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Leishmania mexicana amazonensis: plasma membrane adenine nucleotide translocator and chemotaxis
Authors:Detke S  Elsabrouty R
Affiliation:Department of Biochemistry and Molecular Biology, School of Medicine and Health Sciences, University of North Dakota, 501 N. Columbia Road, Grand Forks, ND 58203, USA. sdetke@medicine.nodak.edu
Abstract:Leishmania cannot synthesize purines de novo and rely on their host to furnish these compounds. To accomplish this, they possess multiple purine nucleoside and nucleobase transporters. Subcellular fractionation, immunohistochemical localization with anti-adenine nucleotide translocator (ANT) antibodies and surface biotinylation show that the mitochondrial ANT is also present in the plasma membrane of both promastigotes and amastigotes. Leishmania, however, do not appear to rely on this transporter to supplement their purine or energy requirements via preformed ATP from its host. Rather, Leishmania appear to use the plasma membrane ANT as part of a chemotaxis response. ATP is a chemorepellant for Leishmania and cells treated with atractyloside, an inhibitor of ANT, no longer exhibit negative chemotaxis for this compound.
Keywords:Leishmania   TOR   Mitochondria   Kinetoplast   Plasma membrane   Chemotaxis   Adenine nucleotide translocator   AKII, adenylate kinase II   ANT, adenine nucleotide translocator   CPT, carnitine palmitoyl transferase   GFP, green fluorescent protein   LPG, lipophosphoglycan   MPTP, mitochondrial permeability transition pore complex   YFP, yellow fluorescent protein
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