Temporomandibular disorder (TMD) is a disease of multifactorial etiology and a complex of symptoms, related to disorders of the masticatory muscles, temporomandibular joints and the surrounding orofacial structures. One of the main problems in the course of TMD disorders is the systematic increase in the tension of the masticatory muscles (masseter muscles, temporalis and medial and lateral pterygoid muscles), what is the cause of many damages and the development of pathological conditions in the stomatognathic system. The article discusses the differences in the structure of the masticatory and skeletal muscles, as well as the different nature and isoforms of myosin, which determines the much faster generation of contraction in the masticatory muscles and consequently easier generation of excessive, harmful tensions in the masticatory muscles. The article describes the causes of increased tension in the masticatory muscles and methods of their relaxation used in the basic and supportive treatment of temporomandibular disorders. The use of occlusal splints, physiotherapeutic procedures and TMD treatment with botulinum toxin type A were characterized. A role of psychological support and the methods used for patients with TMD were emphasized.

The compact smooth muscle 10S myosin II is a type of a monomer with folded tail and the heads bending back to interact with each other. This inactivated form is associated with regulatory and enzymatic activities affecting myosin processivity with actin filaments as well as ATPase activity. Phosphorylation by RLC can however, shuttle myosin from the inhibited 10S state to an activated 6S state, dictating the equilibrium. Multiple studies contributed by TEM have provided insights in the structural understanding of the 10S form. However, it is only recently that the true potential of Cryo-EM in deciphering the intramolecular interactions of 10S myosin state has been realized. This has led to an influx of new revelations on the 10S inactivation, unfolding mechanism and association in various diseases. This study reviews the gradual development in the structural interpretation of 10S species from TEM to Cryo-EM era. Furthermore, we discuss the utility of Cryo-EM in future myosin 10S studies and its contribution to human health.

Heating is a vital step in the gelation of surimi. Conventional water bath heating (WB) has the advantages of easy operation and low equipment requirements. However, the slow heat penetration during WB may lead to poor gel formation or gels prone to deterioration, especially with one-step heating. The two-step WB is time-consuming, and a large amount of water used tends to cause environmental problems. This review focuses on key factors affecting the quality of surimi gels in various heating technologies, such as surimi protein structure, chemical forces, or the activity of endogenous enzymes. In addition, the relationships between these factors and the gel performance of surimi under various heating modes are discussed by analyzing the heating temperature and heating rate. Compared with WB, the gel performance can be improved by controlling the heating conditions of microwave heating and ohmic heating, which are mainly achieved by changing the molecular structure of myofibrillar proteins or the activity of endogenous enzymes in surimi. Nevertheless, the novel thermal technologies still face several limitations and further research is needed to realize large-scale industrial production. This review provides ideas and directions for developing heat-induced surimi products with excellent gel properties.

The development of myofibrillar proteins drinks (MPDs) can provide meat protein nutrition to specific groups of people. However, one major challenge is that myofibrillar proteins (MPs) are insoluble in solutions with a low ionic strength. Another functional constraint is the susceptibility of MPs to heat-induced aggregation. Currently, the primary approach used to improve the water solubility of MPs is to inhibit the assembly of myofilaments. Increasing the thermostability of MPs primarily inhibits the aggregation of myosin or oxidizes myosin to soluble substances. This review focuses on the description of several chemical and physical strategies, with an emphasis on the advantages, disadvantages, and recent progress. Under the myosin filament assembly process and the cross-linking aggregation mechanism, this summary helps improve our understanding of the solution and thermostability of MPs in low-ionic-strength solutions, thus providing new ideas to the development of MPDs.

The 1968 review article on Calcium ion and muscle contraction by Setsuro Ebashi and Makoto Endo is one of the highest cited in the journal since it was required reading in the early days of understanding what triggers contraction of the myofilaments. It correctly identified the major steps in excitation-contraction coupling and still inspires mathematical models of muscle activity today. It also successfully identified the role of troponin.

Congestive heart failure (HF) remains a major cause of cardiac-related morbidity and mortality, despite major therapeutic advancements. A newer class of medications has recently been developed which targets the root cause of HF, which is reduced myocardial contractility. This article aims to highlight the cardiac myosin activator class of drugs and the trials to date highlighting their effects on HF outcomes.

As studies examining the hypertrophic effects of resistance training (RT) at the cellular level have produced inconsistent results, we performed a systematic review and meta-analysis to investigate muscle fiber size before and after a structured RT intervention in older adults. A random-effects model was used to calculate mean effect size (ES) and 95% confidence intervals (CI). Thirty-five studies were included (age range: 59.0-88.5 yr), and 44 and 30 effects were used to estimate RT impact on myosin heavy chain (MHC) I and II fiber size. RT produced moderate-to-large increases in MHC I (ES = +0.51, 95%CI +0.31 to +0.71; P < 0.001) and II (ES = +0.81, 95%CI +0.56 to +1.05; P < 0.001) fiber size, with men and women having a similar response. Age was negatively associated with change in muscle fiber size for both fiber types (MHC I: R2 = 0.11, β = -0.33, P = 0.002; MHC II: R2 = 0.10, β = -0.32, P = 0.04), indicating a less robust hypertrophic response as age increases in older adults. Unexpectedly, a higher training intensity (defined as percentage of one-repetition maximum) was associated with a smaller increase in MHC II fiber size (R2 = 15.09%, β = -0.39, P = 0.01). Notably, MHC II fiber subtypes (IIA, IIX, IIAX) were examined less frequently, but RT improved their size. Overall, our findings indicate that RT induces cellular hypertrophy in older adults, although the effect is attenuated with increasing age. In addition, hypertrophy of MHC II fibers was reduced with higher training intensity, which may suggest a failure of muscle fibers to hypertrophy in response to high loads in older adults.

Most GTPases and many ATPases belong to the P-loop class of proteins with significant structural and mechanistic similarities. Here we compare and contrast the basic properties of the Ras family GTPases and myosin, and conclude that there are fundamental similarities but also distinct differences related to their specific roles. © 2016 Wiley Periodicals, Inc. Biopolymers 105: 422-430, 2016.