Prior heat stress improves survival of ischemic-reperfused skeletal muscle in vivo

Lepore, Diana A.; Hurley, James C.; Stewart, Alastair G.; Morrison, Wayne A.; Anderson, Robin L.

doi:10.1002/1097-4598(200012)23:12<1847::aid-mus8>3.0.co;2-u

Cited by 46 publications

(30 citation statements)

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“…For example, overexpression of HSP70 in striated muscle cells, either in transgenic mice or physiologically, by exposure of cells to a mild heat shock, is associated with protection from ischemia-reperfusion injury (23)(24)(25)(26), hyperthermia (27), and Ca 2ϩ overload (28). The molecular basis for the cytoprotective effects of HSP70 remains to be established but presumably is related to the ability of HSP70 to prevent protein aggregation and assist with refolding of denatured or partially folded proteins (22,29).…”

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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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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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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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“…Unlike regional 20 or whole-body 24,34 hyperthermia and other preconditioning methods, LSTS was applied on a specific proximal point from target muscles in this study. According to neurophysiology, the gastrocnemius-soleus muscles unit is innervated by the same lumbosacral roots as the cutaneous input from posterior middle thigh.…”

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confidence: 99%

“…Unlike the 120-and 90-min ischemic durations described by Lepore et al 20 and Garramone et al, 18 we designed our experiment with a 30-min ischemic duration to simulate tourniquet-induced I/R injury in human surgery. In Figure 1.…”

Section: Discussionmentioning

confidence: 99%

“…19 An exciting area of research is prior heat stress. 20,21 The preconditioned heat stress upregulates heat-shock proteins (HSP) 22 that play an important role in coping with the oxidative cascade and protecting cells from damage. 23 Forms of the preconditioned heat stress, such as whole-body hyperthermia 5,18,24 and regional heat, have shown little clinical benefit.…”

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confidence: 99%

“…23 Forms of the preconditioned heat stress, such as whole-body hyperthermia 5,18,24 and regional heat, have shown little clinical benefit. Direct regional heat 20 is sometimes difficult to apply, especially when the extremity has an inflammatory wound, and the patient is scheduled for an operation with a tourniquet. Local somatothermal stimulation (LSTS) increased myocardial and hepatic HSP-70 and protected rat hearts and livers against I/R injury.…”

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confidence: 99%

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Protective effects of preconditioned local somatothermal stimulation on neuromuscular plasticity against ischemia–reperfusion injury in rats

Pan¹,

Chan²,

Yang³

et al. 2008

Journal Orthopaedic Research

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The aim of this study was to investigate whether preconditioned local somatotheral stimulation (LSTS) protects the muscle and nerve against ischemia-reperfusion (I/R) injuries. Male rats were randomly assigned to normal, preconditioned LSTS only, and I/R-injured groups with or without LSTS preconditioning. I/R injuries of the lower limb were induced by rubber band wrapping, followed by measurements of gait function and nerve conduction, muscle pathology, serum enzymatic activity, and the expression of heat-shock protein 70 (HSP-70) in the gastrocnemius muscles. No significant change of neuromuscular function was found between LSTS (À) and LSTS (þ) groups on the first day after I/R injury. In contrast, gait stride length, compound motor action potential, and serum creatine phosphokinase MM isoenzyme were significantly improved on the eighth day after one or two doses of preconditioned LSTS and subsequent I/R injury. Western blot analysis disclosed no significant change of HSP-70 expression in the muscle of I/R injured limbs between LSTS (À) and LSTS (þ) groups. We conclude that preconditioned LSTS is a safe modality that improves the neuromuscular plasticity against I/R injured limbs, which provides a new strategy for I/R injury in clinical applications, such as intraoperative use of tourniquets. ß

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Ischemic preconditioning: Lack of delayed protection against skeletal muscle ischemia-reperfusion

Lepore

Morrison

2000

Microsurgery

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We investigated the ability of ischemic preconditioning to induce expression of heat shock protein 70 (Hsp 70) and/or to increase muscle survival after ischemia‐reperfusion in the rat hind limb. Ischemic preconditioning regimens tested were; 1 × 5 min of ischemia, 4 × 5 min of ischemia interrupted by 10 min of reperfusion, 1 × 10 min of ischemia or 2 × 10 min of ischemia interrupted by 15 min of reperfusion. Western blot analysis revealed only a modest induction of Hsp 70 at 24 h after preconditioning using the latter two protocols of 1 × 10 min of ischemia or 2 × 10 min. Used at 24 h prior to prolonged ischemia, neither protocol improved muscle survival measured at 24 h after reperfusion. In conclusion, ischemic preconditioning did not produce delayed protection from ischemia‐reperfusion in this model and the study suggests that ischemic preconditioning is not a useful protective strategy against skeletal muscle necrosis in the long‐term. © 2000 Wiley‐Liss, Inc. MICROSURGERY 20:350–355 2000

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Prior heat stress improves survival of ischemic-reperfused skeletal muscle in vivo

Cited by 46 publications

References 44 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

Protective effects of preconditioned local somatothermal stimulation on neuromuscular plasticity against ischemia–reperfusion injury in rats

Ischemic preconditioning: Lack of delayed protection against skeletal muscle ischemia-reperfusion

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