title: Characterization of Trypanosoma cruzi telomerase.
abstract: High telomerase activity is always associated with actively dividing cells, however the detection of this activity in dividing Leishmania and Trypanosoma cruzi cells has always been disappointingly low. Recently, we have found that Leishmania major telomerase activity can be activated by heat, which combined with dilutions of the nuclear extracts produced an increase in activity comparable to cancer cells. Here we examined whether T. cruzi telomerase shares the same physicochemical properties of primer specificity and overall features of the L. major. Our studies revealed that no telomerase inhibitory factors were present in the nuclear lysates of T. cruzi however the enzyme was activated by heat and was very resilient to heat denaturation. We also showed the extension primer specificity, susceptibility to RNase-A and RNase-H digestion, and the effect of telomerase inhibitors.
authors: Instituto de Estudios Avanzados, MppCiencia, Tecnología e Industrias Ligeras, Caracas, Venezuela.
authors: Riward
authors: R
authors: Campelo
authors: Maria Mercedes
authors: MM
authors: Galindo
authors: Jose Luis
authors: JL
authors: Ramirez
mesh_terms: D004791:Enzyme Inhibitors / Q000378:metabolism; D004795:Enzyme Stability; D006358:Hot Temperature; D011489:Protein Denaturation / Q000528:radiation effects; D055550:Protein Stability; D016914:Ribonuclease H / Q000378:metabolism; D012259:Ribonuclease, Pancreatic / Q000378:metabolism; D013379:Substrate Specificity; D019098:Telomerase / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D014349:Trypanosoma cruzi / Q000201:enzymology*
chemical_list: D004791:Enzyme Inhibitors; D019098:Telomerase; D016914:Ribonuclease H; D012259:Ribonuclease, Pancreatic