Background: Several randomized controlled trials (RCTs) have demonstrated that intraoperative goal-directed fluid therapy (GDFT) can decrease postsurgical complications in patients undergoing major abdominal surgery. However, very few studies have demonstrated the value of goal-directed therapy (GDT) in patients undergoing orthopaedic surgery and confirmed it is as useful in real-life conditions. Therefore, we initiated a GDFT implementation programme in patients undergoing hip revision arthroplasty in order to assess its effects on postoperative complications (e.
View Article and Find Full Text PDFCytoplasmic dynein is a minus end-directed microtubule motor that performs distinct functions in interphase and mitosis. In interphase, dynein transports organelles along microtubules, whereas in metaphase this motor has been implicated in mitotic spindle formation and orientation as well as chromosome segregation. The manner in which dynein activity is regulated during the cell cycle, however, has not been resolved.
View Article and Find Full Text PDFKinesin is a microtubule-based motor protein involved in intracellular organelle transport. Neurons are characterized by the presence of at least two isoforms of conventional kinesin: ubiquitous kinesin, expressed in all cells and tissues, and neuronal kinesin, whose pattern of expression is confined to neuronal cells. In order to investigate whether the two kinesin motors, which are encoded by different genes, may play distinct biological roles in neurons, we studied their expression during neuronal differentiation.
View Article and Find Full Text PDFKinesin is a microtubule-based motor protein involved in organelle transport in neuronal and nonneuronal cells. Although a single kinesin motor has been thought to serve all cell types, we document here that neurons express a second conventional kinesin heavy chain (nKHC) that is 65% identical in amino acid sequence to the ubiquitously expressed kinesin heavy chain (uKHC). By preparing antibodies which distinguish between the two KHCs, we demonstrate that nKHC is a nucleotide-dependent microtubule-binding protein which partially cofractionates with membrane organelles.
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