Increased phosphorylation of myosin light chain associated with slow-to-fast transition in rat soleus

Bozzo, Cyril; Stevens, Laurence; Toniolo, Luana; Mounier, Yvonne; Reggiani, Carlo

doi:10.1152/ajpcell.00441.2002

Cited by 45 publications

(52 citation statements)

References 52 publications

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“…As previously described by Bozzo et al (2003), in unloaded soleus, MLC2 phosphorylation was increased alongside a decrease in Ca 2+ affinity (Gardetto et al, 1989;Stevens et al, 1993). These observations led us to suggest that modifications in Ca 2+ affinity induced by changes in the gravity factor could not be directly explained by variations in MLC2 phosphorylation.…”

Section: Mlc and Mlc2 Isoform Transitionssupporting

confidence: 78%

“…Proteins were separated by two-dimensional (2-D) gel electrophoresis using a procedure similar to those previously described by Morano et al (1988), Gonzalez et al (2002) and Bozzo et al (2003). For the first dimension or isoelectric focusing (IEF), proteins were solubilized in 8·mol·l -1 urea, 2% Chaps, 0.01·mol·l -1 dithitreitol (DTT) and a 2% carrier ampholites (Amersham) buffer, and then separated using the Ettan IPGphor Isoelectric Focusing System (Amersham) on 3.5% acrylamide strips with immobilized pH gradients (47) (Amersham).…”

Section: Two-dimensional Electrophoresis For Mlc Analysismentioning

confidence: 99%

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Hypergravity from conception to adult stage: effects on contractile properties and skeletal muscle phenotype

Bozzo¹,

Stevens²,

Bouët

et al. 2004

Journal of Experimental Biology

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SUMMARY This study examined the effects of an elevation of the gravity factor(hypergravity – 2 g) on the molecular and functional characteristics of rat soleus and plantaris muscles. Long Evans rats were conceived, born and reared (CBR) continuously in hypergravity conditions until the age of 100 days. Whole muscle morphological parameters, Ca2+activation characteristics from single skinned fibers, troponin (Tn) subunit and myosin heavy (MHC) and light (MLC) chains isoform compositions were examined in CBR and control muscles from age-paired terrestrial rats. Decreases in body and muscle mass in soleus and plantaris muscles were observed and associated, in the soleus, with a decrease in fiber diameter. The specific force of CBR soleus fibers was increased, and correlated with the elevation of Ca2+ affinity. This was accompanied by slow-to-slower TnC and TnI isoform transitions and a rearrangement in TnT fast isoform content. The MHC transformations of the soleus after hypergravity were associated with the up (down)-regulation of the MHCI (MHCIIa) mRNA isoforms. The MLC2 phosphorylation state remained unchanged in the soleus muscle. The results suggested that the gravity factor could interact with rat muscle development and that hypergravity experiments could provide good tools for the study of myofibrillar protein plasticity and their associated pathways of regulation.

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Section: Mlc and Mlc2 Isoform Transitionssupporting

confidence: 78%

Section: Two-dimensional Electrophoresis For Mlc Analysismentioning

confidence: 99%

Hypergravity from conception to adult stage: effects on contractile properties and skeletal muscle phenotype

Bozzo¹,

Stevens²,

Bouët

et al. 2004

Journal of Experimental Biology

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“…Also, monophosphorylated isoforms of MLC2f and MLC2s were detected in gastrocnemius muscle. These phosphorylated forms have been described during the process of slow-to-fast transition associated with the increase of force production at low-Ca 2+ concentrations [10,29,30]. Concerning the group of metabolic enzymes, a greater expression of glycolytic enzymes, such as glyceraldehyde 3-phosphate dehydrogenase, aldolase, and enolase, was not unexpectedly found in gastrocnemius, in agreement with a greater potential in ATP production by anaerobic pathways [9,10].…”

Section: Discussionsupporting

confidence: 54%

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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“…involved in the differential epitope expression of the slow MHC in adult rabbit masseter muscle (47). The authors proposed a modulation by O-N-acetylglycosaminylation of the phosphorylated states of slow MHC.…”

Section: Discussionmentioning

confidence: 99%

O-Linked N-Acetylglucosaminylation Is Involved in the Ca2+ Activation Properties of Rat Skeletal Muscle

Hedou¹,

Cieniewski-Bernard

Leroy

et al. 2007

Journal of Biological Chemistry

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O-Linked N-acetylglucosaminylation termed O-GlcNAc is a dynamic cytosolic and nuclear glycosylation that is dependent both on glucose flow through the hexosamine biosynthesis pathway and on phosphorylation because of the existence of a balance between phosphorylation and O-GlcNAc. This glycosylation is a ubiquitous post-translational modification, which probably plays an important role in many aspects of protein functions. We have previously reported that, in skeletal muscle, proteins of the glycolytic pathway, energetic metabolism, and contractile proteins were O-GlcNAc-modified and that O-GlcNAc variations could control the muscle protein homeostasis and be implicated in the regulation of muscular atrophy.In this paper, we report O-N-acetylglucosaminylation of a number of key contractile proteins (i.e. myosin heavy and light chains and actin), which suggests that this glycosylation could be involved in skeletal muscle contraction. Moreover, our results showed that incubation of skeletal muscle skinned fibers in N-acetyl-D-glucosamine, in a concentration solution known to inhibit O-GlcNAc-dependent interactions, induced a decrease in calcium sensitivity and affinity of muscular fibers, whereas the cooperativity of the thin filament proteins was not modified. Thus, our results suggest that O-GlcNAc is involved in contractile protein interactions and could thereby modulate muscle contraction. O-Linked N-acetylglucosaminylation, termed O-GlcNAc,5 is a regulatory post-translational modification that occurs in nuclear and cytosolic proteins, corresponding to the addition of a unique monosaccharide, N-acetyl-D-glucosamine, to a serine and threonine hydroxyl group by a ␤-linkage (1). Because of the existence of the UDP-GlcNAc-peptide-␤-GlcNAc transferase, which transfers the monosaccharide into proteins (2, 3), and the N-acetyl-␤-D-glucosaminidase, which removes it (4), OGlcNAc is more similar to phosphorylation than classical glycosylation. The half-life of the monosaccharide is shorter than the half-life of the protein backbone (5), indicating that the O-GlcNAc cycle could rapidly respond to cellular signals (6). All of the known O-GlcNAc proteins described to date are also phosphoproteins (7) (for review, see Ref. 8). Modifications by O-GlcNAc or phosphorylation could occur on the same site (9) or at neighboring sites (10); this competition between O-GlcNAc and phosphorylation is called the "Yin-Yang" process.O-GlcNAc has been described to play a role in various cell functions: in nuclear transport (11-13); in protein degradation, with a reversible inhibition of the proteasome itself (14) and a protection of the modified protein against proteasomal degradation (9, 15, 16); and in regulation of protein expression, with the regulation of transcription (10, 17-19) and translation (20). The involvement of O-GlcNAc in protein-protein interactions has been described in different biological systems. Indeed, many proteins playing a key role in organization and assembly of cytoskeleton are O-GlcNAc-modified, including cytok...

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Increased phosphorylation of myosin light chain associated with slow-to-fast transition in rat soleus

Cited by 45 publications

References 52 publications

Hypergravity from conception to adult stage: effects on contractile properties and skeletal muscle phenotype

Hypergravity from conception to adult stage: effects on contractile properties and skeletal muscle phenotype

Subcellular proteomics of mice gastrocnemius and soleus muscles

O-Linked N-Acetylglucosaminylation Is Involved in the Ca2+ Activation Properties of Rat Skeletal Muscle

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