XXXX phosphorylase: a two-face Janus in anticancer chemotherapy.

@entity5 @entity2353 @entity1014 @entity1015
Several cytokines and growth factors modulate angiogenesis through a fine tuned paracrine or autocrine mode of action. Among them is plateled-derived endothelial cell growth factor ( @entity1015 ), which is highly is expressed in @entity5 , and is angiogenic by stimulation of endothelial cell migration. Studies have shown that @entity1015 is identical to the well known enzyme @entity1014 phosphorylase (TP), which is involved in @entity1014 metabolism and homeostasis. Interestingly, @entity1015 plays an angiogenic role as a result of its TP enzyme activity. In light of these findings, @entity1015 /TP should not be considered a true growth factor, and its @entity1015 name is now actually a misnomer. Recently, TP activity was thought of as an interesting potential two-face target for controling @entity5 -dependent angiogenesis. In fact, on one hand, its high levels of expression in @entity5 compared to non-neoplastic regions, and its broad substrate specificity suggested that TP could be used as an enzymatic tool to locally activate anticancer @entity2353 bases or base analogs. On the other hand, its enzyme-dependent angiogenic activity engendered the search for specific inhibitors to reduce TP-dependent angiogenesis. This review will describe TP, its activity, its possible mechanisms of action and its role in angiogenesis. Particular attention will be focused on the design and biological characterization of novel TP inhibitors which recently showed promising anticancer activity.
