Exploiting flow dynamics for super-resolution in contrast-enhanced ultrasound

Ultrasound localization microscopy offers new radiation-free diagnostic tools for vascular imaging deep within the tissue. Sequential localization of echoes returned from inert microbubbles with low-concentration within the bloodstream reveal the vasculature with capillary resolution. Despite its high spatial resolution, low microbubble concentrations dictate the acquisition of tens of thousands of images, over the course of several seconds to tens of seconds, to produce a single super-resolved image. %since each echo is required to be well separated from adjacent microbubbles. Such long acquisition times and stringent constraints on microbubble concentration are undesirable in many clinical scenarios. To address these restrictions, sparsity-based approaches have recently been developed. These methods reduce the total acquisition time dramatically, while maintaining good spatial resolution in settings with considerable microbubble overlap. %Yet, non of the reported methods exploit the fact that microbubbles actually flow within the bloodstream. % to improve recovery. Here, we further improve sparsity-based super-resolution ultrasound imaging by exploiting the inherent flow of microbubbles and utilize their motion kinematics. While doing so, we also provide quantitative measurements of microbubble velocities. Our method relies on simultaneous tracking and super-localization of individual microbubbles in a frame-by-frame manner, and as such, may be suitable for real-time implementation. We demonstrate the effectiveness of the proposed approach on both simulations and {\it in-vivo} contrast enhanced human prostate scans, acquired with a clinically approved scanner.Comment: 11 pages, 9 figure

Avidity enhancement of L-selectin bonds by flow: shear-promoted rotation of leukocytes turn labile bonds into functional tethers

L-selectin is a key lectin essential for leukocyte capture and rolling on vessel walls. Functional adhesion of L-selectin requires a minimal threshold of hydrodynamic shear. Using high temporal resolution videomicroscopy, we now report that L-selectin engages its ligands through exceptionally labile adhesive bonds (tethers) even below this shear threshold. These tethers share a lifetime of 4 ms on distinct physiological ligands, two orders of magnitude shorter than the lifetime of the P-selectin–PSGL-1 bond. Below threshold shear, tether duration is not shortened by elevated shear stresses. However, above the shear threshold, selectin tethers undergo 14-fold stabilization by shear-driven leukocyte transport. Notably, the cytoplasmic tail of L-selectin contributes to this stabilization only above the shear threshold. These properties are not shared by P-selectin– or VLA-4–mediated tethers. L-selectin tethers appear adapted to undergo rapid avidity enhancement by cellular transport, a specialized mechanism not used by any other known adhesion receptor

Constructing bounded remainder sets and cut-and-project sets which are bounded distance to lattices, II

Recent results of several authors have led to constructions of parallelotopes which are bounded remainder sets for totally irrational toral rotations. In this brief note we explain, in retrospect, how some of these results can easily be obtained from a geometric argument which was previously employed by Duneau and Oguey in the study of deformation properties of mathematical models for quasicrystals

Dynamic ergosterol- and ceramide-rich domains in the peroxisomal membrane serve as an organizing platform for peroxisome fusion

We describe unusual ergosterol- and ceramide-rich (ECR) domains in the membrane of yeast peroxisomes. Several key features of these detergent-resistant domains, including the nature of their sphingolipid constituent and its unusual distribution across the membrane bilayer, clearly distinguish them from well characterized detergent-insoluble lipid rafts in the plasma membrane. A distinct set of peroxisomal proteins, including two ATPases, Pex1p and Pex6p, as well as phosphoinositide- and GTP-binding proteins, transiently associates with the cytosolic face of ECR domains. All of these proteins are essential for the fusion of the immature peroxisomal vesicles P1 and P2, the earliest intermediates in a multistep pathway leading to the formation of mature, metabolically active peroxisomes. Peroxisome fusion depends on the lateral movement of Pex1p, Pex6p, and phosphatidylinositol-4,5-bisphosphate–binding proteins from ECR domains to a detergent-soluble portion of the membrane, followed by their release to the cytosol. Our data suggest a model for the multistep reorganization of the multicomponent peroxisome fusion machinery that transiently associates with ECR domains