Distributed Finite Time Consensus of Secondorder Multi-agent Systems via Pinning Control (August 2018).

The robust distributed finite time consensus of second-order multi-agent systems via pinning control has been investigated in this paper. A new nonsingular finite time TSM control method is proposed for second-order single system with disturbances. Based on the pinning error function vector, robust distributed finite time consensus of second-order multi-agent systems via pinning control method is given. Simulations results are performed to validate the effectiveness of the theoretical results.

Preparation of tissue-specific monoclonal antibodies using purified endothelial membrane proteins from biotinylated pulmonary vasculature of rhesus monkey.

In the present study, we perfused the rhesus lung vascular bed in situ with sulfo-NHS-LC-Biotin to biotinylate its luminal surface membrane proteins. After homogenization, dialysis, and affinity chromatography, biotinylated endothelial membrane proteins were successfully isolated and characterized as enriched endothelial membrane proteins with no contamination of intracellular proteins. When they were used as immunogens to develop monoclonal antibodies (MAbs), three MAbs--TX111, TX112, and TX113--were obtained. Among them, TX111 was demonstrated to specifically bind to rhesus lung tissue by Western blotting and enzymelinked immunosorbent assay (ELISA)--that is, positively stained capillary endothelium of rhesus lung. The molecular weight of the corresponding antigen for TX111 was approximately 70 kDa under reducing conditions. TX111 also reacted with human lung homogenate, but not with rat lung homogenate. These results suggest that (1) the biotinylation method is applicable for isolating endothelial proteins in situ from large animals; (2) anti-human protein MAbs are likely to be obtained using monkey proteins; and (3) TX111 is potentially useful for pulmonary vascular targeting.

A novel method to isolate and map endothelial membrane proteins from pulmonary vasculature.

Vascular endothelium has attracted extensive attention due to its important role in many physiological and pathological processes. Many methods have been developed to study the components and their functions in vascular endothelium. Here we report a novel approach to investigate vascular endothelium using normal rat lungs as the model. We perfused lung vascular beds with sulfosuccinimidyl-6-(biotinamido) hexanoate, a biotin analog, to label endothelial membrane proteins. The biotinylated proteins were isolated from lung homogenate with immobilized monomeric avidin and confirmed to be highly pure endothelial membrane proteins with little contamination of intracellular proteins. These biotinylated proteins were used as immunogens for development of monoclonal antibodies. Indeed, newly generated monoclonal antibodies have revealed different expression patterns of proteins across tissues. Some proteins were found highly specifically expressed to capillary vessels of pulmonary vasculature. This method has also been proven useful for investigating vasculature of other organs, as this study explored.

Lung endothelium targeting for pulmonary embolism thrombolysis.

BACKGROUND: Pulmonary embolism occurs frequently in hospitalized patients. Thrombolytic therapy, currently used as the major treatment, has often been associated with severe bleeding complications and has thereby been life-threatening. We have developed a novel therapeutic method based on our newly created pulmonary endothelium-specific antibody. METHODS AND RESULTS: We isolated membrane proteins of rat pulmonary vascular luminal endothelium and obtained a monoclonal antibody, RE8F5, which antigen was uniquely expressed by the pulmonary capillary endothelium. In vivo biodistribution showed that RE8F5 and its urokinase conjugate were rapidly and specifically accumulated in lung. Urokinase and the conjugate were compared in rats with pulmonary, hepatic, and lower-limb embolus. In a pulmonary embolus model, the conjugate exhibited 12-fold enhanced thrombolytic potency over urokinase, whereas plasma fibrinogen and bleeding time were unaffected. In 2 other models, no significant thrombolysis was induced by the conjugate. In contrast, thrombolysis by urokinase was found to be comparable to the pulmonary embolus model. In addition, urokinase caused significant consumption of fibrinogen in all experiments. CONCLUSIONS: These data show that urokinase equipped with lung endothelium-specific antibody is an ideal treatment for pulmonary embolism, with a high efficacy of thrombolysis and low risk of bleeding.