Myosin heavy chain isoform distribution in single fibres of bodybuilders

Kesidis, Nikolaos; Metaxas, Thomas; Vrabas, Ioannis S.; Stefanidis, Panagiotis; Vamvakoudis, Efstratios; Christoulas, Kosmas; Mandroukas, Athanasios; Balasas, Dimitrios G; Mandroukas, Konstantinos

doi:10.1007/s00421-008-0751-5

Cited by 21 publications

(24 citation statements)

References 29 publications

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“…MYH7 is a slow molecular ATPase involved in muscle contraction . Our proteomic data indicated that MYH7 protein expression was upregulated ∼19 fold in cardiac hypertrophy (Fig.…”

Section: Discussionmentioning

confidence: 82%

“…Our informatics analysis led to the prioritization of 52 hypertrophy-associated protein candidates down to four proteins, including ANXA2, IGFBP7, MYH7, and DESM. MYH7 is a slow molecular ATPase involved in muscle contraction [32]. Our proteomic data indicated that MYH7 protein expression was upregulated ∼19 fold in cardiac hypertrophy (Fig.…”

Section: Establishment Of Biomarkers Of Heart Failurementioning

confidence: 80%

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Pilot study identifying myosin heavy chain 7, desmin, insulin‐like growth factor 7, and annexin A2 as circulating biomarkers of human heart failure

Chugh

Ouzounian

et al. 2013

Proteomics

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In depth proteomic analyses offer a systematic way to investigate protein alterations in disease and, as such, can be a powerful tool for the identification of novel biomarkers. Here, we analyzed proteomic data from a transgenic mouse model with cardiac-specific overexpression of activated calcineurin (CnA), which results in severe cardiac hypertrophy. We applied statistically filtering and false discovery rate correction methods to identify 52 proteins that were significantly different in the CnA hearts compared to controls. Subsequent informatic analysis consisted of comparison of these 52 CnA proteins to another proteomic dataset of heart failure, three available independent microarray datasets, and correlation of their expression with the human plasma and urine proteome. Following this filtering strategy, four proteins passed these selection criteria including: myosin heavy chain 7, insulin-like growth factor-binding protein 7, annexin A2, and desmin. We assessed expression levels of these proteins in mouse plasma by immunoblotting, and observed significantly different levels of expression between healthy and failing mice for all 4 proteins. We verified antibody cross reactivity by examining human cardiac explant tissue by immunoblotting. Finally, we assessed protein levels in plasma samples obtained from 4 unaffected and 4 heart failure patients and demonstrated that all four proteins increased between 2-fold and 150-fold in heart failure. We conclude that MYH7, IGFBP7, ANXA2, and DESM are all excellent candidate plasma biomarkers of heart failure in mouse and human.

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“…MYH7 is a slow molecular ATPase involved in muscle contraction . Our proteomic data indicated that MYH7 protein expression was upregulated ∼19 fold in cardiac hypertrophy (Fig.…”

Section: Discussionmentioning

confidence: 82%

Section: Establishment Of Biomarkers Of Heart Failurementioning

confidence: 80%

Pilot study identifying myosin heavy chain 7, desmin, insulin‐like growth factor 7, and annexin A2 as circulating biomarkers of human heart failure

Chugh

Ouzounian

et al. 2013

Proteomics

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“…Although hybrid fibers definitely play a role in muscle fiber type transitions, a number of studies have now shown that hybrid fibers also form a common component of normal muscles (1,16,25,60). Many of these hybrid fibers represent very stable phenotypes, even in the face of different types of exercise (25,28,40). The relative proportion of hybrid fibers varies among different muscles (1,16,25) and even among anatomical regions within the same muscle (16,25).…”

Section: Discussionmentioning

confidence: 98%

The continuum of hybrid IIX/IIB fibers in normal mouse muscles: MHC isoform proportions and spatial distribution within single fibers

Zhang

Medler

2010

American Journal of Physiology-Regulatory, Integrative and Comp

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Although skeletal muscle fiber types are often defined as belonging to discrete categories, many muscles possess fibers with intermediate phenotypes. These hybrid fiber types can be identified by their expression of two or more myosin heavy chain (MHC) isoforms within the same single fiber. In mouse muscles, the most common hybrid fibers are those coexpressing the IIX and IIB MHC isoforms. In the present study, we focused on these IIX/IIB fibers from normal mouse muscles to determine the relative proportions of MHC isoforms at both the protein and mRNA levels and to examine the longitudinal distribution of isoforms within single fibers. We found that IIX/IIB hybrids represent ∼25 and 50% of the fibers in the mouse tibialis anterior and brachioradialis, respectively. The relative proportion of the IIX and IIB isoforms in these fibers spans a continuum, from predominantly IIB-like hybrids to IIX-like hybrids. Quantitative assessment of mRNA levels using real-time PCR from single fibers indicated that IIB expression dominated over IIX expression in most fibers and that a general correlation existed between mRNA isoform levels and MHC protein content. However, the match between mRNA levels and protein content was not precise. Finally, we measured MHC isoform proportions in adjacent fiber segments and discovered that ∼30% of hybrids possessed significant differences in isoform content along their length. In some instances, the muscle fiber type as defined by MHC content changed completely along the length of a fiber. This pattern of asymmetrical MHC isoform content along the length of single fibers suggests that the multiple myonuclei of a muscle fiber may express distinct myofibrillar isoforms in an uncoordinated fashion.

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“…Several studies have reported the transition from fast-to-slow muscle fiber types and MHC isoforms after resistance training (Roy et al, 1997;Carroll et al, 1998;Sharman et al, 2001). Kesidis et al (2008) observed a high percentage of fibers expressing MHCIIa and MHCI/ IIa in bodybuilders, compared to non-trained individuals. Similarly, Otis et al (2007) in a study on tumorbearing rats submitted to functional overload, observed a reduction in MHCIIb isoform, associated with increased levels of MHCI isoform.…”

Section: Skeletal Muscle Changes During Resistance Trainingmentioning

confidence: 99%

High‐Intensity Resistance Training with Insufficient Recovery Time Between Bouts Induce Atrophy and Alterations in Myosin Heavy Chain Content in Rat Skeletal Muscle

Souza

Aguiar

Carani

et al. 2011

The Anatomical Record

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The aim of this study was to test whether high-intensity resistance training with insufficient recovery time between bouts, could result in a decrease of muscle fiber cross-sectional area (CSA), alter fiber-type frequencies and myosin heavy chain (MHC) isoform content in rat skeletal muscle. Wistar rats were divided into two groups: trained (Tr) and control (Co). Tr group were subjected to a high-intensity resistance training program (5 days/week) for 12 weeks, involving jump bouts into water, carrying progressive overloads based on percentage body weight. At the end of experiment, animals were sacrificed, superficial white (SW) and deep red (DR) portions of the plantaris muscle were removed and submitted to mATPase histochemical reaction and SDS-PAGE analysis. Throughout the experiment, both groups increased body weight, but Tr was lower than Co. There was a significant reduction in IIA and IID muscle fiber CSA in the DR portion of Tr compared to Co. Muscle fiber-type frequencies showed a reduction in Types I and IIA in the DR portion and IID in the SW portion of Tr compared to Co; there was an increase in Types IIBD frequency in the DR portion. Change in muscle fiber-type frequency was supported by a significant decrease in MHCI and MHCIIa isoforms accompanied by a significant increase in MHCIIb isoform content. MHCIId showed no significant differences between groups. These data show that high-intensity resistance training with insufficient recovery time between bouts promoted muscle atrophy and a transition from slow-to-fast contractile activity in rat plantaris muscle. Anat Rec, 294:1393Rec, 294: -1400Rec, 294: , 2011. V V C 2011 Wiley-Liss, Inc.

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Myosin heavy chain isoform distribution in single fibres of bodybuilders

Cited by 21 publications

References 29 publications

Pilot study identifying myosin heavy chain 7, desmin, insulin‐like growth factor 7, and annexin A2 as circulating biomarkers of human heart failure

Pilot study identifying myosin heavy chain 7, desmin, insulin‐like growth factor 7, and annexin A2 as circulating biomarkers of human heart failure

The continuum of hybrid IIX/IIB fibers in normal mouse muscles: MHC isoform proportions and spatial distribution within single fibers

High‐Intensity Resistance Training with Insufficient Recovery Time Between Bouts Induce Atrophy and Alterations in Myosin Heavy Chain Content in Rat Skeletal Muscle

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