Evaluation of a point-of-care ultrasound curriculum and ocular phantom in residency training.

Specialized training in ocular ultrasound is not a focus for most emergency medicine residencies, despite the fact that it allows physicians to quickly and accurately identify ocular pathology and prioritize emergency ophthalmological consultations. Therefore, we tested the value of utilizing normal and pathologic ocular ultrasound phantoms as a training tool for residents. Twenty emergency medicine residents were given a pre-test including written and practical skills diagnosis of ocular phantom pathologies, a short video on common ocular pathologies, practice time with the phantoms and a post-test including written and scanning components. Residents were then asked to complete an overall evaluation of the learning activity. After didactic and hands-on training with phantoms, residents demonstrated a significant increase in knowledge, skills and preparedness for diagnosing real patients with ocular pathologies. Overall, the phantoms allowed residents an unrestricted opportunity to practice and refine their technique. This study provided a framework for teaching emergency medicine residents the basics of ocular US through a brief didactic and practical intervention using novel ocular pathology US phantoms. Our curriculum resulted in both objective and subjective improvement in residents' performance and understanding of ocular US.

The N-terminus of thrombospondin: the domain stands apart.

Thrombospondin 1 (TSP1) was first recognized as a thrombin-sensitive protein associated with platelet membranes. It is secreted by numerous cell types and its expression is predominant in areas of active tissue remodeling. Thrombospondins 1 and 2 are large, trimeric, matricellular proteins, composed of multiple structural motifs which interact with a diverse array of receptors and molecules. Thrombospondin's capacity to bind multiple receptors renders it multifunctional. The functions of its isolated domains can be overlapping or contradictory. In this review, we focus on the N-terminus of the molecule, first recognized for its strong heparin binding properties and characterized by its susceptibility to proteolytic cleavage from the stalk region of thrombospondin. The N-terminus, called the heparin binding domain (HBD), interacts with a variety of macromolecules including heparan sulfate proteoglycans at the membrane and in the matrix, LDL receptor-related protein (LRP), sulfated glycolipids, calreticulin, and integrins. The HBD mediates endocytosis of thrombospondin. It functions both as a soluble and an insoluble modulator of cell adhesion and motility. In contrast to thrombospondin, the HBD has pro-angiogenic activity. We propose that the HBD of thrombospondins 1 and 2 are found primarily in the cellular microenvironment in conditions of cellular injury, stress and tissue remodeling and that the HBD conveys multiple signals involved in cellular adaptation to injury.