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“Characterization of chicken natural resistance-associated macrophage protein encoding genes (Nramp1 and Nramp2) and association with salmonellosis resistance”, vol. 12, pp. 618-630, 2013.
, Ates O, Dalyan L, Musellim B, Hatemi G, et al. (2009). NRAMP1 (SLC11A1) gene polymorphisms that correlate with autoimmune versus infectious disease susceptibility in tuberculosis and rheumatoid arthritis. Int. J. Immunogenet. 36: 15-19.
http://dx.doi.org/10.1111/j.1744-313X.2008.00814.x
PMid:19055603
Baker ST, Barton CH and Biggs TE (2000). A negative autoregulatory link between Nramp1 function and expression. J. Leukoc. Biol. 67: 501-507.
PMid:10770282
Barshes NR, Lee TR, Goss JA, Goodpastor SE, et al. (2006). Slc11a1 (formerly Nramp1) polymorphisms and susceptibility to post-transplant lymphoproliferative disease following pediatric liver transplantation. Transpl. Infect. Dis. 8: 108-112.
http://dx.doi.org/10.1111/j.1399-3062.2006.00139.x
PMid:16734634
Blackwell JM and Searle S (1999). Genetic regulation of macrophage activation: understanding the function of Nramp1 (=Ity/Lsh/Bcg). Immunol. Lett. 65: 73-80.
http://dx.doi.org/10.1016/S0165-2478(98)00127-8
Blackwell JM, Searle S, Goswami T and Miller EN (2000). Understanding the multiple functions of Nramp1. Microbes. Infect. 2: 317-321.
http://dx.doi.org/10.1016/S1286-4579(00)00295-1
Blackwell JM, Searle S, Mohamed H and White JK (2003). Divalent cation transport and susceptibility to infectious and autoimmune disease: continuation of the Ity/Lsh/Bcg/Nramp1/Slc11a1 gene story. Immunol. Lett. 85: 197-203.
http://dx.doi.org/10.1016/S0165-2478(02)00231-6
Blasco H, Vourc'h P, Nadjar Y, Ribourtout B, et al. (2011). Association between divalent metal transport 1 encoding gene (SLC11A2) and disease duration in amyotrophic lateral sclerosis. J. Neurol. Sci. 303: 124-127.
http://dx.doi.org/10.1016/j.jns.2010.12.018
PMid:21276595
Boyer E, Bergevin I, Malo D, Gros P, et al. (2002). Acquisition of Mn(II) in addition to Fe(II) is required for full virulence of Salmonella enterica serovar Typhimurium. Infect. Immun. 70: 6032-6042.
http://dx.doi.org/10.1128/IAI.70.11.6032-6042.2002
PMid:12379679 PMCid:130432
Canonne-Hergaux F, Gruenheid S, Ponka P and Gros P (1999). Cellular and subcellular localization of the Nramp2 iron transporter in the intestinal brush border and regulation by dietary iron. Blood 93: 4406-4417.
PMid:10361139
Canonne-Hergaux F, Calafat J, Richer E, Cellier M, et al. (2002). Expression and subcellular localization of NRAMP1 in human neutrophil granules. Blood 100: 268-275.
http://dx.doi.org/10.1182/blood.V100.1.268
PMid:12070036
Cellier MF, Courville P and Campion C (2007). Nramp1 phagocyte intracellular metal withdrawal defense. Microbes. Infect. 9: 1662-1670.
http://dx.doi.org/10.1016/j.micinf.2007.09.006
PMid:18024118
Cohen A, Nevo Y and Nelson N (2003). The first external loop of the metal ion transporter DCT1 is involved in metal ion binding and specificity. Proc. Natl. Acad. Sci. U. S. A. 100: 10694-10699.
http://dx.doi.org/10.1073/pnas.1934572100
PMid:12954986 PMCid:196866
Courville P, Chaloupka R and Cellier MF (2006). Recent progress in structure-function analyses of Nramp proton-dependent metal-ion transporters. Biochem. Cell Biol. 84: 960-978.
http://dx.doi.org/10.1139/o06-193
PMid:17215883
Ganguly I, Sharma A, Singh R, Deb SM, et al. (2008). Association of microsatellite (GT)n polymorphism at 3'UTR of NRAMP1 with the macrophage function following challenge with Brucella LPS in buffalo (Bubalus bubalis). Vet. Microbiol. 129: 188-196.
http://dx.doi.org/10.1016/j.vetmic.2007.10.033
PMid:18078724
Gazouli M, Atsaves V, Mantzaris G, Economou M, et al. (2008). Role of functional polymorphisms of NRAMP1 gene for the development of Crohn's disease. Inflamm. Bowel. Dis. 14: 1323-1330.
http://dx.doi.org/10.1002/ibd.20488
PMid:18454481
Gruenheid S, Cellier M, Vidal S and Gros P (1995). Identification and characterization of a second mouse Nramp gene. Genomics 25: 514-525.
http://dx.doi.org/10.1016/0888-7543(95)80053-O
Gruenheid S, Canonne-Hergaux F, Gauthier S, Hackam DJ, et al. (1999). The iron transport protein NRAMP2 is an integral membrane glycoprotein that colocalizes with transferrin in recycling endosomes. J. Exp. Med. 189: 831-841.
http://dx.doi.org/10.1084/jem.189.5.831
PMid:10049947 PMCid:2192949
Gunshin H, Mackenzie B, Berger UV, Gunshin Y, et al. (1997). Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature 388: 482-488.
http://dx.doi.org/10.1038/41343
PMid:9242408
Hu J, Bumstead N, Skamene E, Gros P, et al. (1996). Structural organization, sequence, and expression of the chicken NRAMP1 gene encoding the natural resistance-associated macrophage protein 1. DNA Cell Biol. 15: 113-123.
http://dx.doi.org/10.1089/dna.1996.15.113
PMid:8634139
Hu J, Bumstead N, Barrow P, Sebastiani G, et al. (1997). Resistance to salmonellosis in the chicken is linked to NRAMP1 and TNC. Genome Res. 7: 693-704.
PMid:9253598
Jabado N, Jankowski A, Dougaparsad S, Picard V, et al. (2000). Natural resistance to intracellular infections: natural resistance-associated macrophage protein 1 (Nramp1) functions as a pH-dependent manganese transporter at the phagosomal membrane. J. Exp. Med. 192: 1237-1248.
http://dx.doi.org/10.1084/jem.192.9.1237
PMid:11067873 PMCid:2193348
Jabado N, Cuellar-Mata P, Grinstein S and Gros P (2003). Iron chelators modulate the fusogenic properties of Salmonella-containing phagosomes. Proc. Natl. Acad. Sci. U. S. A. 100: 6127-6132.
http://dx.doi.org/10.1073/pnas.0937287100
PMid:12711734 PMCid:156337
Kishi F, Yoshida T and Aiso S (1996). Location of NRAMP1 molecule on the plasma membrane and its association with microtubules. Mol. Immunol. 33: 1241-1246.
http://dx.doi.org/10.1016/S0161-5890(96)00088-0
Lam-Yuk-Tseung S, Govoni G, Forbes J and Gros P (2003). Iron transport by Nramp2/DMT1: pH regulation of transport by 2 histidines in transmembrane domain 6. Blood 101: 3699-3707.
http://dx.doi.org/10.1182/blood-2002-07-2108
PMid:12522007
Lam-Yuk-Tseung S, Camaschella C, Iolascon A and Gros P (2006). A novel R416C mutation in human DMT1 (SLC11A2) displays pleiotropic effects on function and causes microcytic anemia and hepatic iron overload. Blood Cells Mol. Dis. 36: 347-354.
http://dx.doi.org/10.1016/j.bcmd.2006.01.011
PMid:16584902
Leung KH, Yip SP, Wong WS, Yiu LS, et al. (2007). Sex- and age-dependent association of SLC11A1 polymorphisms with tuberculosis in Chinese: a case control study. BMC Infect. Dis. 7: 19.
http://dx.doi.org/10.1186/1471-2334-7-19
PMid:17371589 PMCid:1847518
Liu W, Kaiser MG and Lamont SJ (2003). Natural resistance-associated macrophage protein 1 gene polymorphisms and response to vaccine against or challenge with Salmonella enteritidis in young chicks. Poult. Sci. 82: 259-266.
PMid:12619803
Mackenzie B and Hediger MA (2004). SLC11 family of H+-coupled metal-ion transporters NRAMP1 and DMT1. Pflugers Arch. 447: 571-579.
http://dx.doi.org/10.1007/s00424-003-1141-9
PMid:14530973
Mackenzie B, Ujwal ML, Chang MH, Romero MF, et al. (2006). Divalent metal-ion transporter DMT1 mediates both H+ -coupled Fe2+ transport and uncoupled fluxes. Pflugers Arch. 451: 544-558.
http://dx.doi.org/10.1007/s00424-005-1494-3
PMid:16091957
Peracino B, Wagner C, Balest A, Balbo A, et al. (2006). Function and mechanism of action of Dictyostelium Nramp1 (Slc11a1) in bacterial infection. Traffic 7: 22-38.
http://dx.doi.org/10.1111/j.1600-0854.2005.00356.x
PMid:16445684
Rose PP, Hanna SL, Spiridigliozzi A, Wannissorn N, et al. (2011). Natural resistance-associated macrophage protein is a cellular receptor for sindbis virus in both insect and mammalian hosts. Cell Host Microbe 10: 97-104.
http://dx.doi.org/10.1016/j.chom.2011.06.009
PMid:21843867 PMCid:3164510
Stiles KM and Kielian M (2011). Alphavirus entry: NRAMP leads the way. Cell Host Microbe 10: 92-93.
http://dx.doi.org/10.1016/j.chom.2011.07.008
PMid:21843864 PMCid:3163168
Tandy S, Williams M, Leggett A, Lopez-Jimenez M, et al. (2000). Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells. J. Biol. Chem. 275: 1023-1029.
http://dx.doi.org/10.1074/jbc.275.2.1023
PMid:10625641
Touret N, Furuya W, Forbes J, Gros P, et al. (2003). Dynamic traffic through the recycling compartment couples the metal transporter Nramp2 (DMT1) with the transferrin receptor. J. Biol. Chem. 278: 25548-25557.
http://dx.doi.org/10.1074/jbc.M212374200
PMid:12724326
Trinder D, Macey DJ and Olynyk JK (2000). The new iron age. Int. J. Mol. Med. 6: 607-612.
PMid:11078817
“Promoter methylation negatively correlated with mRNA expression but not tissue differential expression after heat stress”, vol. 12, pp. 809-819, 2013.
, Bird A (2002). DNA methylation patterns and epigenetic memory. Genes Dev. 16: 6-21.
http://dx.doi.org/10.1101/gad.947102
PMid:11782440
Brena RM, Huang TH and Plass C (2006). Quantitative assessment of DNA methylation: Potential applications for disease diagnosis, classification, and prognosis in clinical settings. J. Mol. Med. 84: 365-377.
http://dx.doi.org/10.1007/s00109-005-0034-0
PMid:16416310
Dai Z, Zhu WG, Morrison CD, Brena RM, et al. (2003). A comprehensive search for DNA amplification in lung cancer identifies inhibitors of apoptosis cIAP1 and cIAP2 as candidate oncogenes. Hum. Mol. Genet. 12: 791-801.
http://dx.doi.org/10.1093/hmg/ddg083
PMid:12651874
Dionello NJL, Ferro JA, Macari M, Rutz F, et al. (2001). Effect of acute heat stress on hepatic and cerebral messenger RNA heat shock protein 70 and heat shock protein 70 level of broiler chicks from 2 to 5 days old of different strains. Rev. Bras. Zootec. 5: 1506-1513.
http://dx.doi.org/10.1590/S1516-35982001000600018
Ehrich M, Nelson MR, Stanssens P, Zabeau M, et al. (2005). Quantitative high-throughput analysis of DNA methylation patterns by base-specific cleavage and mass spectrometry. Proc. Natl. Acad. Sci. U. S. A. 102: 15785-15790.
http://dx.doi.org/10.1073/pnas.0507816102
PMid:16243968 PMCid:1276092
Esteller M (2007). Epigenetic gene silencing in cancer: the DNA hypermethylome. Hum. Mol. Genet. 16 Spec No 1: R50-R59.
http://dx.doi.org/10.1093/hmg/ddm018
PMid:17613547
Esteller M (2008). Epigenetics in evolution and disease. Lancet 372: S90-S96.
http://dx.doi.org/10.1016/S0140-6736(08)61887-5
Gabriel JE, Ferro JA, Stefani RM, Ferro MI, et al. (1996). Effect of acute heat stress on heat shock protein 70 messenger RNA and on heat shock protein expression in the liver of broilers. Br. Poult. Sci. 37: 443-449.
http://dx.doi.org/10.1080/00071669608417875
PMid:8773853
Givisiez PEN, Furlan RL, Malheiros EB and Macari M (2003). Incubation and rearing temperature effects on Hsp70 levels and heat stress response in broilers. Can. J. Anim. Sci. 2: 213-220.
http://dx.doi.org/10.4141/A02-038
Guerreiro EN, Giachetto PF, Givisiez PEN, Ferro JA, et al. (2004). Brain and hepatic Hsp70 protein levels in heat-acclimated broiler chickens during heat stress. Braz. J. Poult. Sci. 6: 201-206.
http://dx.doi.org/10.1590/S1516-635X2004000400002
Hartl FU (1996). Molecular chaperones in cellular protein folding. Nature 381: 571-579.
http://dx.doi.org/10.1038/381571a0
PMid:8637592
Kregel KC (2002). Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance. J. Appl. Physiol. 92: 2177-2186.
PMid:11960972
Kuroda A, Rauch TA, Todorov I, Ku HT, et al. (2009). Insulin gene expression is regulated by DNA methylation. PLoS One 4: e6953.
http://dx.doi.org/10.1371/journal.pone.0006953
PMid:19742322 PMCid:2735004
Lopez-Serra L and Esteller M (2008). Proteins that bind methylated DNA and human cancer: reading the wrong words. Br. J. Cancer 98: 1881-1885.
http://dx.doi.org/10.1038/sj.bjc.6604374
PMid:18542062 PMCid:2441952
Maak S, Melesse A, Schmidt R, Schneider F, et al. (2003). Effect of long-term heat exposure on peripheral concentrations of heat shock protein 70 (Hsp70) and hormones in laying hens with different genotypes. Br. Poult. Sci. 44: 133-138.
http://dx.doi.org/10.1080/0007166031000085319
PMid:12737235
Mahmoud KZ (2000). Genetic and Environmental Variations of Chicken Heat Shock Proteins. PhD thesis, North Carolina State University, North Carolina.
Mayer MP and Bukau B (2005). Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol. Life Sci. 62: 670-684.
http://dx.doi.org/10.1007/s00018-004-4464-6
PMid:15770419 PMCid:2773841
Mazzi CM, Ferro MIT, Coelho AAD, Savino VJM, et al. (2002). Effect of heat exposure on the thermoregulatory responses of selected naked neck chickens. Arq. Bras. Med. Vet. Zootec. 54: 35-41.
http://dx.doi.org/10.1590/S0102-09352002000100006
Mazzi CM, Ferro JA, Ferro MIT, Savino VJM, et al. (2003). Polymorphism analysis of the hsp70 stress gene in Broiler chickens (Gallus gallus) of different breeds. Genet. Mol. Biol. 3: 275-281.
Robertson KD and Wolffe AP (2000). DNA methylation in health and disease. Nat. Rev. Genet. 1: 11-19.
http://dx.doi.org/10.1038/35049533
PMid:11262868
Safe S and Abdelrahim M (2005). Sp transcription factor family and its role in cancer. Eur. J. Cancer 41: 2438-2448.
http://dx.doi.org/10.1016/j.ejca.2005.08.006
PMid:16209919
Samson SL and Wong NC (2002). Role of Sp1 in insulin regulation of gene expression. J. Mol. Endocrinol. 29: 265-279.
http://dx.doi.org/10.1677/jme.0.0290265
PMid:12459029
Song F, Smith JF, Kimura MT, Morrow AD, et al. (2005). Association of tissue-specific differentially methylated regions (TDMs) with differential gene expression. Proc. Natl. Acad. Sci. U. S. A. 102: 3336-3341.
http://dx.doi.org/10.1073/pnas.0408436102
PMid:15728362 PMCid:552919
Straussman R, Nejman D, Roberts D, Steinfeld I, et al. (2009). Developmental programming of CpG island methylation profiles in the human genome. Nat. Struct. Mol. Biol. 16: 564-571.
http://dx.doi.org/10.1038/nsmb.1594
PMid:19377480
Strichman-Almashanu LZ, Lee RS, Onyango PO, Perlman E, et al. (2002). A genome-wide screen for normally methylated human CpG islands that can identify novel imprinted genes. Genome Res. 12: 543-554.
PMid:11932239 PMCid:187522
Ushijima T and Asada K (2010). Aberrant DNA methylation in contrast with mutations. Cancer Sci. 101: 300-305.
http://dx.doi.org/10.1111/j.1349-7006.2009.01434.x
PMid:19958364
Wang S and Edens FW (1998). Heat conditioning induces heat shock proteins in broiler chickens and turkey poults. Poult. Sci. 77: 1636-1645.
PMid:9835337
Watanabe Y and Maekawa M (2010). Methylation of DNA in cancer. Adv. Clin. Chem. 52: 145-167.
http://dx.doi.org/10.1016/S0065-2423(10)52006-7
Xing JY, Kang L, Hu Y, Jiang YL, et al. (2011). Effect of dietary betaine supplementation on mRNA expression and promoter CpG methylation of lipoprotein lipase gene in laying hens. J. Poult. Sci. 3: 224-228.
Xu Q, Zhang Y, Sun D, Wang Y, et al. (2007). Analysis on DNA methylation of various tissues in chicken. Anim. Biotechnol. 18: 231-241.
http://dx.doi.org/10.1080/10495390701574838
PMid:17934897
Yossifoff M, Kisliouk T and Meiri N (2008). Dynamic changes in DNA methylation during thermal control establishment affect CREB binding to the brain-derived neurotrophic factor promoter. Eur. J. Neurosci. 28: 2267-2277.
http://dx.doi.org/10.1111/j.1460-9568.2008.06532.x
PMid:19046370
Zaid A, Li R, Luciakova K, Barath P, et al. (1999). On the role of the general transcription factor Sp1 in the activation and repression of diverse mammalian oxidative phosphorylation genes. J. Bioenerg. Biomembr. 31: 129-135.
http://dx.doi.org/10.1023/A:1005499727732
PMid:10449239
Zhang X, Du H and Li J (2002). Single Nucleotide Polymorphism of Chicken Heat Shock Protein 70 Gene. 7th World Congress on Genetics Applied to Livestock Production, Montpellier.
Zhen FS, Du HL, Xu HP, Luo QB, et al. (2006). Tissue and allelic-specific expression of hsp70 gene in chickens: basal and heat-stress-induced mRNA level quantified with real-time reverse transcriptase polymerase chain reaction. Br. Poult. Sci. 47: 449-455.
http://dx.doi.org/10.1080/00071660600827690
PMid:16905471