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Review
. 2001 Dec;3(12):773-84.
doi: 10.1046/j.1462-5822.2001.00150.x.

SLC11A1 (formerly NRAMP1) and disease resistance

J M Blackwell  1 , T Goswami, C A Evans, D Sibthorpe, N Papo, J K White, S Searle, E N Miller, C S Peacock, H Mohammed, M Ibrahim
Affiliations
Review

SLC11A1 (formerly NRAMP1) and disease resistance

J M Blackwell et al. Cell Microbiol. 2001 Dec.
No abstract available

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Figures

Fig. 1
Fig. 1
Bone marrow-derived mformula image from Slc11a1 wild-type (A and B) versus mutant (C and D) congenic mice infected with M. avium. A and C. Staining of mformula image nuclei and bacterial DNA with propidium iodide. B and D. The same images merged with the green fluorescence channel showing anti-C-terminal anti-Slc11a1 staining. For wild-type mformula image (B), Slc11a1-positive vesicles have migrated to fuse with mycobacterial phagosomes. For mutant mformula image (D), no co-localization is observed. Reproduced with permission from Searle et al. (1998).
Fig. 2
Fig. 2
Model of divalent cation homeostasis in mformula image and its relationship to oxygen-and nitrogen-dependent antimicrobial pathways. The symport activity of Slc11a2 delivers divalent cations (e.g. Fe2+) to the cytosol across early endosomal membranes after recruitment of V-ATPase and acidification of the vacuole. The antiport activity of Slc11a1 delivers divalent cations from the cytosol to acidic late endosomes and lysosomes, where the Fenton reaction generates toxic antimicrobial radicals. Hydroxyl radicals (OH•) generated from the Fenton reaction may then react with nitric oxide (NO) to produce toxic peroxynitrate.
Fig. 3
Fig. 3
Slc11a1 as viewed from the cytosol or the vesicle assuming a topology in which N-and C-termini are cytosolic. This diagrammatic representation shows the locations of: conserved and Slc11a1-specific Cys (C), His (H) and Met (M) residues; N-and C-terminal YXXZ putative endosomal targeting motifs (where X = any amino acid, Z = bulky, hydrophobic residue); the Pro–Ser-rich N-terminus; PKC binding sites; and the position of the murine transmembrane domain 4 functional null mutation.
See this image and copyright information in PMC

References

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