Hsp27 inhibits IKKβ‐induced NF‐κΕ activity and skeletal muscle atrophy

Dodd, Stephen; Hain, Brian A.; Senf, Sarah M.; Judge, Sarah M.

doi:10.1096/fj.08-124602

Cited by 75 publications

(55 citation statements)

References 48 publications

(85 reference statements)

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“…16,20) Conversely, an increase in HSPB1 by overexpression with recombinant HSPB1 attenuates muscle atrophy in an experimental model. 39) By combining our results with those studies, we suggest that chicken HSPB1 formed complexes with αB-crystallin and acts as a molecular chaperon in aged chicken muscle.…”

Section: Discussionsupporting

confidence: 77%

Chicken heat shock protein HSPB1 increases and interacts with αB-crystallin in aged skeletal muscle

Ueda

Kokaji

Simizu

et al. 2015

Bioscience, Biotechnology, and Biochemistry

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International trading markets of meat require the animal’s age information to prevent cross-contamination of ineligible meat products. Individual livestock age is either evaluated from physiological features or verified by breeding history. However, it remains impossible to perform age verification on meat when a suspicion of error occurred in the importing country. To investigate an age-related protein in skeletal muscle of livestock, we compared protein expression among chicken pectoralis major of different ages. Results indicated that the level of expression of chicken HSPB1, one of the small heat shock proteins, was increased in aged muscles. On the other hand, other heat shock proteins, heat shock factors, and myosin heavy chain isoform did not change the expression levels in aged chicken muscle. In addition, we identified that αB-crystallin interacted with HSPB1 in aged chicken muscle. These results suggest that HSPB1 protein forms complexes with αB-crystallin in aged chicken muscle and suppose to become the candidate of age-related bio-marker for verifying the age of chicken meat.

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Section: Discussionsupporting

confidence: 77%

Chicken heat shock protein HSPB1 increases and interacts with αB-crystallin in aged skeletal muscle

Ueda

Kokaji

Simizu

et al. 2015

Bioscience, Biotechnology, and Biochemistry

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“…HSPs, especially HSP72 and HSP25, are inducible molecular chaperones that are upregulated when cells are exposed to stress (24). The upregulations of HSP72 and HSP25 prevent muscle atrophy, which is caused by disuse and/or immobilization (4,26,38). The transcription of HSPs is mediated by HSF1, which binds to heat shock elements located on HSP genes and induces their expressions (24).…”

Section: Discussionmentioning

confidence: 99%

“…In addition, overexpression of HSP72 in skeletal muscle prevented immobilization-induced atrophy in rat (38) and improved the structural and functional recovery from atrophy of mouse muscle (26). It was also demonstrated that transfection of 27-kDa HSP (HSP27 and so-called HSP25) attenuated the disuse atrophy of rat muscle (4). The molecular mechanism, by which HSPs regulate skeletal muscle mass, is associated with inhibition of the Foxo pathway and decrease of MuRF1 and atrogin-1 expressions (4, 21, 37, 38).…”

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confidence: 96%

AICAR-induced activation of AMPK negatively regulates myotube hypertrophy through the HSP72-mediated pathway in C₂C₁₂skeletal muscle cells

Egawa

Ohno

Goto

et al. 2014

American Journal of Physiology-Endocrinology and Metabolism

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induced activation of AMPK negatively regulates myotube hypertrophy through the HSP72-mediated pathway in C2C12 skeletal muscle cells. Am J Physiol Endocrinol Metab 306: E344 -E354, 2014. First published December 17, 2013; doi:10.1152/ajpendo.00495.2013.-5=-AMP-activated protein kinase (AMPK) plays an important role as a negative regulator of skeletal muscle mass. However, the precise mechanism of AMPK-mediated regulation of muscle mass is not fully clarified. Heat shock proteins (HSPs), stress-induced molecular chaperones, are related with skeletal muscle adaptation, but the association between AMPK and HSPs in skeletal muscle hypertrophy is unknown. Thus, we investigated whether AMPK regulates hypertrophy by mediating HSPs in C2C12 cells. The treatment with AICAR, a potent stimulator of AMPK, decreased 72-kDa HSP (HSP72) expression, whereas there were no changes in the expressions of 25-kDa HSP, 70-kDa heat shock cognate, and heat shock transcription factor 1 in myotubes. Protein content and diameter were less in the AICARtreated myotubes in those without treatment. AICAR-induced suppression of myotube hypertrophy and HSP72 expression was attenuated in the siRNA-mediated AMPK␣ knockdown myotubes. AICAR increased microRNA (miR)-1, a modulator of HSP72, and the increase of miR-1 was not induced in AMPK␣ knockdown condition. Furthermore, siRNA-mediated HSP72 knockdown blocked AICARinduced inhibition of myotube hypertrophy. AICAR upregulated the gene expression of muscle Ring-finger 1, and this alteration was suppressed in either AMPK␣ or HSP72 knockdown myotubes. The phosphorylation of p70 S6 kinase Thr 389 was downregulated by AICAR, whereas this was attenuated in AMPK␣, but not in HSP72, knockdown myotubes. These results suggest that AMPK inhibits hypertrophy through, in part, an HSP72-associated mechanism via miR-1 and protein degradation pathways in skeletal muscle cells. microRNA; heat shock transcription factor 1; muscle rRing-finger 1; atrogin-1; acetyl-CoA carboxylase SKELETAL MUSCLE HAS A GREATER CAPACITY to adapt to various stimuli. Increased loading, such as resistance training and mechanical stretching, stimulates protein synthesis and reduces protein degradation, thereby inducing muscle hypertrophy (10). On the other hand, decrease of use, such as immobilization, denervation, aging, and/or various pathological conditions, attenuates protein synthesis and increases protein degradation, resulting in atrophy (12,32). Although the process of skeletal muscle adaptation to hypertrophic and atrophic stimuli has been studied, the molecular mechanism involved in this process is not fully understood yet.5=-AMP-activated protein kinase (AMPK) is well known as a sensor for cellular energy status and metabolic stress, such as muscle contraction, fasting, hypoxia, ischemia, and/or oxidative and osmotic stresses and as a signaling intermediary that controls the use of glucose and fatty acids in skeletal muscle (8,14,15). In addition, several studies in the past decade have suggested that AMPK plays an important rol...

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“…Senf et al reported that HSP70 overexpression prevented rat soleus muscle fiber atrophy induced by hind limb immobilization (18). Furthermore, overexpression of HSP27 also prevented muscle fiber atrophy of the soleus muscle induced by disuse in rats (5). HSPs are expressed in response to several types of stress such as heat (14,15) and exercise (12).…”

mentioning

confidence: 99%

Heat stress attenuates skeletal muscle atrophy of extensor digitorum longus in streptozotocin-induced diabetic rats

Nonaka¹,

Une²,

Akiyama³

2015

Acta Physiologica Hungarica

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To investigate whether heat stress attenuates skeletal muscle atrophy of the extensor digitorum longus (EDL) muscle in streptozotocin-induced diabetic rats, 12-week-old male Wistar rats were randomly assigned to four groups (n = 6 per group): control (Con), heat stress (HS), diabetes mellitus (DM), and diabetes mellitus/heat stress (DM + HS). Diabetes was induced by intraperitoneal injection of streptozotocin (50 mg/kg). Heat stress was induced in the HS and DM + HS groups by immersion of the lower half of the body in hot water at 42 °C for 30 min; it was initiated 7 days after injection of streptozotocin, and was performed once a day, five times a week for 3 weeks. The muscle fiber cross-sectional area of EDL muscles from diabetic and non-diabetic rats was determined; heat stress protein (HSP) 72 and HSP25 expression levels were also analyzed by western blotting. Diabetes-induced muscle fiber atrophy was attenuated upon heat stress treatment in diabetic rats. HSP72 and HSP25 expression was upregulated in the DM + HS group compared with the DM group. Our findings suggest that heat stress attenuates atrophy of the EDL muscle by upregulating HSP72 and HSP25 expression.Keywords: extensor digitorum longus muscle, heat stress, HSP72, HSP25, skeletal muscle atrophy, streptozotocin-induced diabetes Diabetes mellitus (DM) induces skeletal muscle atrophy (7, 19) and decreases muscle strength (7, 9). Consequently, patients with diabetes have a higher risk of falls because of reduced muscle strength (8, 16) and DM-induced-muscle atrophy. Where DM induces skeletal muscle atrophy, fast-twitch fibers are prone to greater atrophy than are slow-twitch fibers (1). Fast-twitch fibers are responsible for high force/power/speed production and maintaining physical balance during postural perturbation. Hence, atrophy of fast-twitch muscle increases the risk of falling in DM patients. Therefore, an efficient strategy is required to attenuate muscle atrophy in order to reduce the risk of falls in DM patients. Heat shock proteins (HSPs) have a protective effect on muscle atrophy. Senf et al. reported that HSP70 overexpression prevented rat soleus muscle fiber atrophy induced by hind limb immobilization (18). Furthermore, overexpression of HSP27 also prevented muscle fiber atrophy of the soleus muscle induced by disuse in rats (5). HSPs are expressed in response to several types of stress such as heat (14, 15) and exercise (12). Exercise increased HSP72 expression (2) and attenuated skeletal muscle fiber atrophy (3) in streptozotocin

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Hsp27 inhibits IKKβ‐induced NF‐κΕ activity and skeletal muscle atrophy

Cited by 75 publications

References 48 publications

Chicken heat shock protein HSPB1 increases and interacts with αB-crystallin in aged skeletal muscle

Chicken heat shock protein HSPB1 increases and interacts with αB-crystallin in aged skeletal muscle

AICAR-induced activation of AMPK negatively regulates myotube hypertrophy through the HSP72-mediated pathway in C₂C₁₂skeletal muscle cells

Heat stress attenuates skeletal muscle atrophy of extensor digitorum longus in streptozotocin-induced diabetic rats

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Hsp27 inhibits IKKβ‐induced NF‐κΕ activity and skeletal muscle atrophy

Cited by 75 publications

References 48 publications

Chicken heat shock protein HSPB1 increases and interacts with αB-crystallin in aged skeletal muscle

Chicken heat shock protein HSPB1 increases and interacts with αB-crystallin in aged skeletal muscle

AICAR-induced activation of AMPK negatively regulates myotube hypertrophy through the HSP72-mediated pathway in C2C12skeletal muscle cells

Heat stress attenuates skeletal muscle atrophy of extensor digitorum longus in streptozotocin-induced diabetic rats

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AICAR-induced activation of AMPK negatively regulates myotube hypertrophy through the HSP72-mediated pathway in C₂C₁₂skeletal muscle cells