α-Actinin and Filamin Cooperatively Enhance the Stiffness of Actin Filament Networks

BACKGROUND: The close subcellular proximity of different actin filament crosslinking proteins suggests that these proteins may cooperate to organize F-actin structures to drive complex cellular functions during cell adhesion, motility and division. Here we hypothesize that alpha-actinin and filamin, two major F-actin crosslinking proteins that are both present in the lamella of adherent cells, display synergistic mechanical functions. METHODOLOGY/PRINCIPAL FINDINGS: Using quantitative rheology, we find that combining alpha-actinin and filamin is much more effective at producing elastic, solid-like actin filament networks than alpha-actinin and filamin separately. Moreover, F-actin networks assembled in the presence of alpha-actinin and filamin strain-harden more readily than networks in the presence of either alpha-actinin or filamin. SIGNIFICANCE: These results suggest that cells combine auxiliary proteins with similar ability to crosslink filaments to generate stiff cytoskeletal structures, which are required for the production of internal propulsive forces for cell migration, and that these proteins do not have redundant mechanical functions

Ultrasound-Diagnosed Tibia Stress Fracture: A Case Report

Stress fractures are a frequent cause of lower extremity pain in athletes, and especially in runners. Plain imaging has a low sensitivity. Magnetic resonance imaging (MRI) or bone scan scintigraphy is the criterion standard, but expensive. We present the case of a young female distance runner with left shin pain. Plain radiography was unremarkable. Ultrasound showed focal hyperechoic elevation of the periosteum with irregularity over the distal tibia and increased flow on Doppler. These findings were consistent with a distal tibia stress fracture and confirmed by MRI. Examination of our case will highlight the utility of considering an ultrasound for diagnosis of tibial stress fracture