Response to Mechanical Properties and Physiological Challenges of Fascia: Diagnosis and Rehabilitative Therapeutic Intervention for Myofascial System Disorders.

Damage to the fascia can cause significant performance deficits in high-performance sports and recreational exercise and may contribute to the development of musculoskeletal disorders and persistent potential pain. The fascia is widely distributed from head to toe, encompassing muscles, bones, blood vessels, nerves, and internal organs and comprising various layers of different depths, indicating the complexity of its pathogenesis. It is a connective tissue composed of irregularly arranged collagen fibers, distinctly different from the regularly arranged collagen fibers found in tendons, ligaments, or periosteum, and mechanical changes in the fascia (stiffness or tension) can produce changes in its connective tissue that can cause pain. While these mechanical changes induce inflammation associated with mechanical loading, they are also affected by biochemical influences such as aging, sex hormones, and obesity. Therefore, this paper will review the current state of knowledge on the molecular level response to the mechanical properties of the fascia and its response to other physiological challenges, including mechanical changes, innervation, injury, and aging; imaging techniques available to study the fascial system; and therapeutic interventions targeting fascial tissue in sports medicine. This article aims to summarize contemporary views.

Rapid identification of ligand-binding sites by using an assignment-free NMR approach.

In this study, we developed an assignment-free approach for rapid identification of ligand-binding sites in target proteins by using NMR. With a sophisticated cell-free stable isotope-labeling procedure that introduces (15)N- or (13)C-labels to specific atoms of target proteins, this approach requires only a single series of ligand titrations with labeled targets. Using titration data, ligand-binding sites in the target protein can be identified without time-consuming assignment procedures. We demonstrated the feasibility of this approach by using structurally well-characterized interactions between mitogen-activated protein (MAP) kinase p38α and its inhibitor 2-amino-3-benzyloxypyridine. Furthermore, we confirmed the recently proposed fatty acid binding to p38α and confirmed the fatty acid-binding site in the MAP kinase insert region.