αB-Crystallin Maintains Skeletal Muscle Myosin Enzymatic Activity and Prevents its Aggregation under Heat-shock Stress

Melkani, Girish C.; Cammarato, Anthony; Bernstein, Sanford I.

doi:10.1016/j.jmb.2006.02.043

Cited by 55 publications

(58 citation statements)

References 48 publications

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“…They are particularly involved in the protection of structural proteins like desmin, titin, and actin (Bullard et al, 2004;Ghosh, Houck, & Clark, 2007). The HSP20 proteins inhibit the protein aggregates formation, to maintain protein accessibility (Melkani, Cammarato, & Bernstein, 2006). So, HSP20 proteins could enhance structural proteins proteolysis, especially during meat tenderization, and so meat tenderness.…”

Section: Discrimination Of St Tenderness Classesmentioning

confidence: 99%

Different phenotypic and proteomic markers explain variability of beef tenderness across muscles

Guillemin¹,

Jurie²,

Renand³

et al. 2012

IJB

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This study analyzed the abundance of tenderness biomarkers: 24 proteins and 11 phenotypic carcass characteristics and muscle properties. This was done on 111 samples of two muscles, Longissimus thoracis (LT) and Semitendinosus (ST) from the Charolais cattle breed. The strategy was to constitute and explain three tenderness classes on the two muscles separately, on the shear-force data (Warner-Bratzler). Results showed that ST classes were explained by 12 proteins and 6 phenotypic characteristics. LT classes could only be explained by 7 phenotypic characteristics. This demonstrates that in ST and LT the tenderness variability is explained by different factors. In ST, the main results demonstrated the importance of Heat Shock Proteins such as Hsp27 (P = 0.002) and the oxidative stress protein: PRDX6 (P = 0.003). We also confirmed the role of the glycolytic enzyme Enolase 3 (P = 0.003), and contractile protein such as MyHC IIx (P = 0.028).

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Section: Discrimination Of St Tenderness Classesmentioning

confidence: 99%

Different phenotypic and proteomic markers explain variability of beef tenderness across muscles

Guillemin¹,

Jurie²,

Renand³

et al. 2012

IJB

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“…Following various stress interventions the two small HSPs, HSP25 and ␣B-crystallin, have been found to bind to a wide variety of different cytoskeletal/ myofibrillar proteins (2,16), including desmin (15,19,20,38), titin (15), actin (28,43), myosin (24), and possibly also Z-disk proteins. Consistent with this, we have recently shown that in rat SOL muscles heated in vitro to 45°C for 30 min, Ͼ95% of the HSP25 and ␣B-crystallin became tightly bound within the fibers and did not diffuse out even when all internal membranes were dispersed with the detergent Triton X-100 (21).…”

mentioning

confidence: 99%

Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers

Larkins

Murphy

Lamb

2012

American Journal of Physiology-Cell Physiology

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Larkins NT, Murphy RM, Lamb GD. Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers. Am J Physiol Cell Physiol 303: C654 -C665, 2012. First published July 3, 2012; doi:10.1152/ajpcell.00180.2012.-Heat shock proteins (HSPs) help maintain cellular function in stressful situations, but the processes controlling their interactions with target proteins are not well defined. This study examined the binding of HSP72, HSP25, and ␣B-crystallin in skeletal muscle fibers following various stresses. Rat soleus (SOL) and extensor digitorum longus (EDL) muscles were subjected in vitro to heat stress or strongly fatiguing stimulation. Superficial fibers were "skinned" by microdissection and HSP diffusibility assessed from the extent of washout following 10-to 30 min exposure to a physiological intracellular solution. In fibers from nonstressed (control) SOL muscle, Ͼ80% of each HSP is readily diffusible. However, after heating a muscle to 40°C for 30 min ϳ95% of HSP25 and ␣B-crystallin becomes tightly bound at nonmembranous myofibrillar sites, whereas HSP72 bound at membranous sites only after heat treatment to Ն44°C. The ratio of reduced to oxidized cytoplasmic glutathione (GSH:GSSG) decreased approximately two-and fourfold after heating muscles to 40°and 45°C, respectively. The reducing agent dithiothreitol reversed HSP72 binding in heated muscles but had no effect on the other HSPs. Intense in vitro stimulation of SOL muscles, sufficient to elicit substantial oxidation-related loss of maximum force and approximately fourfold decrease in the GSH:GSSG ratio, had no effect on diffusibility of any of the HSPs. When skinned fibers from heat-treated muscles were bathed with additional exogenous HSP72, total binding increased approximately two-and 10-fold, respectively, in SOL and EDL fibers, possibly reflective of the relative sarco(endo)plasmic reticulum Ca 2ϩ -ATPase pump densities in the two fiber types. Phosphorylation at Ser59 on ␣B-crystallin and Ser85 on HSP25 increased with heat treatment but did not appear to determine HSP binding. The findings highlight major differences in the processes controlling binding of HSP72 and the two small HSPs. Binding was not directly related to cytoplasmic oxidative status, but oxidation of cysteine residues influenced HSP72 binding. oxidation; stress response; skinned fiber; chaperones HEAT SHOCK PROTEINS (HSPs) are highly conserved and ubiquitously expressed proteins that act as protein chaperones and in stress situations bind and interact with various proteins to help preserve or restore their function (23,32). A great deal of work in skeletal muscle has focused on the increase in HSP protein and/or mRNA expression levels occurring in hours to days after various stressful stimuli, such as eccentric exercise (11,17,26,27,39), oxidative stress (50), heat (4, 35), and glycogen depletion (12). The present study focuses instead on the acute responses of HSPs to stresses, examining the effects of heat, contraction, and o...

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“…Chicken skeletal muscle myosin was unfolded by heat shock in vitro and in the presence of αB-crystallin, myosin retained enzymatic activity and aggregation was prevented (Melkani et al 2006 ). αB-Crystallin was shown in vitro to prevent the acidic-induced aggregation of the N2A region of skeletal muscle titin, which contains Ig domains that are prone to unfolding during exercise (Kotter et al 2014 ).…”

Section: Skeletal Muscle: Exercisementioning

confidence: 99%

Multifunctional Roles of αB-Crystallin in Skeletal and Cardiac Muscle Homeostasis and Disease

Mitzelfelt

Benjamin

2015

Heat Shock Proteins

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αB-Crystallin, or HspB5, is a small molecular-weight heat shock protein expressed highly in cardiac and skeletal muscle with multifaceted cellular roles including, chaperone function towards essential myofi brillar components. Insights into protective roles played by αB-crystallin, as well as mutations in the gene encoding αB-crystallin, CRYAB , which resulted in human pathologies, have highlighted the critical functions of αB-crystallin in both skeletal and cardiac muscle, inter alia . Various human mutations in CRYAB appear to have tissue-specifi c effects, with loss of αB-crystallin only impacting skeletal muscle under basal conditions. This review aims to highlight the roles of αB-crystallin in skeletal and cardiac muscle homeostasis as well as under conditions of stress and disease, drawing insights from human pathologies resulting from CRYAB mutations, and to discuss the potential of using induced pluripotent stem cells to model αB-crystallin-opathies in vitro.

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αB-Crystallin Maintains Skeletal Muscle Myosin Enzymatic Activity and Prevents its Aggregation under Heat-shock Stress

Cited by 55 publications

References 48 publications

Different phenotypic and proteomic markers explain variability of beef tenderness across muscles

Different phenotypic and proteomic markers explain variability of beef tenderness across muscles

Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers

Multifunctional Roles of αB-Crystallin in Skeletal and Cardiac Muscle Homeostasis and Disease

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