A polyhedral bound on the indeterminate contact forces in 2D fixturing and grasping arrangements

This paper considers 2D contact arrangements where several bodies grasp, fixture, or support an object via frictional point contacts. Within a strictly rigid body modelling paradigm, when an external wrench (i.e. force and torque) acts on the object, the reaction forces at the contacts are indeterminate and span an unbounded linear space. This paper analyzes the contact forces within a quasi-rigid body framework that keeps the desirable geometric properties of rigid body modelling, while also includes more realistic physical effects. Using two principles governing the mechanics of quasi-rigid contacts, we show that for any given external wrench acting on the object, the contact forces lie in a bounded polyhedral set. The polyhedral bound depends on the external wrench, the grasp's geometry, and the preload forces. But it does not depend on any detailed knowledge of the contact mechanics parameters. The bound is useful for "robust" grasp and fixture synthesis. Given a collection of external wrenches that may act on an object, the grasp's geometry and preload forces can be chosen such that all of these external wrenches would be automatically supported by the contacts

Focal Adhesion Kinase contributes to insulin-induced actin reorganization into a mesh harboring Glucose transporter-4 in insulin resistant skeletal muscle cells

<p>Abstract</p> <p>Background</p> <p>Focal Adhesion Kinase (FAK) is recently reported to regulate insulin resistance by regulating glucose uptake in C2C12 skeletal muscle cells. However, the underlying mechanism for FAK-mediated glucose transporter-4 translocation (Glut-4), responsible for glucose uptake, remains unknown. Recently actin remodeling was reported to be essential for Glut-4 translocation. Therefore, we investigated whether FAK contributes to insulin-induced actin remodeling and harbor Glut-4 for glucose transport and whether downregulation of FAK affects the remodeling and causes insulin resistance.</p> <p>Results</p> <p>To address the issue we employed two approaches: gain of function by overexpressing FAK and loss of function by siRNA-mediated silencing of FAK. We observed that overexpression of FAK induces actin remodeling in skeletal muscle cells in presence of insulin. Concomitant to this Glut-4 molecules were also observed to be present in the vicinity of remodeled actin, as indicated by the colocalization studies. FAK-mediated actin remodeling resulted into subsequent glucose uptake via PI3K-dependent pathway. On the other hand FAK silencing reduced actin remodeling affecting Glut-4 translocation resulting into insulin resistance.</p> <p>Conclusion</p> <p>The data confirms that FAK regulates glucose uptake through actin reorganization in skeletal muscle. FAK overexpression supports actin remodeling and subsequent glucose uptake in a PI3K dependent manner. Inhibition of FAK prevents insulin-stimulated remodeling of actin filaments resulting into decreased Glut-4 translocation and glucose uptake generating insulin resistance. To our knowledge this is the first study relating FAK, actin remodeling, Glut-4 translocation and glucose uptake and their interrelationship in generating insulin resistance.</p