ATP-Diphosphohydrolases in Parasites: Localization, Functions and Recent Developments in Drug Discovery
Autor: | de Faria Pinto P, da Silva Filho Aa, Junqueira Lr, de Carvalho Lsa, Lorena Rodrigues Riani, Alves Jr Ij, Lívia Mara Silva |
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Rok vydání: | 2018 |
Předmět: |
Purine
Antiprotozoal Agents Biochemistry 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Immune system Adenosine Triphosphate Antigens CD Drug Discovery Animals Humans Parasites Platelet activation Enzyme Inhibitors Molecular Biology 030304 developmental biology chemistry.chemical_classification 0303 health sciences Chemistry Drug discovery Apyrase Cell Biology General Medicine Enzyme 030220 oncology & carcinogenesis Nucleoside Function (biology) |
Zdroj: | Current proteinpeptide science. 20(9) |
ISSN: | 1875-5550 |
Popis: | ATP-diphosphohydrolases (EC 3.6.1.5), also known as ATPDases, NTPases, NTPDases, EATPases or apyrases, are enzymes that hydrolyze a variety of nucleoside tri- and diphosphates to their respective nucleosides, being their activities dependent on the presence of divalent cations, such as calcium and magnesium. Recently, ATP-diphosphohydrolases were identified on the surface of several parasites, such as Trypanosoma sp, Leishmania sp and Schistosoma sp. In parasites, the activity of ATPdiphosphohydrolases has been associated with the purine recuperation and/or as a protective mechanism against the host organism under conditions that involve ATP or ADP, such as immune responses and platelet activation. These proteins have been suggested as possible targets for the development of new antiparasitic drugs. In this review, we will comprehensively address the main aspects of the location and function of ATP-diphosphohydrolase in parasites. Also, we performed a detailed research in scientific database of recent developments in new natural and synthetic inhibitors of the ATPdiphosphohydrolases in parasites. |
Databáze: | OpenAIRE |
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