Translationally controlled tumor protein

Bhisutthibhan, J., Pan, X.-O., Hossler, P.A., Walker, D.J., Yowell, C.A., Carlton, J., Dame, J.B., and Meshnick, S.R. The plasmodium falciparum translationally controlled tumor protein homolog and its reaction with the antimalarial drug artemisinin,. Biol. Chem., 273,16192,1998. 

Bhisutthibhan, J., Pan, X.-O., Hossler, P.A., Walker, D.J., Yowell, C.A., Carlton, J., Dame, J.B., and Meshnick, S.R. The plasmodium falciparum translationally controlled tumor protein homolog and its reaction with the antimalarial drug artemisinin, /. Biol. Chem., 273,16192,1998. 21. Avery, M.A., Chong, W.K.M., and Jennings-White, C. Stereoselective total synthesis of (+)-artemisinin, the antimalarial constituent of Artemisia annua L., /. Am. Chem. Soc., 114,974,1992. Avery, M.A., Bonk, J.D., and Bupp, J. Radiolabeled antimalarials synthesis of 14C-artemisinin, /. Labelled Comp. Radiopharm., 38, 263, 1996. 

Gnanasekar M, K Ramaswamy. Translationally controlled tumor protein of Brugia malayi fimetions as an antioxidant protein. Parasitol Res 2007 101 1533-1540. 

Gnanasekar M, Rao KVN, Chen L et al. Molecular characterization of a calcium bindii translationally controlled tumor protein homologue fi ora the filarial parasites Brugia malayi and Wuchereria bancrofii. Mol Biochem Parasitol 2002 121 107-118. 

One of the most heavily labeled proteins was later isolated from parasite grown in the presence of [ Hjdihydroartemismin (300 mM) and identified as a 25-kDa translationally controlled tumor protein (TCTP) homolog, that is able to bind heme with modest affinity (17). In vitro, the reaction of dihydroartemisinin with recombinant TCTP is clearly dependent on the presence of heme the single cysteine of the protein also appears to be necessary for the reaction, probably serving as a source of electrons for the heme-mediated activation of e drug. 

Mevinolin and compatin, independently discovered by Merck and Sankyo, both control cholesterol synthesis in humans. The Merck group screened directly for inhibition of HMG-CoA reductase, a key enzyme involved in cholesterol synthesis, while the Sankyo group sought agents that would interfere the incorporation of radiolabelled acetate into cholesterol in a cell-free enzyme system. The search for microbial products that interfere with cholesterol metabolism continues, given the importance of serum cholesterol in coronary heart disease. Compatin and mevinolin, being HMG-CoA reductase inhibitors, also prevent maturation (a post-translational modification near the carboxy terminal) of ras proteins. They thus may be of value in the treatment of ras-dependent tumors. 

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