Comparison of the small heat shock proteins ?B-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle

Golenhofen, Nikola; Perng, Ming Der; Quinlan, Roy A.; Drenckhahn, Detlev

doi:10.1007/s00418-004-0711-z

Cited by 155 publications

(186 citation statements)

References 51 publications

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“…These three HSPs were more abundant in LT than in ST and in young bulls compared to steers. These results are consistent with the study of Golenhofen et al (2004) in rats, showing a higher abundance of HSPs in soleus (slow oxidative) compared to extensor digitorum longus (fast glycolytic) muscle. In cattle, LT contains a lower proportion of fast glycolytic fibres and higher proportion of oxidative fibres (I and IIa) compared with ST .…”

Section: Hspssupporting

confidence: 92%

“…There are very few data in the literature on differences in HSP expression according to the muscle type. Our results in Protein content according to muscle and animal types cattle with those of Golenhofen et al (2004) in rats, show that HSPs form a complex stress-response system in skeletal muscle with some common and some distinct functions between different muscle types. Golenhofen et al (2004), using immunostaining, showed a higher intensity with an antiaB-crystallin antibody in type I fibres compared to II fibres.…”

Section: Hspsmentioning

confidence: 57%

“…Our results in Protein content according to muscle and animal types cattle with those of Golenhofen et al (2004) in rats, show that HSPs form a complex stress-response system in skeletal muscle with some common and some distinct functions between different muscle types. Golenhofen et al (2004), using immunostaining, showed a higher intensity with an antiaB-crystallin antibody in type I fibres compared to II fibres. Moreover, they observed some fast fibres displaying no staining and others with a strong staining, suggesting a differential expression between IIa and IIx/IIb fibres.…”

Section: Hspsmentioning

confidence: 57%

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Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type

Guillemin

Jurie

Cassar-Malek

et al. 2011

Animal

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Some proteins have been revealed as biomarkers for beef tenderness by previous studies. These markers could be used in immunological tests to predict beef tenderness, in living animals as well as in carcasses. It is well known that rearing practices modify the amounts of mRNA and proteins. Therefore, the reliability of protein tests could be affected by livestock and biological effects such as production systems, breed, muscle and animal type. This study analysed the effects of animal and muscle type on 24 proteins. The animals studied were 67 young bulls and 44 steers of the Charolais breed, and muscles were Longissimus thoracis and Semitendinosus. Protein amounts were determined by Dot blot, an immunological technique. Results showed that expressions of 20 proteins were influenced by animal and/or muscle type. These results could lead to modifications and adaptations of prediction tests according to rearing practice, bovine breed and beef cut.

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Section: Hspssupporting

confidence: 92%

Section: Hspsmentioning

confidence: 57%

Section: Hspsmentioning

confidence: 57%

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Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type

Guillemin

Jurie

Cassar-Malek

et al. 2011

Animal

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“…HSP27, HSP90, and alphaB-crystallin-related B6 were identified in the nuclear fraction of the gastrocnemius muscle, whereas HSP27, HSP70, HSP90, HSP1 (chaperonin), heat shock protein (HSP) family member 7, and cryab protein were identified in the nuclear fraction of the soleus muscle. The presence of HSP1 in soleus is in agreement with the observed overexpression of this protein shown by Golenhofen and coworkers [32] when comparing soleus with gastrocnemius. The notion of more members of the HSP family confirms the functional properties of the red soleus muscle, and this would make this muscle more susceptible to stress conditions related to HSP as compared with the white portion of the gastrocnemius muscle.…”

Section: Discussionsupporting

confidence: 90%

Subcellular proteomics of mice gastrocnemius and soleus muscles

Vitorino

Ferreira

Neuparth

et al. 2007

Analytical Biochemistry

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A proteomics characterization of mice soleus and gastrocnemius white portion skeletal muscles was performed using nuclear, mitochondrial/membrane, and cytosolic subcellular fractions. The proposed methodology allowed the elimination of the cytoskeleton proteins from the cytosolic fraction and of basic proteins from the nuclear fraction. The subsequent protein separation by twodimensional gel electrophoresis prior to mass spectrometry analysis allowed the detection of more than 600 spots in each muscle. In the gastrocnemius muscle fractions, it was possible to identify 178 protein spots corresponding to 108 different proteins. In the soleus muscle fractions, 103 different proteins were identified from 253 positive spot identifications. A bulk of cytoskeleton proteins such as actin, myosin light chains, and troponin were identified in the nuclear fraction, whereas mainly metabolic enzymes were detected in the cytosolic fraction. Transcription factors and proteins associated with protein biosynthesis were identified in skeletal muscles for the first time by proteomics. In addition, proteins involved in the mitochondrial redox system, as well as stress proteins, were identified. Results confirm the potential of this methodology to study the differential expressions of contractile proteins and metabolic enzymes, essential for generating functional diversity of muscles and muscle fiber types. Keywords Skeletal muscle; Subcellular fractionation; ProteomicsHuman skeletal muscle is very heterogeneous in composition, being constituted by different types of muscle fibers showing significant differences in their contractile speed and metabolic profile that result from specific protein expression [1][2][3][4]. In rodents, especially mice and rats, muscle fibers present a more uniform distribution among the different muscles, allowing the use of the entire muscles to study specific phenotypes. In this regard, the soleus and the white portion of gastrocnemius of mice are composed mainly of fast-and slow-twitch muscle fibers, respectively [5][6][7], and these two muscles have been used as typical models in proteomics. During the past few years, several studies have been performed using two-dimensional gel electrophoresis (2-DE) 1 combined with mass spectrometry (MS) to characterize skeletal muscle protein composition of typical slow-and fast-twitch skeletal muscles [8][9][10][11][12][13][14][15][16][17]. In a recent proteomics study on murine gastrocnemius and soleus muscle extracts, performed by Gelfi and coworkers [9], more than 800 spots on each 2-DE were detected by silver staining, leading to the identification of 85 different proteins belonging to the most abundant structural and metabolic protein classes. Despite the large number of visualized spots by 2-DE, proteins with lower relative abundances, usually involved in protein biosynthesis and cell stress response, are probably masked by structural or metabolic proteins [18,19]. To counteract this, Jarrold and coworkers [14] performed the depletion of abundant mus...

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“…In the heart, cardio myocytes express high levels of specific mem bers of one of the small HSP families, the HSPBs. These include HSPB1 (HSP27), HSPB5 (α crystallin B chain), HSPB6 (HSP20), HSPB7 (cardiovascular HSP), and HSPB8 (HSP22), and are considered to safeguard cardiomyocytes from proteotoxicity by stabilizing the contractile apparatus 38,39 .…”

Section: The Proteostasis Network Componentsmentioning

confidence: 99%

Proteostasis in cardiac health and disease

Henning

Brundel²

2017

Nat Rev Cardiol

140

126

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The worldwide increase in life expectancy gives rise to an increasing prevalence of cardiac diseases, which remain the leading cause of disability and death in the developed world [1][2][3] . Currently, the mechanisms under lying how ageing contributes to the initiation or acceler ation of cardiac diseases are essentially unresolved. Prevailing theories of ageing centre on gradual derail ment of cellular protein homeostasis -proteostasis -either by design (genetically) or by 'wear and tear' (environmentally) 3 . Central to the role of proteostasis derailment as a major factor in ageing is the observation that protein function declines over time.Proteins are the most versatile and complex macro molecules and are involved in the proper functioning of every biological process 4 . After synthesis as a poly peptide chain from the genetic code, proper function of a protein relies heavily on its correct folding into a 3D native state and on various post translational modifi cations, mostly involving the addition of chem ical groups (including phosphate, acetate, and carbo hydrate). Protein maturation, transport, and ultimately breakdown is monitored and supported by various classes of proteins, collectively called 'protein quality control' (PQC) [3][4][5] . Balanced proteostasis, therefore, depends on proper PQC and is crucial for cellular and organismal health 6 . The intricate network making up the PQC involves numerous proteins, of which the main players are the chaperones and their regula tors 4,7-9 (assisting in folding and refolding of proteins) and the pathways that clear irreversibly misfolded and aggregation prone proteins (the ubiquitin-proteasome system [UPS] and autophagy systems) 9-11 . With ageing, the gradual accumulation of misfolded or damaged pro teins, together with concomitant failure of PQC, results in proteotoxic stress and compromised defence against reactive oxygen species (ROS) 10 , a process that is likely to be accelerated in various age related diseases includ ing neurodegenerative diseases 12,13 , type 2 diabetes mel litus 14 , cancer 15 , and cardiac diseases [16][17][18][19][20] . In addition to the accumulation of misfolded proteins, ageing is accompanied by an imbalance in the proteome, as indi cated by lowered expression of chaperone, proteaso mal, ribosomal, and mitochondrial proteins, whereas proteins related to oxidative stress are upregulated 21,22 . Although mild impairment of proteostasis extends lifespan in Caenorhabditis elegans, referred to as hormesis, sustained impairment is accompanied by loss of PQC to neutralize this effect 3,5 . Importantly, evidence indicates that the amount of soluble, aggregate prone protein oligomers, rather than the abundance of pro tein aggregates, correlates with disease severity 23,24 . Therefore, protein aggregates, which contain both misfolded proteins and elevated levels of chaper ones, constitute an adequate PQC response, aimed at sequestering potentially harmful protein oligomers, rather than embodying the ultimate cellular threat 25 . This ...

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Comparison of the small heat shock proteins ?B-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle

Cited by 155 publications

References 51 publications

Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type

Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type

Subcellular proteomics of mice gastrocnemius and soleus muscles

Proteostasis in cardiac health and disease

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