110-kDa integral membrane proteins that catalyze the ATPdependent transport of Ca 2ϩ from the cytosol to the lumen of the sarco(endo)plasmic reticulum (SR) (1). Two SERCA isoforms predominate in adult striated muscle, namely SERCA1a and SERCA2a. SERCA1a accounts for more than 99% of the SERCA isoforms expressed in adult fast-twitch skeletal muscle, whereas SERCA2a is the major isoform expressed in heart and slow-twitch skeletal muscle (2). In muscle, SERCAs perform at least two crucial functions obligatory for precise control of intracellular Ca 2ϩ . In conjunction with plasma membrane Ca 2ϩ -ATPases, SERCAs are responsible for setting resting cytoplasmic Ca 2ϩ concentrations, and during repetitive muscle contractions, they induce muscle relaxation through the rapid sequestration of large Ca 2ϩ loads from the cytoplasm into the lumen of the SR, thereby determining the size of the SR Ca 2ϩ

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Section: Discussionmentioning

confidence: 99%

Section: Fitc Binding Capacity-fitc Covalently Labels Lysmentioning

confidence: 99%

HSP70 Binds to the Fast-twitch Skeletal Muscle Sarco(endo)plasmic Reticulum Ca2+-ATPase (SERCA1a) and Prevents Thermal Inactivation

Tupling

Gramolini²,

Duhamel

et al. 2004

Journal of Biological Chemistry

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“…Hence, both muscle glycogen and SR Ca 2+ release rate remained depressed in the H 2 O group whereas muscle glycogen and SR Ca 2+ release were significantly elevated in the CHO group in comparison to the Post measurement. (10,26) and unaltered (19,33) following exercise. These discrepancies in research may be related to the exercise mode and training status of individuals.…”

Section: Figure 1 and 2 Near Herementioning

confidence: 94%

Muscle Glycogen Content Modifies SR Ca2+ Release Rate in Elite Endurance Athletes

Gejl

Hvid

Frandsen

et al. 2014

Medicine &Amp; Science in Sports &Amp; Exercise

102

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“…Luminal Ca 2ϩ content is dependent on several factors including, but not limited to, function of the SR Ca 2ϩ ATPase, leakiness of the SR membrane and/or RYR channel, and the total amount of Ca 2ϩ released that is a function of duration and frequency of the contractile protocol. Inhibition of the SR ATPase (22,91) and reductions in Ca 2ϩ accumulation by SR have been demonstrated after exhaustive running in rats (22,78), in single-fiber experiments (135,141), and in exercising humans (17). Evidence suggests that with prolonged stimulation resting intracellular Ca 2ϩ concentrations are significantly elevated (89).…”

Section: Sr Ca 2ϩ Release From An Experimental Perspectivementioning

confidence: 99%

Sarcoplasmic reticulum Ca²⁺release and muscle fatigue

Favero

1999

Journal of Applied Physiology

108

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Efforts to examine the relevant mechanisms involved in skeletal muscle fatigue are focusing on Ca2+ handling within the active muscle cell. It has been demonstrated time and again that reductions in sarcoplasmic reticulum (SR) Ca2+release resulting from increased or intense muscle contraction will compromise tension development. This review seeks to accomplish two related goals: 1) to provide an up-to-date molecular understanding of the Ca2+-release process, with considerable attention devoted to the SR Ca2+ channel, including its associated proteins and their regulation by endogenous compounds; and 2) to examine several putative mechanisms by which cellular alterations resulting from intense and/or prolonged contractile activity will modify SR Ca2+ release. The mechanisms that are likely candidates to explain the reductions in SR Ca2+ channel function following contractile activity include elevated Ca2+ concentrations, alterations in metabolic homeostasis within the “microcompartmentalized” triadic space, and modification by reactive oxygen species.

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Prolonged exercise induces structural changes in SR Ca2+-ATPase of rat muscle

Cited by 62 publications

References 47 publications

HSP70 Binds to the Fast-twitch Skeletal Muscle Sarco(endo)plasmic Reticulum Ca2+-ATPase (SERCA1a) and Prevents Thermal Inactivation

HSP70 Binds to the Fast-twitch Skeletal Muscle Sarco(endo)plasmic Reticulum Ca2+-ATPase (SERCA1a) and Prevents Thermal Inactivation

Muscle Glycogen Content Modifies SR Ca2+ Release Rate in Elite Endurance Athletes

Sarcoplasmic reticulum Ca²⁺release and muscle fatigue

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Prolonged exercise induces structural changes in SR Ca2+-ATPase of rat muscle

Cited by 62 publications

References 47 publications

HSP70 Binds to the Fast-twitch Skeletal Muscle Sarco(endo)plasmic Reticulum Ca2+-ATPase (SERCA1a) and Prevents Thermal Inactivation

HSP70 Binds to the Fast-twitch Skeletal Muscle Sarco(endo)plasmic Reticulum Ca2+-ATPase (SERCA1a) and Prevents Thermal Inactivation

Muscle Glycogen Content Modifies SR Ca2+ Release Rate in Elite Endurance Athletes

Sarcoplasmic reticulum Ca2+release and muscle fatigue

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Product

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Sarcoplasmic reticulum Ca²⁺release and muscle fatigue