HGT is an important force modulating bacterial evolution and depends on the number of transferred genes and their maintenance in the host cells by means of positive selection. In this way, genes coding for new proteins with novel properties are preserved while nonbeneficial genes tend to be removed. Also, it depends on the extent of the phenomenon, in both evolutionary

time and phylogenetic distance between the organisms involved (Boto, 2010). Although HGT is a widespread phenomenon among bacteria, there are few reports on gene transfer in extreme cold environments probably due to our lack of knowledge and understanding of polar microbial diversity. There are a few reports concerning gene transfer from bacteria to arthropods (Song Adriamycin manufacturer et al., 2010), crustacea (Kiko, 2010), or prokaryotes. Table 1 summarizes PS-341 chemical structure examples of HGT in Antarctic prokaryotes. The transfer of genes associated with antibacterial metabolites such as the biosynthesis

of violacein (Hakvåg et al., 2009), hydrocarbon biodegradation (Ma et al., 2006; Pini et al., 2007), signal transduction (López-García et al., 2004; Allen et al., 2009), vitamin metabolism (López-García et al., 2004; Moreira et al., 2006), central metabolism (López-García et al., 2004; Allen et al., 2009), and hydrolytic enzyme production (Xiao et al., 2005) illustrates the crucial role of HGT in the evolution and the adaptation of bacterial communities in a changing environment. In the oligotrophic Antarctic environment, the production of the hydrolytic enzyme chitinase, which breaks

down glycosidic bonds, might confer a fitness improvement to a microbe that can now use the chitin found in the outer skeleton of invertebrates as a C- and N-source. Another recalcitrant substrate available for microorganisms in Antarctica is fossil fuels. It is used for human activities and has led to hydrocarbon contamination, a serious environmental problem because of their persistence and high toxicity SPTLC1 in biological systems. Studies carried out by Flocco et al. (2009) showed a relative abundance of ndo genes in polluted soils from anthropogenic sources compared to noncontaminated sites. In those sites, the transfer of genes related to hydrocarbon degradation clearly has an impact on the bacterial fitness. It is very likely that the acquisition of genes related to antibiotics, biodegradation of carbon and nitrogen supplies, or contaminants, plays a key role in such environmental conditions. Usually, among prokaryotes, HGT is facilitated by a number of genetic elements, including plasmids, transposons, and integrons, and most attention has been focused on the first two. However, considering that nonindigenous microorganisms are not likely to be metabolically active, natural transformation might be the predominant form of HGT in Antarctic soils (Cowan et al., 2011).

There was no associated

history of fevers, diaphoresis, cough, or dyspnea. His symptoms were refractory to antacids (Mylanta, Johnson & Johnson Pty Ltd) and www.selleckchem.com/products/bmn-673.html pantoprazole (Somac, Nycomed). He immigrated to Australia 8 months prior, had no previous medical or family history or allergies, and physical examination was unremarkable. Laboratory results revealed microcytic hypochromic anemia (hemoglobin concentration 112 g/L, normal 130–180 g/L; mean cell volume 74 fL, normal 80–100 fL; and mean cell hemoglobin 24 pg, normal, 27–32 pg), thrombocytosis (platelet concentration 521 × 109 L−1, normal 150–450 × 109 L−1), raised erythrocyte sedimentation rate (76 mm/h, normal 1–10 mm/h), and C-reactive protein (56 mg/L, normal <5 mg/L) suggesting an inflammatory process (albeit a normal white cell count and differential), normal renal function and electrolytes, an isolated raised alkaline phosphatase (205 U/L, normal 35–110 U/L) on liver function

panel, and a positive quantiferon gold [tuberculosis (TB) antigen 1.50 IU/mL, normal <0.35 IU/mL and mitogen 5.44 IU/mL, normal >0.50 IU/mL]. Subsequent amebic and schistosoma serology were negative. Contrast enhanced chest, abdominal, and pelvic computed tomography (CT) revealed a calcified granuloma within www.selleckchem.com/products/VX-809.html the left lower lung lobe with left hilar and subcarinal foci of calcification, marked right colonic wall thickening with surrounding inflammation (Figure 1), prominent regional lymphadenopathy with one showing nodal calcification, and terminal ileal thickening. Gastroscopy revealed a 5 cm area of mucosal inflammation in the posterior wall of the antrum and prepyloric region with a cobble stone

appearance, small ulcerations, and scant mucopurulent exudates. Similar changes were noted in the pyloric channel and proximal duodenum. Multiple antral and pyloric biopsies were obtained. Colonoscopy revealed a Clomifene cobblestone mucosa in the ascending colon that was associated with inflammation, mucopurulent exudate, and multiple large ulcers. The cecum revealed similar inflammatory and ulcerative changes, and a fistulous opening but the terminal ileum appeared normal. Similarly, multiple biopsies of the terminal ileum and ascending colon were obtained for histopathology, polymerase chain reaction (PCR), microscopy, and culture for Mycobacterium tuberculosis (MTB). Histopathological examination of gastric mucosal biopsies showed severe Helicobacter pylori-associated gastritis, whereas a nonspecific chronic inflammatory cell infiltrate was noted in colonic mucosal biopsies. The changes were not suggestive of either Crohn’s disease or mycobacterial infection. Terminal ileal biopsies did not reveal any histological abnormalities. Microscopy and PCR of right colon biopsies were negative for MTB.

Among MSM there was concern that providing adequate post-test counselling would be difficult in community settings such as bars and clubs [39]. Researchers reported overall positive attitudes of staff towards community testing [18, 20, 30, 35, 39, 44]. Staff training was highlighted as an important component of community testing as it increased the levels of comfort about both the testing and the provision of results in this setting [20, 44]. Developing strong relationships and building trust between venue owners HDAC inhibitors cancer and testing staff was also seen as important [35]. In one study examining the attitudes to introducing

HIV testing in bars and saunas frequented by MSM, although venue owners were supportive overall, they did express some concerns that the service may be a deterrent to potential customers [39]. The results of the studies included in this review indicate that community testing initiatives

are successful in diagnosing previously undiagnosed HIV infections among MSM communities [32-34, 37, 38, 41, 43, 45, 46] and people from BME [54, 55] communities and are acceptable to both clients and staff. Rapid testing technologies increased the likelihood of a person receiving their test result and are acceptable to clients [18, 20, 23, 27, 46]. The proportions of patients testing in community settings who had never previously Erastin tested were generally small [17, 18, 27, 31, 34, 36, 41, 43, 47, 51, 59]. In addition,

comparisons of seropositivity among clients attending community testing settings and those attending more traditional settings were conflicting [19, 34, 43, 55]. Therefore, although it is clear that community testing services are providing an important choice for individuals regarding where they have an HIV test, whether the services are diagnosing individuals from who would otherwise not test until they are unwell is less clear. Evidence from the studies included in this review demonstrates the importance of selecting appropriate venues, building relationships with venue owners and choosing suitable locations within those venues [35, 39]. The location should be conducive to providing a confidential testing service of equal professional standard to those services in healthcare facilities. In addition, training of staff conducting the tests as well as of staff working in the venues will increase confidence and acceptability [20, 44]. There are some limitations to our review. Studies were only included if they had been published in peer-reviewed journals and were written in English.

Moreover, we observed upregulation of sae in the agr mutant and upregulation

of agr in the sae mutant compared with the isogenic Newman strain, suggesting that the Agr and Sae may be inhibiting each other. The SigB mutation did not affect ssl5 and ssl8 expression, but they were downregulated in the agr/sigB double mutant, indicating that SigB probably acts synergistically with Agr in their upregulation. Staphylococcus aureus is a significant human pathogen capable of causing a variety of diseases ranging from mild skin and soft tissue infections to bacteremia, pneumonia, endocarditis, and osteomyelitis SCH772984 mouse (Lowy, 1998). The ability of S. aureus to cause a wide range of infections is partly due to the expression of a wide array of virulence factors including, but not limited to, cell wall-associated adhesions, clumping factors, exotoxins, and secreted proteins such as staphylococcal superantigen-like (SSL) proteins (Lowy, 1998; Dinges et al., 2000; Williams et al., 2000; Fitzgerald et al., 2003). The SSL proteins are encoded by a cluster of 11 ssl genes located on S. aureus pathogenicity island-2 (Fitzgerald et al., 2003). These proteins have limited sequence homology to the enterotoxins and toxic shock syndrome toxin 1 and thus represent

a novel family of exotoxin-like AZD6244 mouse proteins (Williams et al., 2000). The overall order of ssl genes on an S. aureus chromosome is conserved, and allelic forms of individual ssl genes have been identified in different strains. The sequence homology

for individual ssl genes ranges from 85% to 100% in different strains. However, 11 ssl genes within a strain have sequence homology from 36% to 67%, suggesting possible selective pressures encountered during infection (Kuroda et al., 2001; Smyth et al., 2007). Every strain of S. aureus examined so far carries a cluster of at least seven of the 11 ssl genes, suggesting that they probably have distinct and possibly nonredundant Tobramycin functions (Arcus et al., 2002; Fitzgerald et al., 2003; Smyth et al., 2007). Expression studies of a family of ssl genes in COL, an early methicillin-resistant S. aureus (MRSA) strain, showed that they are upregulated during the stationary phase like other exotoxin genes (Fitzgerald et al., 2003). SSL5 and SSL11 show high structural homology with the chemotaxis inhibitory protein of S. aureus and have been shown to interfere with the interaction between P-selectin glycoprotein ligand-1 and P-selectin, suggesting that S. aureus uses SSL proteins to prevent neutrophil recruitment towards the site of infection (Bestebroer et al., 2007; Chung et al., 2007). The same binding site was also found in SSL2, SSL3, SSL4, and SSL6 (Baker et al., 2007). SSL7 and SSL9 interact with two separate cell surface ligands of human antigen-presenting cells (monocytes and dendritic cells), leading to internalization by these cells, and may thus play a role in the modulation of host immunity against S.

M41 ATCC12373 falls into class I GAS (Rakonjac et al.,

1995). M41-type GAS-bound HDL might not be disrupted because SOF is not expressed by this strain. Hence HDL binding might be disadvantageous to M41 GAS. In such case, the counter-protective learn more mechanism used by GAS remains unknown. C176, via its V region, could also interact with LDL, whereas C176T (partial V region-truncated variant) still bound to LDL (data not shown), but did not bind HDL. These results suggest that the sites on Scl1 for binding to HDL and LDL may be different. Additionally, C176 could be used for the production of lipid-free serum because it can specifically absorb both LDL and HDL from plasma or serum. ApoAI and ApoAII are major apolipoproteins in HDL. In order to explore the sites of HDL interacting with rScl1, affinity chromatography assays were used to examine the interaction between C176 and purified recombinant ApoAI and ApoAII. However, C176 could bind to neither ApoAI nor ApoAII (data not shown). Purified ApoAI and ApoAII may have different Selleckchem Ion Channel Ligand Library conformations from those of native ApoAI and ApoAII in complex with HDL and so the possibility that C176 can bind to HDL via ApoAI and ApoAII cannot be excluded completely. In summary, the V region of Scl1 derived from M41-type GAS could bind to purified and plasma HDL, and this binding may be mediated by a hydrophobic interaction. The HDL–Scl1 interaction may play Succinyl-CoA an important role during GAS

infection. We thank Y. Pang, S. Du, L.M. Li, and F. Huo for technical assistance. This work was supported by the start-up Grant K32615 from the Inner Mongolia Agricultural University (to R.H.) and in part by National Institutes of Health Grant AI50666 (to S.L.).

Y.G. and C.L. contributed equally to this work. “
“A monomeric hemolysin with a molecular mass of 29 kDa was isolated from fresh fruiting bodies of the split gill mushroom Schizophyllum commune. The hemolysin was purified by successive adsorption on DEAE-cellulose, carboxymethyl-cellulose and Q-Sepharose and finally gel filtration on Superdex 75. This demonstrated the N-terminal sequence ATNYNKCPGA, different from those of previously reported fungal and bacterial hemolysins. The hemolysin was stable up to 40 °C. Only partial activity remained at 50 and 60 °C. Activity was indiscernible at 70 °C. A pH of 6.0 was optimal for activity. The hemolytic activity was most potently inhibited by dithiothreitol, sucrose and raffinose, followed by cellobiose, maltose, rhamnose, inulin, lactose, fructose and inositol. The metal ions Cu2+, Mg2+, Zn2+, Al3+ and Fe3+ significantly, and Pb2+ to a lesser extent, curtailed the activity of the hemolysin. The hemolysin inhibited HIV-1 reverse transcriptase with an IC50 of 1.8 μM. Mushrooms produce a large number of biologically active proteins. Hemolysins (Berne et al., 2002), antifungal proteins (Lam & Ng, 2001), laccases (Giardina et al.

The up-regulation of tryptophan synthase in Pseudomonas sp. TLC6-6.5-4 in the presence of copper was consistent with our transposon mutational analysis (CSM1 trpA) (Table 1). The overexpression of trpA gene induced by copper treatment was reported in Helicobacter pylori (Waidner et al., 2002). Besides tryptophan,

our metabolomic analysis showed that the levels of several other amino acids such as l-proline and l-isoleucine were significantly increased when Pseudomonas sp. TLC6-6.5-4 was grown in the presence of 4 mM copper (Fig. 4), which correlates with the up-regulation of ketol-acid reductoisomerase, an enzyme involved in the biosynthesis of leucine and isoleucine (Table 1). An increase in amino acid synthesis was also identified in the multiple metal-resistant Oligomycin A bacteria P. fluorescens in both biofilm and planktonic selleck chemicals culture, which could be a protective

mechanism against enzyme inhibition or replacement of damaged proteins caused by the presence of copper (Booth et al., 2011). Furthermore, the accumulation of l-proline itself is the protective mechanism that bacteria (and plants and yeast) use to cope with the oxidative stress caused by heavy metals (Nandakumar et al., 2011). The Clp proteases play an important role in regulating cellular functions by refolding or degrading damaged proteins and also regulate the expression of genes involved in oxidative stress and DNA repair (Hengge & Bukau, 2003; Michel et al., 2006). However, very little is known about the role of Clp proteases in Pseudomonas species except for the basic function of proteolysis. Disruption of ClpA in P. putida CA-3 decreased polyhydroxyalkanoates, the intracellular granules,

in response to inorganic nutrient limitation (Goff et al., 2009). In the present study, we demonstrated that the transposon insertion mutant, CSM2, disrupted in Clp protease subunit ClpA showed a significant reduction in copper resistance compared with the wild-type strain. A recent study on Staphylococcus aureus also showed that the expression Interleukin-3 receptor of ClpA was up-regulated in response to copper (Baker et al., 2010). The disruption of ClpA caused the down-regulation of glycosyl transferase and tRNA (guanine-N(7)-)-methyltransferase (Table 1). Glycosyl transferase is essential for bacterial biofilm formation and resistance to oxidative stress (Erb et al., 2009; Tao et al., 2010). The higher levels of tRNA methyltransferase under cellular stress response are likely to reduce the degradation of tRNAs by ribonucleases activated under stress conditions (Thompson & Parker, 2009; Chan et al., 2010). DnaJ-class molecular chaperone (Table 1), whose expression was up-regulated in wild-type strain grown with copper compared with wild type without copper, binds unfolded polypeptide chains, preventing their irreversible aggregation (Düppre et al.

The up-regulation of tryptophan synthase in Pseudomonas sp. TLC6-6.5-4 in the presence of copper was consistent with our transposon mutational analysis (CSM1 trpA) (Table 1). The overexpression of trpA gene induced by copper treatment was reported in Helicobacter pylori (Waidner et al., 2002). Besides tryptophan,

our metabolomic analysis showed that the levels of several other amino acids such as l-proline and l-isoleucine were significantly increased when Pseudomonas sp. TLC6-6.5-4 was grown in the presence of 4 mM copper (Fig. 4), which correlates with the up-regulation of ketol-acid reductoisomerase, an enzyme involved in the biosynthesis of leucine and isoleucine (Table 1). An increase in amino acid synthesis was also identified in the multiple metal-resistant Seliciclib ic50 bacteria P. fluorescens in both biofilm and planktonic find more culture, which could be a protective

mechanism against enzyme inhibition or replacement of damaged proteins caused by the presence of copper (Booth et al., 2011). Furthermore, the accumulation of l-proline itself is the protective mechanism that bacteria (and plants and yeast) use to cope with the oxidative stress caused by heavy metals (Nandakumar et al., 2011). The Clp proteases play an important role in regulating cellular functions by refolding or degrading damaged proteins and also regulate the expression of genes involved in oxidative stress and DNA repair (Hengge & Bukau, 2003; Michel et al., 2006). However, very little is known about the role of Clp proteases in Pseudomonas species except for the basic function of proteolysis. Disruption of ClpA in P. putida CA-3 decreased polyhydroxyalkanoates, the intracellular granules,

in response to inorganic nutrient limitation (Goff et al., 2009). In the present study, we demonstrated that the transposon insertion mutant, CSM2, disrupted in Clp protease subunit ClpA showed a significant reduction in copper resistance compared with the wild-type strain. A recent study on Staphylococcus aureus also showed that the expression Thymidine kinase of ClpA was up-regulated in response to copper (Baker et al., 2010). The disruption of ClpA caused the down-regulation of glycosyl transferase and tRNA (guanine-N(7)-)-methyltransferase (Table 1). Glycosyl transferase is essential for bacterial biofilm formation and resistance to oxidative stress (Erb et al., 2009; Tao et al., 2010). The higher levels of tRNA methyltransferase under cellular stress response are likely to reduce the degradation of tRNAs by ribonucleases activated under stress conditions (Thompson & Parker, 2009; Chan et al., 2010). DnaJ-class molecular chaperone (Table 1), whose expression was up-regulated in wild-type strain grown with copper compared with wild type without copper, binds unfolded polypeptide chains, preventing their irreversible aggregation (Düppre et al.

The up-regulation of tryptophan synthase in Pseudomonas sp. TLC6-6.5-4 in the presence of copper was consistent with our transposon mutational analysis (CSM1 trpA) (Table 1). The overexpression of trpA gene induced by copper treatment was reported in Helicobacter pylori (Waidner et al., 2002). Besides tryptophan,

our metabolomic analysis showed that the levels of several other amino acids such as l-proline and l-isoleucine were significantly increased when Pseudomonas sp. TLC6-6.5-4 was grown in the presence of 4 mM copper (Fig. 4), which correlates with the up-regulation of ketol-acid reductoisomerase, an enzyme involved in the biosynthesis of leucine and isoleucine (Table 1). An increase in amino acid synthesis was also identified in the multiple metal-resistant click here bacteria P. fluorescens in both biofilm and planktonic Selleckchem PD-332991 culture, which could be a protective

mechanism against enzyme inhibition or replacement of damaged proteins caused by the presence of copper (Booth et al., 2011). Furthermore, the accumulation of l-proline itself is the protective mechanism that bacteria (and plants and yeast) use to cope with the oxidative stress caused by heavy metals (Nandakumar et al., 2011). The Clp proteases play an important role in regulating cellular functions by refolding or degrading damaged proteins and also regulate the expression of genes involved in oxidative stress and DNA repair (Hengge & Bukau, 2003; Michel et al., 2006). However, very little is known about the role of Clp proteases in Pseudomonas species except for the basic function of proteolysis. Disruption of ClpA in P. putida CA-3 decreased polyhydroxyalkanoates, the intracellular granules,

in response to inorganic nutrient limitation (Goff et al., 2009). In the present study, we demonstrated that the transposon insertion mutant, CSM2, disrupted in Clp protease subunit ClpA showed a significant reduction in copper resistance compared with the wild-type strain. A recent study on Staphylococcus aureus also showed that the expression Etofibrate of ClpA was up-regulated in response to copper (Baker et al., 2010). The disruption of ClpA caused the down-regulation of glycosyl transferase and tRNA (guanine-N(7)-)-methyltransferase (Table 1). Glycosyl transferase is essential for bacterial biofilm formation and resistance to oxidative stress (Erb et al., 2009; Tao et al., 2010). The higher levels of tRNA methyltransferase under cellular stress response are likely to reduce the degradation of tRNAs by ribonucleases activated under stress conditions (Thompson & Parker, 2009; Chan et al., 2010). DnaJ-class molecular chaperone (Table 1), whose expression was up-regulated in wild-type strain grown with copper compared with wild type without copper, binds unfolded polypeptide chains, preventing their irreversible aggregation (Düppre et al.

The MBA proteins of ureaplasmas appear to be particularly analogous to the Vsa proteins because of the size variation that results from gain or loss of tandem repeats and the phase variation that results from DNA inversion (Zimmerman et al., 2011). Proteins that undergo extensive size variation because of gain or loss of tandem repeats has been described for other pathogenic species of Mycoplasma including M. agalactiae, M. arthritidis, M. bovis, M. hominis, and M. hyorhinis (Yogev et al., 1991; Lysnyansky et al., 1996; Zhang Regorafenib & Wise, 1996; Ladefoged, 2000; Tu et al., 2005; Nouvel et al., 2009), but the

pathogenic significance and effect on cytoadherence of protein size variation in these species have

for the most part not been studied. Mycoplasmas producing a long Vsa protein have been shown in previous Thiazovivin manufacturer studies to be shielded from the lytic effects of complement and to have a markedly reduced ability to form a biofilm on glass and plastic surfaces (Simmons & Dybvig, 2003; Simmons et al., 2004, 2007). We extend these findings in this study to include cytoadherence. Independent of the Vsa isotype, mycoplasmas producing a long Vsa protein adhered less efficiently to epithelial cells than did mycoplasmas producing a short Vsa protein. We also found that the EPS-I polysaccharide is required for full cytoadherence. The mutants that lack the polysaccharide exhibited extremely poor adherence to MLE-12 cells, despite the fact that these mutants adhere robustly to abiotic surfaces and efficiently colonize mice in vivo (Daubenspeck et al., 2009). Cytoadherence in this system may be complex. Although it is possible that EPS-I, which is composed of glucose and galactose, serves as an adhesin, the addition of the pertinent monosaccharides galactose and glucose or the disaccharide lactose to binding

assays failed to inhibit the adherence of M. pulmonis to erythrocytes (Minion et al., 1984). Nevertheless, EPS-I may be required for an initial 6-phosphogluconolactonase interaction that brings the mycoplasma into close contact with host cells. The adhesins that are responsible for cytoadherence may be partially buried within the Vsa shield when the Vsa proteins are long. These adhesins would be exposed leading to efficient adherence when the Vsa proteins are short. This suggested process for adherence of the mycoplasma to host cells is reminiscent of a model proposed by Minion et al. (1984). Because of the high frequency of Vsa size variation that occurs during growth of the mycoplasma (Simmons et al., 2007), varied subpopulations of mycoplasmas would be present throughout the infection with some cells more adherent than others. The presence of the adherent population would be needed for colonization. The nonadherent population might better resist interactions with macrophages and other cells of the host immune system.

Moreover, following induction of apoptosis by shifting the medium from a high (25 mm) to a low (5 mm) potassium concentration, we observed that: (i) LAP1 levels are decreased in the PCI-32765 chemical structure nuclear fraction, but not in the cytosolic fraction, and its Ser105 phosphorylation disappears; and (ii) in parallel, LIP levels are increased in the nuclear fraction. Furthermore, by transfecting

CGNs with plasmids expressing LAP1, LAP2, or LIP, we observed that: (i) LAP2, but not LAP1, is transcriptionally active, as demonstrated by luciferase activity in pODC–Luc-co-transfected cells; and that (ii) both LAP2 and LAP1 were able to counteract apoptosis in transfected neurons, whereas LIP overexpression did not show any effect on neuronal survival/death. Finally, Lumacaftor in stable clones overexpressing LAP2 or LIP in DAOY medulloblastoma cells, derived from cerebellar neuron precursors, LAP2, but not LIP, was able to protect these cells from lactacystin toxicity. The role of C/EBP β in neurons has been mainly studied in relation to its transcriptional regulation of neuronal activity, memory, neurogenesis, and neuronal differentiation (Yukawa et al.,1998; Taubenfeld et al.,2001a,b; Cortés-Canteli et al.,2002,2011; Paquin et al.,2005; Garcia-Osta et al.,2006; Calella et al.,2007).

However, C/EBP β has also been proposed to be involved in neurodegenerative diseases, both acute, such as brain injury, ischemia, and stroke (Soga et al.,

2003; Cortés-Canteli et al., 2004, 2008; Nadeau et al., 2005; Kapadia et al., 2006), and chronic, such as Huntington’s disease (Obrietan & Hoyt, 2004). This dual role has emerged from in vivo models of brain injury, in which C/EBP β protein is upregulated and induces the expression of pro-inflammatory genes (Cortés-Canteli et al., 2004, 2008), but also of regeneration-associated genes (Nadeau et al., 2005). In ischemia, C/EBPs, including C/EBP β, are expressed in the selectively vulnerable regions during neuronal degeneration, suggesting roles in progression towards death and DNA fragmentation (Soga et al., 2003), and in the regulation of gene expression in post-ischemic inflammation and Coproporphyrinogen III oxidase brain damage (Kapadia et al., 2006). More recently, it has been demonstrated that upregulation of C/EBP β expression in hypoxic conditions plays a neuroprotective role both in vitro and in vivo (Halterman et al., 2008; Rininger et al., 2012). It is important to note, however, that C/EBP β-dependent expression of inflammatory and neurodegenerative genes seems to be largely attibutable to the activity of C/EBP β in non-neuronal cells, such as microglia and astrocytes (Cardinaux et al., 2000; Pérez-Capote et al., 2006; Ejarque-Ortiz et al., 2007; Samuelsson et al., 2008; Ruffell et al., 2009; Sandhir & Berman, 2010). It is thus useful to study the role of C/EBP β in neuronal survival or death in in vitro models without glial cells.