Changes in α7β1 integrin signaling after eccentric exercise in heat‐shocked rat soleus

Graham, Zachary A.; Touchberry, Chad D.; Gupte, Anisha A.; Bomhoff, Gregory L.; Geiger, Paige C.; Gallagher, Patricia A.

doi:10.1002/mus.24324

Cited by 6 publications

(9 citation statements)

References 43 publications

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“…In skeletal muscle, RhoA protein expression decreases following 3 days of hindlimb unloading and increases following reloading (McClung et al 2004). We have seen RhoA decrease similarly to FAK following downhill running (Graham et al 2015). SRF can colocalize with both RhoA and FAK (Sakuma et al 2003) and unloading decreased SRF protein expression along with FAK protein expression in rat hindlimb muscles (Gordon et al 2001).…”

Section: Fak and Actin Dynamicsmentioning

confidence: 74%

“…Cyclic strain decreases phosphorylation of cSrc at tyrosine 527, the main inhibitory site on this kinase, thus activating cSrc; this effect is maintained for 60 min in cultured C2C12 (Kumar et al 2004). We have observed that in rat soleus, total and activated cSrc protein expression are not affected by 90 min of eccentric downhill running at 2 and 48 h post-exercise despite decreases in FAK levels (Graham et al 2015) We have also found that cSrc activation is decreased 56 days following spinal cord injury (SCI) in rat gastrocnemius with no changes in total or activated ERK1/2 (Graham, manuscript in review). This suggests that in skeletal muscle, direct FAK and cSrc signaling through ERK1/2 may occur (1) less than 2 h following exercise; (2) during the immediate time-frame following unloading or paralysis or; (3) independently of ERK1/2 in load-induced cell signaling.…”

Section: Mechanisms For Muscle Hypertrophymentioning

confidence: 99%

“…We have found that total and phosphorylated FAK are lower following 90 min of muscle damage-inducing downhill treadmill exercise in the rat soleus compared to non-exercised controls. This decrease was seen at 2 h post-exercise but not 48 h post-exercise (Graham et al 2015). In C2C12 cells, 30 min of static stretch decreases phosphorylated FAK by roughly 50 % while FAK phosphorylation was not altered in isolated primary muscle fibers from control or γ-sarcoglycan knockout mice over the course of 4 h of static stretching (Moorwood et al 2014).…”

Section: Fak and The Response To Altered Loadingmentioning

confidence: 99%

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Focal adhesion kinase and its role in skeletal muscle

Graham

Gallagher

Cardozo

2015

J Muscle Res Cell Motil

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Skeletal muscle has a remarkable ability to respond to different physical stresses. Loading muscle through exercise, either anaerobic or aerobic, can lead to increases in muscle size and function while, conversely, the absence of muscle loading stimulates rapid decreases in size and function. A principal mediator of this load-induced change is focal adhesion kinase (FAK), a downstream non-receptor tyrosine kinase that translates the cytoskeletal stress and strain signals transmitted across the cytoplasmic membrane by integrins to activate multiple anti-apoptotic and cell growth pathways. Changes in FAK expression and phosphorylation have been found to correlate to specific developmental states in myoblast differentiation, muscle fiber formation and muscle size in response to loading and unloading. With the capability to regulate costamere formation, hypertrophy and glucose metabolism, FAK is a molecule with diverse functions that are important in regulating muscle cell health.

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Section: Fak and Actin Dynamicsmentioning

confidence: 74%

Section: Mechanisms For Muscle Hypertrophymentioning

confidence: 99%

Section: Fak and The Response To Altered Loadingmentioning

confidence: 99%

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Focal adhesion kinase and its role in skeletal muscle

Graham

Gallagher

Cardozo

2015

J Muscle Res Cell Motil

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“…We have recently shown that total and phosphorylated cSrc Y416 were not altered 2 or 48 h post-eccentric treadmill exercise. 30 In cardiac myocytes, the FAK/cSrc relationship has been implicated as being an upstream mediator of ERK1/2 activity and hypertrophy following cardiomyocyte overload. 31 This relationship must be subject to additional regulatory controls, such as changes in levels of phosphatases, because 56 days following SCI reductions in FAK and cSrc phosphorylation were not associated with altered phosphorylation of ERK1/2, even though it is necessary for growth, maintenance and regulation of muscle myotubes 32 and can be directly related to sarcolemmal tension.…”

Section: Discussionmentioning

confidence: 99%

Focal adhesion kinase signaling is decreased 56 days following spinal cord injury in rat gastrocnemius

et al. 2015

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Study design: Descriptive study. Objectives: The goal of this study was to determine the effects of spinal cord injury (SCI) on aspects of the focal adhesion kinase (FAK) signaling pathway 56 days post injury in rat gastrocnemius. Setting: This study was conducted in Bronx, NY, USA. Methods: Three-month-old male Wistar rats were exposed to either a sham surgery (n = 10) or complete T4 spinal cord transection (n = 10). Rats were killed 56 days following surgery and the muscle was collected. Following homogenization, proteins of the FAK pathway were analyzed by western immunoblotting or reverse transcription-qPCR. In addition, cellular markers for proteins that target the degradation of FAK were investigated. Results: SCI resulted in significantly lower levels of total and phosphorylated FAK, cSrc and p70S6k, and a trend for increased FRNK protein expression. SCI did not change levels of the α7 or β1 integrin subunits, total or phosphorylated ERK1/2, phosphorylated Akt and TSC2 or total p70S6k. SCI resulted in a greater expression of total Akt. mRNA expression of FAK and the α7 or β1 integrins remained unchanged between sham and SCI groups. Caspase-3/7 activity and Trim72 mRNA and protein expression remained unchanged following SCI. Conclusion: SCI results in diminished FAK signaling and is independent of ERK1/2 and Akt. SCI has no effect on mRNA levels for genes encoding components of the focal adhesion 56 days after injury.

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“…Akt then activates mTORC1 ( Watson and Baar, 2014 ) ( Figure 1 ). In addition to cardiac muscle in skeletal muscle, FAK phosphorylation and β1 integrin for aerobic and anaerobic exercise (75–98% VO 2max three times a week for 8 weeks) increase immediately after exercise ( Wilkinson et al, 2008 ; Flueck et al, 2011 ; Li et al, 2013 ; Graham et al, 2015a ; Graham et al, 2015b ; Franchi et al, 2018 ) ( Table 2 ). In exercise, cardiac hypertrophy occurs with a proportional increase in collagen and possibly integrin, leading to a highly functional matrix ( Burgess et al, 2001 ).…”

Section: Extracellular Apoptosis Signaling Pathwaysmentioning

confidence: 99%

Exercise-induced signaling pathways to counteracting cardiac apoptotic processes

Pahlavani

2022

Front. Cell Dev. Biol.

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Cardiovascular diseases are the most common cause of death in the world. One of the major causes of cardiac death is excessive apoptosis. However, multiple pathways through moderate exercise can reduce myocardial apoptosis. After moderate exercise, the expression of anti-apoptotic proteins such as IGF-1, IGF-1R, p-PI3K, p-Akt, ERK-1/2, SIRT3, PGC-1α, and Bcl-2 increases in the heart. While apoptotic proteins such as PTEN, PHLPP-1, GSK-3, JNK, P38MAPK, and FOXO are reduced in the heart. Exercise-induced mechanical stress activates the β and α5 integrins and subsequently, focal adhesion kinase phosphorylation activates the Akt/mTORC1 and ERK-1/2 pathways, leading to an anti-apoptotic response. One of the reasons for the decrease in exercise-induced apoptosis is the decrease in Fas-ligand protein, Fas-death receptor, TNF-α receptor, Fas-associated death domain (FADD), caspase-8, and caspase-3. In addition, after exercise mitochondrial-dependent apoptotic factors such as Bid, t-Bid, Bad, p-Bad, Bak, cytochrome c, and caspase-9 are reduced. These changes lead to a reduction in oxidative damage, a reduction in infarct size, a reduction in cardiac apoptosis, and an increase in myocardial function. After exercising in the heart, the levels of RhoA, ROCK1, Rac1, and ROCK2 decrease, while the levels of PKCε, PKCδ, and PKCɑ are activated to regulate calcium and prevent mPTP perforation. Exercise has an anti-apoptotic effect on heart failure by increasing the PKA-Akt-eNOS and FSTL1-USP10-Notch1 pathways, reducing the negative effects of CaMKIIδ, and increasing the calcineurin/NFAT pathway. Exercise plays a protective role in the heart by increasing HSP20, HSP27, HSP40, HSP70, HSP72, and HSP90 along with increasing JAK2 and STAT3 phosphorylation. However, research on exercise and factors such as Pim-1, Notch, and FAK in cardiac apoptosis is scarce, so further research is needed. Future research is recommended to discover more anti-apoptotic pathways. It is also recommended to study the synergistic effect of exercise with gene therapy, dietary supplements, and cell therapy for future research.

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Changes in α7β1 integrin signaling after eccentric exercise in heat‐shocked rat soleus

Abstract: Long-duration EE may cause alterations in the FA in rat soleus muscle through the α7 integrin subunit and FAK.

Cited by 6 publications

References 43 publications

Focal adhesion kinase and its role in skeletal muscle

Focal adhesion kinase and its role in skeletal muscle

Focal adhesion kinase signaling is decreased 56 days following spinal cord injury in rat gastrocnemius

Exercise-induced signaling pathways to counteracting cardiac apoptotic processes

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