p(HGNC:ALB)
As shown in Fig. 2d, heme/H2O2/ NO2−-induced loss of cell viability was significantly attenuated by BSA or BSA-T pretreatment, and BSA was more effective than BSA-T. PubMed:30324533
However, pretreatment with 2 μM BSA or BSA-T, we found that both BSA and BSA-T efficiently inhibited heme/H2O2/NO2 −- induced cell apoptotic and increased cell yields. PubMed:30324533
As quantified in Fig. 3c, although heme/H2O2/NO2 − increased the apoptotic rate to 32 ± 6.4%, BSA or BSA-T pretreatment caused a statistically significant reduced apoptotic rate (10 ± 5.0% and 15 ± 6.1%, respectively). PubMed:30324533
HRG strongly inhibited the aggregation at a concentration of 1 mg/mL, whereas the same concentration of HSA showed no effect (Fig. 1B). PubMed:29544683
HRG and HSA both strongly inhibited aggregation when the concentration was increased to 100 mg/mL (Supplementary Fig. 1). PubMed:29544683
HRG and HSA both inhibited PS expression when their concentrations were increased to 10 and 100 mg/mL (Fig. 2B). PubMed:29544683
HRG treatment significantly inhibited the attachment of erythrocytes to the vascular endothelial cell monolayer in a concentration dependent manner (Fig. 4A and B), while HSA did not affect the adhesion. PubMed:29544683
Serum albumin (SA) can act as the heme scavenger by forming heme-SA complex [2, 4–8]. PubMed:30324533
As shown in Fig. 2d, heme/H2O2/ NO2−-induced loss of cell viability was significantly attenuated by BSA or BSA-T pretreatment, and BSA was more effective than BSA-T. PubMed:30324533
However, pretreatment with 2 μM BSA or BSA-T, we found that both BSA and BSA-T efficiently inhibited heme/H2O2/NO2 −- induced cell apoptotic and increased cell yields. PubMed:30324533
However, pretreatment with 2 μM BSA or BSA-T, we found that both BSA and BSA-T efficiently inhibited heme/H2O2/NO2 −- induced cell apoptotic and increased cell yields. PubMed:30324533
As quantified in Fig. 3c, although heme/H2O2/NO2 − increased the apoptotic rate to 32 ± 6.4%, BSA or BSA-T pretreatment caused a statistically significant reduced apoptotic rate (10 ± 5.0% and 15 ± 6.1%, respectively). PubMed:30324533
Both BSA and BSA-T attenuated heme/H2O2/NO2 −-induced protein carbonylation and lipid peroxidation. PubMed:30324533
Both BSA and BSA-T attenuated heme/H2O2/NO2 −-induced protein carbonylation and lipid peroxidation. PubMed:30324533
Of note, incubation with BSA or BSA-T for 24 h decreased heme/ H2O2/NO2 −-derived 3-NT deposits as compared with heme/ H2O2/NO2 − treatment alone, and BSA is more effective on suppressing the formation of 3-NT than BSA-T (Fig. 5b). PubMed:30324533
BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.
If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.