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Uridine triphosphate treatment induces Schwannoma cell migration through activation of P2Y2 receptors and through the increase of extracellular matrix metalloproteinase-2 (MMP-2) activation and expression. Uridine triphosphate-induced proliferation is mediated by protein kinase D, Src-family tyrosine kinase, Ca/calmodulin-dependent protein kinase II, phosphatidylinositol 3-kinase (PI3K), Akt, and phospholipase D. Uridine triphosphate increases phosphorylation of Akt through protein kinase C, Src-family tyrosine kinase, Ca/calmodulin-dependent protein kinase II, and PI3K.

Uridine triphosphate reduces mitochondrial calcium levels following hypoxia. Early or late uridine triphosphate preconditioning is effective to reduce infarct size and superior myocardial function. Uridine triphosphate treatment increases the number of monocytes and macrophages infiltrating the pouch and up-regulates the gene expression of IL-4 and IL-13 in the regional lymph nodes.