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While the human proteome has some 20 dynein proteins (<0.1%), we observed six of them within the 105 modified epithelial proteins (5.7%) in the specimens obtained from allergic subjects. A markedly decreased expression was seen in most of the dyneins together with the progression of the disease symptoms. Dyneins are microtubule-binding proteins known to execute cargo transport within the cells (30). Our previous work showed that the pollen allergen is taken up by the epithelial cells and tissue by a caveolar mechanism. This protein transport through the epithelium to the mast cells, situated usually under the basal lamina, requires controlled intracellular machinery. Caveolae are transported within the cells via the cytoskeleton. Microtubules serve as structural components of the cytoskeleton within cells and also part of the cilia and flagella (31). They are involved in several <a href="http://www.selleckchem.com/products/obeticholic-acid.html">Obeticholic Acid cellular processes including mitosis, cytokinesis and caveolar transport. Dyneins are motor proteins, which convert the chemical energy contained in adenosine triphosphate into the mechanical energy of movement. Dyneins transport cellular FARP1 cargo such as caveolae along the cytoskeleton by sliding one of its arms along the microtubule (32, 33). While the arms are used for ��walking�� the dyneins carry their cargo bound to the light chain (30). Among other cargos, dyneins can carry human immunodeficiency (HI) virus to the nuclei of infected cells (34). Thus, we can put out a hypothesis that dyneins could be consumed during the allergen transport in allergic subjects as this was not seen within the healthy subjects. Instead of concentrating our analysis on just one or a few altered genes or their corresponding proteins, we have tried to generate larger protein-protein interaction networks from our data. No single database alone can provide such a connected network. To understand the new systems levels of diseases we decided to build the integrated data warehouse, by which the information was integrated Doxorubicin in vitro from a number of databases. Thus, we can show that of the 124 proteins that were regulated in allergic patients during the pollen exposure, more than half were only connected to their own transcripts and genes based on the prior legacy knowledge. Of the 53 proteins that were connected to other proteins, a few were major hubs, i.e. proteins that have a large set of known interacting proteins. Proteins known to have many interacting proteins are ACTB, heat shock protein, HSPB8, and serine protease, ISK7. Among its other tasks, ACTB is involved together with dyneins in the organization of nuclear interchromosomal interactions (35). HSPB8 is a temperature-dependent chaperone.