Abstract
Isoniazid (INH) is one of the first-line anti-tuberculosis drugs. Its effect on oxidative stress, however, is unknown. Here we used a model of oxidative stress by employing glucose/glucose oxidase (GOx), which (based on the availability of glucose and oxygen) is known to produce H2O2. This reaction induces oxidative stress culminating in necrotic cell death in HL-60 cells (a human promyelocytic leukemia cell line). The changes in protein levels have been quantified using global proteome expression changes through stable isotope labeling by amino acids in cell culture (SILAC) followed by LC–MS/MS analysis. A total of 1459 and 1712 proteins were identified in forward and reverse experiments, respectively. However, only 390 proteins were reproducibly identified in both samples. These 390 proteins were taken into account for further analysis which has been described in “Cytoprotective effect of isoniazid against H2O2 derived injury in HL-60 cells” [1].
Highlights
Isoniazid (INH) is one of the first-line anti-tuberculosis drugs
The project profiles and analyzes the expression patterns in INH treated HL-60 cells which had been simultaneously exposed to H2O2
The basic experimental design involved the co-exposure of both glucose oxidase (GOx) and 2.5 mM of INH to HL-60 cells for 4 h
Summary
Data format Experimental factors Experimental features Data source location Data accessibility. SILAC-based proteomics in a mammalian cell line (HL-60). Proteomic readout tables (MS Excels) Stable Isotope (13C6) labeling by L-Lysine and L-Arginine in HL-60 cells, run reactions, cell lysis, SDS-PAGE & scanning through LI-COR Odyssey gel scanner, in-gel digestion and LC-MS/MS analysis using nanoflow HPLC (Easy-nLC II, Thermo Scientific) coupled to the LTQ XL-Orbitrap hybrid mass spectrometer (MS) (Thermo Scientific). Raw and analyzed data Protein expression in HL-60 cells at a 4 h time point. The project profiles and analyzes the expression patterns in INH treated HL-60 cells which had been simultaneously exposed to H2O2.
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