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SUMMARYThis paper describes the use of topology optimization as a synthesis tool for the design of largedisplacement compliant mechanisms. An objective function for the synthesis of large-displacement mechanisms is proposed together with a formulation for synthesis of path-generating compliant mechanisms. The responses of the compliant mechanisms are modelled using a total Lagrangian ÿnite element formulation, the sensitivity analysis is performed using the adjoint method and the optimization problem is solved using the method of moving asymptotes. Procedures to circumvent some numerical problems are discussed.

Abstract-We propose a novel algorithm for sensor selflocalization in cooperative wireless networks where observations of relative sensor distances are available. The variational message passing (VMP) algorithm is used to implement a mean field solution to the estimation of the posterior probabilities of the sensor positions in an R 2 scenario. Extension to R 3 is straightforward. Compared to non-parametric methods based on belief propagation, the VMP algorithm features significantly lower communication overhead between sensors. This is supported by performance simulations which show that the estimated mean localization error of the algorithm stabilizes after approximately 30 iterations.

Ficolins are soluble molecules that bind carbohydrate present on the surface of microorganisms and function as recognition molecules in the lectin complement pathway. Three ficolins have been identified in humans: ficolin-1, ficolin-2, and ficolin-3. Ficolin-1 is synthesized in monocytes and type II alveolar epithelial cells. Ficolin-1 has been shown to be present in secretory granules of human neutrophils, but it is not known which subset of the neutrophils' secretory granules harbors ficolin-1. To determine the exact subcellular localization of ficolin-1 in neutrophils, recombinant ficolin-1 was expressed in Chinese hamster ovary cells and used for generation of polyclonal antibodies. This allowed detection of ficolin-1 in subcellular fractions of human neutrophils by ELISA, by Western blotting, and by immunohistochemistry. Real-time PCR examination of normal human bone marrow showed FCN1 gene expression largely in myelocytes, metamyelocytes, and band cells with a profile quite similar to that of gelatinase. In accordance with this, biosynthesis studies of neutrophils precursor cells showed that ficolin-1 was primarily synthesized in myelocytes, metamyelocytes, and band cells. Immunohistochemistry and subcellular fractionation demonstrated that ficolin-1 is primarily localized in gelatinase granules but also in highly exocytosable gelatinase-poor granules, not described previously. Ficolin-1 is released from neutrophil granules by stimulation with fMLP or PMA, and the majority becomes associated with the surface membrane of the cells and can be detected by flow cytometry. Our studies show that neutrophils are a major source of ficolin-1, which can be readily exocytosed by stimulation.

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