02 ± 0.64 0.49 ± 0.19 7.5 μM iron chloride (FeCl3) 3.63 ± 0.73 2.49 ± 0.64 15.3 μM hemin 1.72 ± 0.92 0.25 ± 0.18 10 μM potassium ferrocyanide Tipifarnib (K4[Fe(CN)6]) (Fe2+) 1.34 ± 1.30 0.38 ± 0.33 10 μM potassium Fer-1 mouse ferricyanide (K3[Fe(CN)6]) (Fe3+) 1.80 ± 2.82 0.93 ± 0.85 10 μM ferric ammonium sulfate (Fe(NH4)(SO4)2) 3.33 ± 2.53 2.02 ± 2.11 50 μM iron citrate (C6H5FeO7) 2.20 ± 0.70 3.47 ± 1.17 300 μM 2,2′-dipyridyl < 0.01 < 0.01 300 μM 2,2'-dipyridyl and 200 μM FeCl3 0.04 ± 0.07 < 0.01 300 μM 2,2'-dipyridyl and 200 μM iron citrate 1.59 ± 1.16 0.04 ± 0.06 a Cells were cultivated in M9 minimal medium including 0.8% (w/v) glucose. Iron sources were added

at the given final concentrations. b The activities were determined for triplicate experiments. Extracts of a hypF mutant, IKK inhibitor which cannot synthesize active

hydrogenases [16], had essentially no hydrogenase enzyme activity and served as a negative control. Extracts of the feoB::Tn5 mutant PM06 grown in M9 medium in the absence of iron had a total hydrogenase activity that was 24% that of the wild type without addition of iron compounds (Table 1). Growth of PM06 in the presence of iron chloride or ferric ammonium sulfate restored hydrogenase activity to levels similar to wild type. The exception was potassium ferricyanide, which failed to restore hydrogenase enzyme activity to wild type levels; instead activity was approximately Edoxaban 50% of that measured in MC4100 grown without iron supplementation and only 50% of that measured after growth of the wild type with potassium ferricyanide (Table 1). In contrast,

growth of PM06 in the presence of ferrocyanide did not restore hydrogenase activity. Addition of hemin as a source of oxidized iron also failed to restore hydrogenase activity to PM06, presumably because hemin cannot be taken up by E. coli and the oxidized iron is also tightly bound to the porphyrin. Taken together, these results are consistent with the ferrous iron transport system being an important route of iron uptake for hydrogenase biosynthesis in the wild type. Addition of 2, 2′-dipyridyl to the growth medium resulted in total loss of hydrogenase activity of the wild type MC4100 and PM06 (Table 1). Supplementation of 200 μM iron chloride or iron citrate together with 300 μM dipyridyl showed that iron citrate restored 66% of the wild type activity while iron chloride failed to restore activity. None of these additions restored hydrogenase activity to PM06. The activities of Hyd-1 and Hyd-2 can be visualized after non-denaturing PAGE followed by specific activity staining [14]; Hyd-3 is labile and cannot be visualized under these conditions. This method allows a specific analysis of the effect of mutations or medium supplements on Hyd-1 and Hyd-2 activity and it should be noted that this method is only semi-quantitative.

This result is a significant contribution to the understanding of cell and substrate behavior during cell interaction with chemically active polymer in tissue engineering field. Due to plasma treatment and subsequent BSA grafting to polymer surface, the

cell adhesion and proliferation can be stimulated due to the presence of active functional groups on the surface, which improves the electrostatic interactions between substrates and cells. Acknowledgements This work was supported by the GACR under project P108/12/G108. References 1. Rebollar E, Frischauf I, Olbrich M, Peterbauer T, Hering S, Preiner J, Hinterdorferb P, Romaninb C, Heitz J: Proliferation of aligned mammalian cells on laser-nanostructured polystyrene. Anlotinib order Biomaterials 2008, 29:1796–1806.CrossRef 2. Puppi D, Chiellini F, Piras AM, Chiellini E: Polymeric materials for bone and cartilage repair. Prog Polym Sci 2010, 35:403–440.CrossRef 3. Leor J, Amsalem Y, Cohen S: Cells, scaffolds, and molecules for myocardial tissue engineering. Pharmacol Therapeut 2005, 105:151–163.CrossRef 4. Langer R, Tirrell DA: Designing materials for biology and medicine. Nature 2004, 428:487–492.CrossRef 5. Tabata Y: Biomaterial technology for tissue engineering applications. J R Soc Interface 2009,

6:311–324.CrossRef 6. Shen Q, Shi P, Gao M, Yu X, Liu Y, Luo L, Zhu Y: Progress on materials and scaffold fabrications applied to esophageal tissue engineering. Mater Sci Eng C 2013, 33:1860–1866.CrossRef 7. Nair LS, Laurencin check details CT: Polymers as biomaterials for tissue engineering and controlled drug delivery. Etofibrate Adv Biochem Eng Biot 2006, 102:47–90. 8. Oehr C: Plasma surface modification of polymers for biomedical use. Nucl Instrum Meth B 2003, 208:40–47.CrossRef 9. Gauvin R, Khademhosseini A, Guillemette M, Langer R: Emerging trends in tissue engineering. In Comprehensive Biotechnology. 2nd GSK2399872A research buy edition. Edited

by: Moo-Young M. Amsterdam: Elsevier B.V; 2011:251–263.CrossRef 10. McKellop H, Shen FW, Lu B, Campbell P, Salovey R: Development of an extremely wear-resistant ultra high molecular weight polyethylene for total hip replacements. J Orthop Res 1999, 17:157–167.CrossRef 11. Kang ET, Zhang Y: Surface modification of fluoropolymers via molecular design. Adv Mater 2000, 12:1481–1494.CrossRef 12. Lin YS, Wang SS, Chung TW, Wang YH, Chiou SH, Hsu JJ, Chou NK, Hsieh KH, Chu SH: Growth of endothelial cells on different concentrations of Gly-Arg-Gly-Asp photochemically grafted in polyethylene glycol modified polyurethane. Artif Organs 2001, 25:617–621.CrossRef 13. Švorčík V, Hnatowicz V, Stopka P, Bačáková L, Heitz J, Öchsner R, Ryssel H: Amino acids grafting of Ar + ions modified PE. Radiat Phys Chem 2001, 60:89–93.CrossRef 14. Rademacher A, Paulitschke M, Meyer R, Hetzer R: Endothelialization of PTFE vascular grafts under flow induces significant cell changes. Int J Artif Organs 2001, 24:235–242. 15.

It has recently been proposed as the official primary barcoding marker for fungi (Deliberation of 37 mycologists from 12 countries at the Smithsonian’s Conservation and Research Centre, Front Royal, Virginia, May 2007). More than 100 000 fungal ITS sequences generated by see more conventional Sanger sequencing are deposited in the International Nucleotide Sequence Databases and/or

other databases [11], providing a large reference material for identification of fungal taxa. However, these data are to some extent hampered by misidentifications or technical errors such as mixing of DNA templates or sequencing errors [12]. Furthermore, a large amount of partial ITS sequences generated by next-generation sequencing has GM6001 order recently been deposited in public sequence databases. The ITS region includes the ITS1 and ITS2 regions, separated by the 5.8S gene, and is situated between the 18S (SSU) and 28S (LSU) genes in the nrDNA repeat unit (Figure 1). The large number of ITS copies per cell (up to 250; [13]) makes the region an appealing target for sequencing environmental substrates where the quantity of DNA

present is low. The entire ITS region has commonly been targeted with traditional Sanger sequencing approaches and typically ranges between 450 and 700 bp. Either the ITS1 or the ITS2 region have been targeted in recent high-throughput sequencing this website studies [14–17], because the entire ITS region is still too long for 454 sequencing or other high-throughput sequencing methods. Using high-throughput sequencing, thousands of sequences can be analysed from a single environmental sample, enabling in-depth analysis of the fungal diversity. Various primers Sclareol are used for amplifying the entire or parts of the ITS region (Figure 1). The most commonly used primers were published

early in the 1990′s (e.g. [18, 19] when only a small fraction of the molecular variation in the nrDNA repeat across the fungal kingdom was known. Several other ITS primers have been published more recently [20] but have not been used extensively compared to the earlier published primers. However, little is actually known about the potential biases that commonly used ITS primers introduce during PCR amplification. Especially during high-throughput sequencing, where quantification (or semi-quantification) of species abundances is also possible to a certain degree (although hampered by factors like copy-number variation), primer mismatches might potentially introduce large biases in the results because some taxonomic groups are favoured during PCR. Our main focus in this study is on the two dominating taxonomic groups of fungi in the Dikarya, Ascomycota and Basidiomycota.

Pharmacy networks in PHARMO typically comprise a sample of pharmacies in different geographic regions, with careful geographical selection of urban and rural community pharmacies. The provision of pharmaceutical services from Dutch Y-27632 in vitro pharmacies is population-based. Specific populations (e.g. the very poor,

the unemployed) are therefore not excluded from pharmaceutical services. This is an important issue with respect to external validity to populations outside the PHARMO database. Validation studies on PHARMO RLS have confirmed a high level of data completeness and validity with regards to fractures [27, 28]. Study population Data were collected for the period 1 January 1991 to 31 December 2002. Cases were patients aged

18 years and older with a record for a first fracture of the hip or femur during the study period. The index date was the date of hospital ML323 mouse admission. Each case was matched to up to four control patients by year of birth, sex and geographical region. Each control was assigned the same index date as the corresponding case. Exposure assessment Exposure to dopaminergic drugs was determined by reviewing dispensing information prior to the index date: (a) dopamine agonists: bromocriptine, lisuride, pergolide, ATM/ATR inhibitor drugs ropinirole, pramipexole, cabergoline and apomorphine (excluding the sublingual administration form) and Dynein (b) levodopa-containing drugs. The indications these drugs were prescribed for were not recorded in the PHARMO database. For each dispensing of a dopaminergic drug, the written dosage instruction was used to estimate its exposure episode. If a written dosage instruction was missing, the median value of all dispensings was used. ‘Current’ users were patients who were exposed to dopaminergic drugs within the 30-day period before the index date. ‘Recent’ users had discontinued dopaminergic drugs between 31 and 182 days

before the index date. ‘Past’ users had stopped taking dopaminergic drugs >182 days before the index date. Concomitant exposure to psychotropics [anticholinergics (biperiden, dexetimide, orphenadrine, procyclidine, trihexyphenidyl), antidepressants, antipsychotics and benzodiazepines] was measured within the current dopaminergic drug users. For each current dopaminergic drug user, the continuous duration of use was determined by adding up all dopaminergic exposure episodes before the index date. If the period between two exposure episodes exceeded 3 months, this was considered a treatment gap. Exposure episodes before a treatment gap were not added to the total period of continuous duration of use. Potential confounders The records of cases and controls were reviewed for evidence of potential confounders that have previously been associated with fracture risk [29, 30].

Distribution of SSU0757 in S. suis Selected S. suis strains were tested for the presence of the subtilisin-encoding gene (SSU0757): S428 (serotype 1), 31533 (serotype 2), 89-999 (serotype 2), S735 (serotype 2), 90-1330 (serotype 2), 65 (serotype 2), https://www.selleckchem.com/products/brigatinib-ap26113.html 89-4223 (serotype this website 2), 2651 (serotype 1/2), 4961 (serotype 3), Amy12C (serotype 5), 1078212 (untypeable), and 1079277 (untypeable). Except for strains 90-1330, 65 and 89-4223, which were isolated from healthy pigs, all

other isolates were from diseased pigs. Cell lysates were prepared from bacterial colonies recovered from agar plates. The presence of the gene was determined by PCR using the SUB163 (5′-GTCAGCGAATCAGCCTCAGAAAGTCCCGTT-3′) and SUB4436R (5′-CTTCATCTTTTTTGTCAGTGGCAGTATTTG-3′) primers. Growth studies The generation times of S. suis wild-type strain P1/7 and the proteinase-deficient mutants were determined by inoculating erythromycin-free THB with late-log phase cultures and monitoring growth at OD660. Generation times were calculated from the growth curves. Susceptibility to whole blood Venous blood samples were collected from the antecubital vein of a human volunteer using the Vacutainer™ system and sterile endotoxin-free blood collection tubes containing 150 IU of sodium heparin (Becton Dickinson,

Franklin Lakes, NJ, USA). Informed consent was obtained from the donor prior to the experiment. The protocol was approved by the Université Laval ethics committee. S. MK-8931 price suis (wild-type parent strain and mutants) were cultivated to the early stationary growth phase at 37°C. The cells were harvested by centrifugation at 11,000 g for 10 min, suspended in RPMI-1640 medium to an

OD660 of 0.1, and diluted 1:100 in RPMI-1640 medium. Whole blood (1 ml) was mixed with pig serum anti-S. suis (300 μl) and S. suis cells (100 μl). Anti-S. suis serum was prepared in pigs by injecting whole bacterial cells as previously described [17]. The mixtures were incubated for 4 h at 37°C with occasional gentle shaking. Infected whole blood cultures were harvested at 0 and 4 h. ZD1839 The first time point (0 h) was considered as the 100% viability control. Infected whole blood samples were 10-fold serially diluted (10-1 to 10-4) in PBS and plated on Todd-Hewitt agar plates. After a 24-h incubation at 37°C, the number of colony forming units (cfu) was determined. The experiments were carried out in duplicate. Experimental infections in mice Thirty-nine female six-week-old CD1 mice (Charles River Laboratories, Saint-Constant, QC, Canada) were acclimatized to a 12 h light/dark cycle and were given rodent chow and water ad libitum. On the day of the experiment, the mice (11 per group) were infected by i.p. injection of 1 ml of either S. suis wild-type strain P1/7 or the Tn917 mutants deficient in proteinase activity at a concentration of 7 × 107 CFU/ml in THB. Six control mice were inoculated with the vehicle solution (sterile THB) alone. The CD1 mouse has proven to be an excellent model of S.

miRNA mimics and inhibitors, and siRNA transfection was performed using FuGene® HD transfection reagent (Roche, Mannheim, Germany). In brief, cells were plated in a 24-well plate and grown to 50% confluency. Then, selective HDAC inhibitors 1 μl of FuGene® HD transfection reagent was diluted in 50 μl of Opti-MEM® I Reduced Serum Medium (GIBCO BRL). After that, 100 pmol of siRNA oligomer was diluted in 50 μl of Opti-MEM® I Reduced Serum Medium without serum (final concentration of oligonucleotides

when added to the cells was 20 μM according to the protocol of the manufacture and the preliminary experiments). The FuGene® HD transfection complex and the diluted oligonucleotides were mixed gently and incubated at room temperature. After incubation for 20 min, the complexes were added to each well containing cells and medium. The cells were incubated for 6 h at 37°C in a CO2 incubator prior to testing for transfection. Cell proliferation assay A CCK-8 (Dojindo, Shanghai, China) cell proliferation assay was used to assess cell proliferation, according to the manufacturer’s protocol. Briefly, cells were grown and transfected with hsa-miR-134 and hsa-miR-337-3p mimics and selleck chemical inhibitors (50 nM miRNA scrambled control or buy Pitavastatin miRNA mimic or 200 nM miRNA inhibitor

scrambled control or miRNA inhibitor) for 48 h [15], detached, and cultured in triplicate in 96-well cell culture plates. At the end of the experiments, the cells were washed with phosphate-buffered

saline (PBS), fixed in 1% glutaraldehyde, and stained with 10% CCK-8. The optical density (OD) at 450 nm was directly measured with a Bio-Rad microplate reader (Hercules, CA). Tumor cell invasion assay Gastric cancer cell invasion capacity was assessed by using a two-chamber migration Interleukin-2 receptor system. The upper compartment was inserted into the lower compartment of the BD BioCoat control inserts (BD Discovery Labware, Bedford, MA), 5 × 104 cells in 0.1 mL of serum-free medium containing 1% bovine serum albumin (BSA) were seeded into the upper compartment, and the lower compartment was filled with normal culture medium supplemented with 20% FBS. After incubation for 24 h, cells were wiped away from the upper surface and the cells on the lower surface, which represented the cells that migrated through the control insert membrane, were fixed and stained with crystal violet (Sigma). The number of cells that migrated completely across the filter was determined in five random fields (×400 magnification) for each experiment. Each condition was assayed in triplicate, and each experiment was repeated at least three times. Statistical analysis All experiments were repeated at least three times on different occasions. The results are presented as the mean ± standard deviation (SD) for all values.

e. located before the G1-S transition. However, this hypothesis would not account for the previously mentioned small

percentage of the population that was seemingly blocked in S. The occurrence of a “”DNA replication GS-1101 cell line completion checkpoint”" was suggested for UV-C irradiated E. coli cells [56]. Cells in G1 could not start chromosome replication while S cells could not complete replication selleck kinase inhibitor and hence divide; only cells already in G2 at the time of irradiation were able to complete cytokinesis. In our case, however, because of the tight synchronization of the population, virtually no cell was sufficiently advanced in the cell cycle during the pre-dusk period to complete cytokinesis. It is generally thought that checkpoints are controlled by specific protein complexes involved in signaling (photoreceptors) and/or checking [57]. Thus, Prochlorococcus might possess a UV sensor which, when detecting these wavelengths, could launch a cascade of controlling mechanisms ultimately stopping the replication machinery. A UV-B sensor was characterized in the diazotrophic cyanobacterium Chlorogloeopsis sp. PCC6912 and was shown to mediate the induction of mycosporine-like amino acids synthesis [58]. However, no evidence for such a UV sensor is available in Prochlorococcus and, as argued

later in this paper, its presence is rather unlikely. Recently, Cooper [59] proposed that checkpoints may in fact result from purely internal Selleckchem Y-27632 controls. It is possible that PCC9511 cells actually entered the early S phase but that the extensive occurrence of replication fork

stalling due to accumulated DNA lesions and the elevated need for recovery of the replication process by lesion removal and replisome reloading [60] slowed down or even arrested the whole DNA synthesis process for a few hours, therefore explaining the observed delay without any need for a light sensing signal. The fact that UV-acclimated cultures did not show any obvious decrease in their overall growth rate indicates that if stalling of replication forks occurred, efficient DNA repair mechanisms must have allowed those cells blocked in S to restart and complete chromosome replication. UV stress leads to the downregulation of DNA replication and cell division genes To further our understanding of the molecular bases of the observed delay in S phase completion, we analyzed Aspartate the expression of key genes involved in chromosome replication and cell division. As is typically observed in model bacteria [61, 62], the dnaA gene, encoding the master initiator protein of chromosome replication, was induced just before entry of cells into the S phase. Although an increase in dnaA expression occurred at the same time under HL and HL+UV, its level of expression was considerably lower in the latter condition. It is well known in Escherichia coli that initiation of chromosome replication depends on reaching a threshold level of DnaA protein [63].

Cell culture C6 glioma cells were supplied by Dr. Takashi Masuko (Kinki University, Osaka, Japan) and cultured in Dulbecco’s Modified Eagle’s Medium (Sigma) supplemented with 10% fetal calf serum (FCS) (Gibco, Carlsbad, CA, USA), 100 μg/ml penicillin (Gibco), 100 U/ml streptomycin (Gibco), and 25 mM HEPES (pH 7.4; Wako) in an atmosphere containing 5% CO2. U251MG cells were provided by Health Science Research

Resources Bank (Osaka, Japan) and cultured in minimum essential medium (Sigma) supplemented with 10% fetal calf serum Kinase Inhibitor Library price (Gibco), 100 μg/ml penicillin (Gibco), 100 U/ml streptomycin (Gibco), and 25 mM HEPES (pH 7.4; Wako) in an atmosphere containing 5% CO2. Cell viability Cell viability was quantified by using a trypan blue dye assay. The cells (2000 cells/well) were plated in 96-well plates and incubated with various concentrations of mevastatin, fluvastatin, and simvastatin for 24, 48, and 72 h. After incubation, the cells were stained with trypan blue, and the number of stained cells was counted. Measurement of caspase-3 proteolytic

activity We measured the caspase-3-like enzyme activity by monitoring proteolytic cleavage of the fluorogenic substrate Asp-Glu-Val-Asp-7-Amino-4-trifluoromethylcoumarin (Selleck Z IETD FMK DEVD-AFC) using the ApoTarget caspase-3 protease assay kit (BioSource International Inc., Camarillo, CA). The C6 glioma cells were incubated with or without mevastatin, fluvastatin, and simvastatin CP690550 for 24 h. The cells were then collected, Sinomenine washed in PBS, and lysed in the lysis buffer provided in the aforementioned kit. The assay was performed by incubating a solution of cell lysates containing a 50 μM substrate at 37°C for 1 h. We fluorometrically measured the release of 7-amino-4-methylcoumarin from the substrate by using a fluorescence spectrophotometer (F-4010, Hitachi)

at an emission wavelength of 505 nm and an excitation wavelength of 400 nm. Caspase-3 activity (measured on the basis of proteolytic cleavage of the caspase-3 substrate DEVD-AFC) was expressed in terms of change in substrate concentration (in pM) per h per mg of protein, after correction for the protein content of the lysates; the protein content of the cell lysate was determined by using the bicinchoninic acid (BCA) protein assay kit (Pierce, Rockford, IL, USA). Western blotting C6 glioma cells treated with statins were lysed with a lysis buffer containing 20 mM Tris-HCl (pH 8.0), 150 mM NaCl, 2 mM EDTA, 100 mM NaF, 1% NP-40, 1 μg/ml leupeptin, 1 μg/ml antipain, and 1 mM phenylmethylsulfonyl fluoride. The protein content in the cell lysates was determined using a BCA protein-assay kit. The extracts (40 μg protein) were fractionated on polyacrylamide-SDS gels and transferred to polyvinylidene difluoride (PVDF) membranes (Amersham, Arlington Heights, IL, USA).

Mol Ecol 8:1837–1850CrossRefPubMed Urban A, Puschenreiter M, Strauss J, Gorfer M (2008) Diversity and structure of ectomycorrhizal and co-associated fungal communities in a serpentine soil. Mycorrhiza 18:339–354CrossRefPubMed Urich T, Lanzen A, Qi J, Huson DH, Schleper C, Schuster SC (2008) Simultaneous assessment of soil microbial community structure and function through analysis of the meta-transcriptome. PLoS ONE 3:e2527CrossRefPubMed van der Heijden MG, Bardgett RD, van Straalen NM (2008) The

unseen majority: soil microbes as drivers of plant diversity and productivity in terrestrial ecosystems. Ecol Lett 11:296–310CrossRefPubMed Vandenkoornhuyse P, Baldauf SL, Leyval C, Straczek J, Young JP (2002) Extensive fungal diversity in plant roots. Science 295:2051CrossRefPubMed Waldrop MP, Zak DR, Blackwood CB, Curtis CD, Tilman D (2006) Resource availability controls fungal diversity selleck chemicals across a plant diversity gradient. Ecol Lett 9:1127–1135CrossRefPubMed White TJ, Bruns T, Lee S, Taylor J (1990) Amplification and direct sequencing of fungal ribosomal RNA genes for phylogenetics. In: Innis MH, Gelfand DH, Sninsky JJ, White TJ (eds) PCR protocols: a guide to methods and applications. Academic, San Diego, pp 315–322″
“Introduction Cryptosporiopsis eucalypti is a host-specific

pathogen of Eucalyptus species that occurs over a wide geographical range varying from ALK inhibitor dry to very humid zones including those in Australia, India, Hawaii (Sankaran et al. 1995), New Zealand (Gadgil and Dick 1999), Brazil (Ferreira et al. 1998), Japan, Laos, Indonesia, Sri Lanka, Thailand and Vietnam (Old and Yuan 1994; Old et al. 2003). The selleckchem fungus can be associated with various disease symptoms including leaf spots, shoot blight, cankers on woody tissue, defoliation and even tree death. The leaf spots develop on both sides of leaves and vary in size, shape, and colour among Eucalyptus species (Sharma 1994; Sankaran et al. 1995; Old et al. 2002, 2003). The fungus proliferates by producing

a vast number of spores from conidiomata that develop on infected leaves and shoots. After causing death of shoot tips or small branches, repeated infection can occur over extended Clomifene periods of time. Leaf blight and other foliar diseases induced by C. eucalypti can easily be confused with those caused by other plant-pathogenic fungi, such as Mycosphaerella spp. and their anamorphs (Cheewangkoon et al. 2008, 2009; Crous 2009), and Calonectria (Crous et al. 2004b, 2006a; Lombard et al. 2009, 2010). Although infection by C. eucalypti can eventually lead to yield reduction of Eucalyptus plantations, the biology of this pathogen is not well understood. Infection often appears to be associated with minor mechanical, insect or wind damage (Ciesla et al. 1996), or with lesions caused primarily by Calonectria spp. (Park et al. 2000; Crous 2002).

Electronic supplementary material Additional file 1: Figure S1. Title of data: Moderate steatosis db/db mice. Description of data: Hematoxylin and eosin staining showing mild to moderate steatosis in female and male db/db mice as compared to C57BKS mice livers. (PDF 20 MB) Additional file 2: Table S1. Title of data: Primary antibodies for western blot. Description of data: Type, dilution, molecular weight and sources of primary antibodies for western blot. (DOCX 16 KB) References

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