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Muscle Proteins: Recent Advances and Prospects
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Muscle Proteins: Recent Advances and Prospects

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Macromolecules".

Deadline for manuscript submissions: closed (15 April 2024) | Viewed by 2717

Special Issue Editor

Dr. Ivan M. Vikhlyantsev

E-Mail Website
Guest Editor
Laboratory of Structure and Functions of Muscle Proteins, Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, 142290 Pushchino, Russia
Interests: striated muscles; giant sarcomeric cytoskeleton proteins; muscle disuse and muscle disease; hibernation

Special Issue Information

Dear Colleagues,

More than 100 years have passed since the discovery of myosin peptone which initiated research into muscle proteins. Many discoveries have been made since then in the field of the structural and molecular biology of striated and smooth muscles. Three types of filaments in muscle cells have been discovered, and giant proteins have been found that form a three-dimensional elastic matrix and are involved in the regulation of many processes of intracellular signaling in the norm and under pathological conditions. The amyloidogenic properties of muscle proteins have been determined; their involvement in the development of aging and age-related changes in muscle cells has been shown.

This Special Issue aims to generalize and expand knowledge concerning striated and smooth muscle proteins. Authors are invited to submit original research and review articles on the current state and progress in the field of muscle biology.

Topics include, but are not limited to, the following:

  • Structure and functions of proteins of thick and thin filaments of striated and smooth muscles;
  • Giant muscle proteins; their roles in the norm and in pathology;
  • Molecular mechanisms of muscle disuse;
  • Molecular and cellular mechanisms in muscles at the development of age-dependent diseases and aging.

Dr. Ivan M. Vikhlyantsev
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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

  • striated and smooth muscles
  • thick and thin filament proteins
  • giant sarcomeric cytoskeleton proteins
  • muscle disuse and muscle disease
  • muscle aging

Published Papers (2 papers)

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20 pages, 736 KiB  
Review
Direct Effects of Toxic Divalent Cations on Contractile Proteins with Implications for the Heart: Unraveling Mechanisms of Dysfunction
by Oksana P. Gerzen, Veronika O. Votinova, Iulia K. Potoskueva, Alyona E. Tzybina and Larisa V. Nikitina
Int. J. Mol. Sci. 2023, 24(13), 10579; https://doi.org/10.3390/ijms241310579 - 24 Jun 2023
Cited by 3 | Viewed by 1573
Abstract
The binding of calcium and magnesium ions to proteins is crucial for regulating heart contraction. However, other divalent cations, including xenobiotics, can accumulate in the myocardium and enter cardiomyocytes, where they can bind to proteins. In this article, we summarized the impact of [...] Read more.
The binding of calcium and magnesium ions to proteins is crucial for regulating heart contraction. However, other divalent cations, including xenobiotics, can accumulate in the myocardium and enter cardiomyocytes, where they can bind to proteins. In this article, we summarized the impact of these cations on myosin ATPase activity and EF-hand proteins, with special attention given to toxic cations. Optimal binding to EF-hand proteins occurs at an ionic radius close to that of Mg2+ and Ca2+. In skeletal Troponin C, Cd2+, Sr2+, Pb2+, Mn2+, Co2+, Ni2+, Ba2+, Mg2+, Zn2+, and trivalent lanthanides can substitute for Ca2+. As myosin ATPase is not a specific MgATPase, Ca2+, Fe2+, Mn2+, Ni2+, and Sr2+ could support myosin ATPase activity. On the other hand, Zn2+ and Cu2 significantly inhibit ATPase activity. The affinity to various divalent cations depends on certain proteins or their isoforms and can alter with amino acid substitution and post-translational modification. Cardiac EF-hand proteins and the myosin ATP-binding pocket are potential molecular targets for toxic cations, which could significantly alter the mechanical characteristics of the heart muscle at the molecular level. Full article
(This article belongs to the Special Issue Muscle Proteins: Recent Advances and Prospects)
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11 pages, 1724 KiB  
Brief Report
The Role of Branched Chain Ketoacid Dehydrogenase Kinase (BCKDK) in Skeletal Muscle Biology and Pathogenesis
by Joshua Fernicola, Sagar Vyavahare, Sonu Kumar Gupta, Aditya Kalwaghe, Kate Kosmac, Adam Davis, Matthew Nicholson, Carlos M. Isales, Rahul Shinde and Sadanand Fulzele
Int. J. Mol. Sci. 2024, 25(14), 7601; https://doi.org/10.3390/ijms25147601 - 11 Jul 2024
Viewed by 846
Abstract
Muscle wasting can be caused by nutrition deficiency and inefficient metabolism of amino acids, including Branched Chain Amino Acids (BCAAs). Branched Chain Amino Acids are a major contributor to the metabolic needs of healthy muscle and account for over a tenth of lean [...] Read more.
Muscle wasting can be caused by nutrition deficiency and inefficient metabolism of amino acids, including Branched Chain Amino Acids (BCAAs). Branched Chain Amino Acids are a major contributor to the metabolic needs of healthy muscle and account for over a tenth of lean muscle mass. Branched chain alpha-ketoacid dehydrogenase (BCKD) is the rate limiting enzyme of BCAA metabolism. Inhibition of BCKD is achieved through a reversible phosphorylation event by Branched Chain a-ketoacid dehydrogenase kinase (BCKDK). Our study set out to determine the importance of BCKDK in the maintenance of skeletal muscle. We used the Gene Expression Omnibus Database to understand the role of BCKDK in skeletal muscle pathogenesis, including aging, muscular disease, and interrupted muscle metabolism. We found BCKDK expression levels were consistently decreased in pathologic conditions. These results were most consistent when exploring muscular disease followed by aging. Based on our findings, we hypothesize that decreased BCKDK expression alters BCAA catabolism and impacts loss of normal muscle integrity and function. Further research could offer valuable insights into potential therapeutic strategies for addressing muscle-related disorders. Full article
(This article belongs to the Special Issue Muscle Proteins: Recent Advances and Prospects)
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