Loading...
  • divalent metal
  • Phagosomes from Nramp1(+/+) mice extrude Mn(2+) faster than their Nramp(-/-) counterparts.The difference in the rate of transport is eliminated when acidification of the phagosomal lumen is dissipated, suggesting that divalent metal transport through Nramp1 is H(+) dependent.Such cations are likely essential for microbial function and their removal from the phagosomal microenvironment impairs pathogenesis, resulting in enhanced bacteriostasis or bactericidal activity. (nih.gov)
  • The difference in the rate of transport is eliminated when acidification of the phagosomal lumen is dissipated, suggesting that divalent metal transport through Nramp1 is H(+) dependent. (nih.gov)
  • The broad specificity NRAMP2 (DMT1), which transports a range of divalent metal cations, transports Fe2+ and H+ with a 1:1 stoichiometry and apparent affinities of 6 μm and about 1 μm, respectively. (wikipedia.org)
  • OCT1
  • Amodiaquine, proguanil, pyrimethamine and quinine were the most potent inhibitors of 4-(4-(dimethylamino)styryl)- N -methylpyridinium iodide (ASP) transport, a known substrate of OCT1/2, resulting in half maximal inhibitory concentrations (IC 50 ) of 11, 13, 1.6, and 3.4 µM, respectively. (biomedcentral.com)
  • Macrophages
  • Nramp1 codes for an integral membrane protein expressed in the lysosomal compartment of macrophages, and is recruited to the membrane of phagosomes soon after the completion of phagocytosis. (nih.gov)
  • Quenching of the probe by Mn(2+) was used to monitor the flux of divalent cations across the phagosomal membrane in peritoneal macrophages obtained from Nramp1-expressing (+/+) and Nramp1-deficient (-/-) macrophages. (nih.gov)
  • The intracellular localization of the Nramp1 protein was analyzed in control 129/sv and mutant Nramp1-/- macrophages by immunofluorescence and confocal microscopy and by biochemical fractionation. (nih.gov)
  • In colocalization studies with a specific anti-Nramp1 antiserum and a panel of control antibodies directed against known cellular structures, Nramp1 was found not to be expressed at the plasma membrane but rather localized to the late endocytic compartments (late endosome/lysosome) of resting macrophages in a Lamp1 (lysosomal-associated membrane protein 1)-positive compartment. (nih.gov)
  • Subcellular localization of the Nramp1 protein in macrophages. (nih.gov)
  • GST-35C was used to localize the Nramp1 protein in macrophages by indirect immunofluorescence (Fig. 1). (nih.gov)
  • Molecular
  • Two APC family members, LAT1 and LAT2 (TC #2.A.3.8.7), transport a neurotoxicant, the methylmercury-L-cysteine complex, by molecular mimicry. (wikipedia.org)
  • Isoforms
  • Distribution of the two isoforms of DMT1 proteins and HIF-1α in HepG2 cells under normoxia and hypoxia. (nih.gov)
  • Our data showed that hypoxia could significantly affect the expression of the two isoforms of DMT1 proteins. (nih.gov)
  • The latter three proteins are likely to be closely related thiamin permease isoforms. (wikipedia.org)
  • Calcium
  • Since it transports Ca2+ into the extracellular space, the PMCA is also an important regulator of the calcium concentration in the extracellular space. (wikipedia.org)
  • Yeast
  • The ctpA ctpa (Catalog # MBS1229137 ) is a Recombinant Protein produced from E Coli or Yeast or Baculovirus or Mammalian Cell and is intended for research purposes only. (mybiosource.com)
  • The yeast proteins may be localized to the vacuole and/or the plasma membrane of the yeast cell. (wikipedia.org)
  • A third yeast protein, Smf3p, appears to be exclusively intracellular, possibly in the Golgi. (wikipedia.org)
  • The bacterial and yeast proteins are widely divergent and do not cluster closely on the NCS1 family phylogenetic tree. (wikipedia.org)
  • Two of the yeast proteins (Dal4 (TC# 2.A.39.3.1) and Fur4 (TC# 2.A.39.3.2)) cluster tightly together. (wikipedia.org)
  • natural resistance-associated
  • Natural resistance to intracellular infections: natural resistance-associated macrophage protein 1 (Nramp1) functions as a pH-dependent manganese transporter at the phagosomal membrane. (nih.gov)
  • Mutations at the natural resistance-associated macrophage protein 1 (Nramp1) locus cause susceptibility to infection with antigenically unrelated intracellular pathogens. (nih.gov)
  • The Nramp1 (natural-resistance-associated macrophage protein 1) locus (Bcg, Ity, Lsh) controls the innate resistance or susceptibility of mice to infection with a group of unrelated intracellular parasites which includes Salmonella, Leishmania, and Mycobacterium. (nih.gov)
  • Natural Resistance-Associated Macrophage Proteins (NRAMPs) are members of the Metal Ion (Mn2+-iron) Transporter (NRAMP) Family (TC# 2.A.55). (wikipedia.org)
  • Homologues of this family are found in various yeasts, plants, animals, archaea, and Gram-negative and Gram-positive bacteria termed "natural resistance-associated" macrophage proteins because one of the animal homologues plays a role in resistance to intracellular bacterial pathogens such as Salmonella enterica serovar Typhimurium, Leishmania donovani and Mycobacterium bovis. (wikipedia.org)
  • substrate
  • However, bioinformatics utilizing combinations of homology modelling and mutation experiments have been used to explore the heterdimer nature of the system as well as the mechanisms of substrate recognition and transport. (wikipedia.org)
  • consists
  • The Nucleobase:Cation Symporter-1 (NCS1) Family (TC# 2.A.39) consists of over 1000 currently sequenced proteins derived from Gram-negative and Gram-positive bacteria, archaea, fungi and plants. (wikipedia.org)