BackgroundThe skin, soft tissue, and most parts of the musculoskeletal system are relatively superficial anatomical structures and ideal targets for ultrasound examination in the emergency departments. Soft tissue and musculoskeletal ultrasound applications are relatively underused compared to traditional emergency applications, such as trauma, abdominal aortic aneurysm, and chest and cardiovascular systems.Main textIt is important to have knowledge about sonoanatomy and landmarks within the skin, soft tissue, and musculoskeletal systems. Portable machines equipped with high-resolution transducers are now available to fulfill this field of applications in many emergency departments. After needling practice, emergency physicians can not only diagnose and identify pathological findings but also provide interventional procedures and treatments. In this review, we will introduce point-of-care ultrasound (POCUS) applications regarding the soft tissue and musculoskeletal systems: soft tissue infections, joint effusions, foreign bodies, long bone fractures, muscle and tendon injuries, vascular occlusions, and procedures.ConclusionsWith POCUS, emergency physicians can visualize the structures beneath the skin and provide better and safer cares in the emergency departments.Electronic supplementary materialThe online version of this article (doi:10.1186/s40560-016-0173-0) contains supplementary material, which is available to authorized users.

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Titin, an elastic and giant myofibrillar protein, is responsible for generating passive tension and maintaining sarcomere structure in striated muscles. Several studies have reported attenuation of passive tension and disorganization of sarcomere in atrophic muscles, but the changes of titin have not been investigated after denervation. For this purpose, we used sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunofluorescent staining to examine titin in innervated and denervated tibialis anterior (TA) muscles of the rat. With increasing denervation time, we found a greater loss of titin than myosin heavy chain (MHC) and actin contents in atrophic TA muscle. The ratios of titin/MHC and titin/actin gradually decreased following denervation. In contrast, ratios of MHC/actin in the denervated groups showed no significant differences with the controls even at 56 days postdenervation. The ultrastructure of myofibrils also showed disturbed arrangements of myofilaments and a disorganized contractile apparatus in denervated muscle. Immunofluorescent staining displayed translocation of the titin epitope from the Z-line to the I-band, suggesting that the apparent cleavage of titin occurred near the Z-line region during the atrophying process. Our study provides evidence that titin is more sensitive to degradation than MHC and actin after denervation. Moreover, the titin decline results in the loss of titin-based sarcomeric integrity in atrophic muscle.

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