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Proteomes
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Striated Muscle Proteomics II
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Striated Muscle Proteomics II

A special issue of Proteomes (ISSN 2227-7382).

Deadline for manuscript submissions: closed (15 April 2021) | Viewed by 17684

Special Issue Editor

Prof. Dr. Jatin G. Burniston

E-Mail Website
Guest Editor
Research Institute for Sport & Exercise Sciences, Liverpool John Moores University, Liverpool L3 3AF, UK
Interests: dynamic proteome profiling; proteome responses to exercise; striated muscle proteomics
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

We warmly invite contributions that enhance our understanding regarding cardiac and skeletal muscle biology. Striated muscle is a fascinating tissue that exhibits profound plasticity in response to mechanical loading, nutrition, and exogenous agents. Skeletal muscle undergoes a complex developmental process that creates mature multinucleate fibres exhibiting a broad range of different phenotypes. In response to endurance exercise, muscle can more than double its mitochondrial content, whereas resistance exercise stimulates protein accretion and substantial myofibre hypertrophy. Interestingly, cardiac muscle is exposed to a continuous rhythmic workload, yet pathological and physiological stimuli result in discrete forms of cardiac hypertrophy.

Muscle is the target of monogenic diseases, including muscular dystrophies and complex polygenic diseases such as type 2 diabetes. Similarly, cardiomyopathies occur due to inherited or environmental factors and are often progressive processes that coincide with other complicated risk factors, such as low exercise capacity, hypertension and dyslipidaemia. Therefore, understanding the deterioration of cardiac performance is a particularly challenging area of research. Indeed, from adulthood to old-age, the natural decline in muscle mass and cardiac function negatively impact individuals’ functional independence and health-span.

Striated muscle is a technically challenging substrate for proteomic investigation, and so we also welcome methodological articles that aim to address muscle-specific issues. We hope this Special Issue will serve as a point of reference for burgeoning themes in striated muscle proteomics.

Prof. Dr. Jatin G Burniston
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Proteomes is an international peer-reviewed open access quarterly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1800 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • adaptation to exercise
  • anabolic agents
  • cancer cachexia
  • cardiac muscle
  • cardiomyopathy
  • disuse atrophy
  • heart failure
  • insulin resistance
  • muscle development
  • muscle mitochondria
  • muscle wasting
  • muscular dystrophy
  • myofibre phenotyping
  • myopathy
  • physiological/ pathological cardiac hypertrophy
  • sarcopenia

Published Papers (4 papers)

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Research

23 pages, 2002 KiB  
Article
Advanced Fiber Type-Specific Protein Profiles Derived from Adult Murine Skeletal Muscle
by Britta Eggers, Karin Schork, Michael Turewicz, Katalin Barkovits, Martin Eisenacher, Rolf Schröder, Christoph S. Clemen and Katrin Marcus
Proteomes 2021, 9(2), 28; https://doi.org/10.3390/proteomes9020028 - 08 Jun 2021
Cited by 16 | Viewed by 5363
Abstract
Skeletal muscle is a heterogeneous tissue consisting of blood vessels, connective tissue, and muscle fibers. The last are highly adaptive and can change their molecular composition depending on external and internal factors, such as exercise, age, and disease. Thus, examination of the skeletal [...] Read more.
Skeletal muscle is a heterogeneous tissue consisting of blood vessels, connective tissue, and muscle fibers. The last are highly adaptive and can change their molecular composition depending on external and internal factors, such as exercise, age, and disease. Thus, examination of the skeletal muscles at the fiber type level is essential to detect potential alterations. Therefore, we established a protocol in which myosin heavy chain isoform immunolabeled muscle fibers were laser microdissected and separately investigated by mass spectrometry to develop advanced proteomic profiles of all murine skeletal muscle fiber types. All data are available via ProteomeXchange with the identifier PXD025359. Our in-depth mass spectrometric analysis revealed unique fiber type protein profiles, confirming fiber type-specific metabolic properties and revealing a more versatile function of type IIx fibers. Furthermore, we found that multiple myopathy-associated proteins were enriched in type I and IIa fibers. To further optimize the assignment of fiber types based on the protein profile, we developed a hypothesis-free machine-learning approach, identified a discriminative peptide panel, and confirmed our panel using a public data set. Full article
(This article belongs to the Special Issue Striated Muscle Proteomics II)
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15 pages, 1949 KiB  
Article
Phosphorylation-Dependent Interactome of Ryanodine Receptor Type 2 in the Heart
by David Y. Chiang, Satadru Lahiri, Guoliang Wang, Jason Karch, Meng C. Wang, Sung Y. Jung, Albert J. R. Heck, Arjen Scholten and Xander H. T. Wehrens
Proteomes 2021, 9(2), 27; https://doi.org/10.3390/proteomes9020027 - 07 Jun 2021
Cited by 10 | Viewed by 3858
Abstract
Hyperphosphorylation of the calcium release channel/ryanodine receptor type 2 (RyR2) at serine 2814 (S2814) is associated with multiple cardiac diseases including atrial fibrillation and heart failure. Despite recent advances, the molecular mechanisms driving pathological changes associated with RyR2 S2814 phosphorylation are still not [...] Read more.
Hyperphosphorylation of the calcium release channel/ryanodine receptor type 2 (RyR2) at serine 2814 (S2814) is associated with multiple cardiac diseases including atrial fibrillation and heart failure. Despite recent advances, the molecular mechanisms driving pathological changes associated with RyR2 S2814 phosphorylation are still not well understood. Methods: Using affinity-purification coupled to mass spectrometry (AP-MS), we investigated the RyR2 interactome in ventricles from wild-type (WT) mice and two S2814 knock-in mutants: the unphosphorylated alanine mutant (S2814A) and hyperphosphorylated mimic aspartic acid mutant (S2814D). Western blots were used for validation. Results: In WT mouse ventricular lysates, we identified 22 proteins which were enriched with RyR2 pull-down relative to both IgG control and no antibody (beads-only) pull-downs. Parallel AP-MS using WT, S2814A, and S2814D mouse ventricles identified 72 proteins, with 20 being high confidence RyR2 interactors. Of these, 14 had an increase in their binding to RyR2 S2814A but a decrease in their binding to RyR2 S2814D. We independently validated three protein hits, Idh3b, Aifm1, and Cpt1b, as RyR2 interactors by western blots and showed that Aifm1 and Idh3b had significantly decreased binding to RyR2 S2814D compared to WT and S2814A, consistent with MS findings. Conclusion: By applying state-of-the-art proteomic approaches, we discovered a number of novel RyR2 interactors in the mouse heart. In addition, we found and defined specific alterations in the RyR2 interactome that were dependent on the phosphorylation status of RyR2 at S2814. These findings yield mechanistic insights into RyR2 regulation which may guide future drug designs. Full article
(This article belongs to the Special Issue Striated Muscle Proteomics II)
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13 pages, 2967 KiB  
Article
Western Diet Induced Remodelling of the Tongue Proteome
by Mriga Dutt, Yaan-Kit Ng, Jeffrey Molendijk, Hamzeh Karimkhanloo, Luoping Liao, Ronnie Blazev, Magdalene K. Montgomery, Matthew J. Watt and Benjamin L. Parker
Proteomes 2021, 9(2), 22; https://doi.org/10.3390/proteomes9020022 - 12 May 2021
Cited by 5 | Viewed by 4071
Abstract
The tongue is a heavily innervated and vascularized striated muscle that plays an important role in vocalization, swallowing and digestion. The surface of the tongue is lined with papillae which contain gustatory cells expressing various taste receptors. There is growing evidence to suggest [...] Read more.
The tongue is a heavily innervated and vascularized striated muscle that plays an important role in vocalization, swallowing and digestion. The surface of the tongue is lined with papillae which contain gustatory cells expressing various taste receptors. There is growing evidence to suggest that our perceptions of taste and food preference are remodelled following chronic consumption of Western diets rich in carbohydrate and fats. Our sensitivity to taste and also to metabolising Western diets may be a key factor in the rising prevalence of obesity; however, a systems-wide analysis of the tongue is lacking. Here, we defined the proteomic landscape of the mouse tongue and quantified changes following chronic consumption of a chow or Western diet enriched in lipid, fructose and cholesterol for 7 months. We observed a dramatic remodelling of the tongue proteome including proteins that regulate fatty acid and mitochondrial metabolism. Furthermore, the expressions of several receptors, metabolic enzymes and hormones were differentially regulated, and are likely to provide novel therapeutic targets to alter taste perception and food preference to combat obesity. Full article
(This article belongs to the Special Issue Striated Muscle Proteomics II)
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22 pages, 2440 KiB  
Article
Diurnal Differences in Human Muscle Isometric Force In Vivo Are Associated with Differential Phosphorylation of Sarcomeric M-Band Proteins
by Zulezwan Ab Malik, Kelly A. Bowden Davies, Elliott C. R. Hall, Jennifer Barrett, Samuel A. Pullinger, Robert M. Erskine, Sam O. Shepherd, Zafar Iqbal, Ben J. Edwards and Jatin G. Burniston
Proteomes 2020, 8(3), 22; https://doi.org/10.3390/proteomes8030022 - 26 Aug 2020
Cited by 7 | Viewed by 3597
Abstract
We investigated whether diurnal differences in muscle force output are associated with the post-translational state of muscle proteins. Ten physically active men (mean ± SD; age 26.7 ± 3.7 y) performed experimental sessions in the morning (08:00 h) and evening (17:00 h), which [...] Read more.
We investigated whether diurnal differences in muscle force output are associated with the post-translational state of muscle proteins. Ten physically active men (mean ± SD; age 26.7 ± 3.7 y) performed experimental sessions in the morning (08:00 h) and evening (17:00 h), which were counterbalanced in order of administration and separated by at least 72 h. Knee extensor maximal voluntary isometric contraction (MVIC) force and peak rate of force development (RFD) were measured, and samples of vastus lateralis were collected immediately after exercise. MVIC force was greater in the evening (mean difference of 67 N, 10.2%; p < 0.05). Two-dimensional (2D) gel analysis encompassed 122 proteoforms and discovered 6 significant (p < 0.05; false discovery rate [FDR] = 10%) diurnal differences. Phosphopeptide analysis identified 1693 phosphopeptides and detected 140 phosphopeptides from 104 proteins that were more (p < 0.05, FDR = 22%) phosphorylated in the morning. Myomesin 2, muscle creatine kinase, and the C-terminus of titin exhibited the most robust (FDR < 10%) diurnal differences. Exercise in the morning, compared to the evening, coincided with a greater phosphorylation of M-band-associated proteins in human muscle. These protein modifications may alter the M-band structure and disrupt force transmission, thus potentially explaining the lower force output in the morning. Full article
(This article belongs to the Special Issue Striated Muscle Proteomics II)
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