Within the connective tissue elements of the lamina propria, NTPD1 may be found in blood vessels while NTPD2 occurs in a specific subset of cells which may be ICC. Further work will be necessary to confirm if this is true. These cells lie proximal to the smooth muscle and surround muscle bundles, but are not in the smooth muscle itself. NTPD1 and NT5E however, are richly expressed within the smooth muscle suggesting a functionally important relationship. This expression and localization study provides important novel information about the signature of nucleotidases in mammalian bladder. Knowledge of their SB 611812 tissue-specific distribution will allow the design of rational functional studies to test the contribution of each to normal micturition. For example the use of Cre-lox technology to generate conditional knockouts in specific cell types e.g. urothelium, can now be considered for these enzymes. Altered purinergic signaling occurs frequently in bladder disease and at present the involvement of ectonucleotidases in disease processes is completely unknown. This study sets the stage for further investigations of their role in both physiology and pathophysiology. Furthermore, these ectoenzymes may one day offer tempting therapeutic targets for conditions such as overactive bladder or painful bladder syndrome. In eukaryotes, transcription is finely regulated through complex mechanisms, which promote RNA polymerases recruitment and progression through a chromatin matrix leading to Raclopride efficient RNA synthesis. In vitro and in vivo studies indicate that Pol II movement is discontinuous and that nucleosomes provoke its pausing and backtracking during transcription at promoter-proximal regions and within the body of genes. After backtracking, arrested Pol II is reactivated by the elongation factor TFIIS that binds through its domain II and RSADE structural modules to the jaw and funnel domains of Pol II, thereby enhancing the enzyme��s intrinsic RNA cleavage activity. Escape from backtracking is essential for efficient transcript elongation and, in general, for cell viability. In addition, several studies revealed that TFIIS is associated with gene promoters and acts during preinitiation complex assembly. TFIIS has also been shown to participate in Pol III transcription. It is associated with the Pol III machinery at the majority of class III genes in yeast and mouse embryonic stem cells. Altogether, these findings indicate that TFIIS acts as a positive transcription factor stimulating both Pol II and Pol III transcription and, hence, is implicated in many physiological processes.