A novel target of lithium therapy.
作者： Lynne Yenush , José M Bellés , José M López-Coronado , Rosario Gil-Mascarell , Ramón Serrano
DOI: 10.1016/S0014-5793(00)01183-2
关键词:
摘要: Phosphatases converting 3′-phosphoadenosine 5′-phosphate (PAP) into adenosine are of fundamental importance in living cells as the accumulation PAP is toxic to several cellular systems. These enzymes lithium-sensitive and we have characterized a human phosphatase potential target lithium therapy. A cDNA encoding enzyme was identified by data base screening, expressed Escherichia coli 33 kDa protein purified homogeneity. The exhibits high affinity for (Km<1 μM) sensitive subtherapeutic concentrations (IC50=0.3 mM). also hydrolyzes inositol-1,4-bisphosphate with (Km=0.4 μM), therefore it can be considered dual specificity (μM range) both inositol-1,4-bisphosphate. Hydrolysis inhibited (IC50=0.6 Thus, present experimental evidence novel therapy, which could explain some side effects this
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