Cellular proteome datasets of human endothelial cells under physiologic state and after treatment with caffeine and epigallocatechin-3-gallate

Abstract

Human endothelial cells play several significant roles in vascular biology and homeostasis. We report herein cellular proteome datasets of EA.hy926 human endothelial cells under physiologic condition and after treatment with 100 μM caffeine or EGCG for 24-h. Cellular proteins were extracted and subjected to in-solution tryptic digestion using filter-aided sample preparation (FASP) method. The digested peptides were analyzed by nanoflow liquid chromatography coupled to tandem mass spectrometry (nanoLC-ESI-Qq-TOF MS/MS). Finally, the mass spectral data were searched against the human Swiss-Prot database using Mascot 2.4 search engine and quantified using Skyline v.3.5 software and BiblioSpec algorithm. All of these data were used for further comparative proteomics study followed by bioinformatics analyses to investigate differential biochemical effects of caffeine and EGCG on human endothelial cells (Chanthick et al., 2019) [1].

Caffeine causes cell cycle arrest at G0/G1 and increases of ubiquitinated proteins, ATP and mitochondrial membrane potential in renal cells

“…Herein, our data revealed a small portion of the cellular proteome of MDCK renal cells that were significantly altered by 100 µM caffeine treatment for 24 h, suggesting that the condition used herein did not induce obvious cytotoxic effects, but rather reflected the cellular adaptive response of the renal cells to caffeine. In addition, our findings were consistent with the findings reported from previous studies showing that caffeine commonly affects ribosome and cytoplasmic translation of HepG2 hepatocytes [32] and EA.hy926 endothelial cells [34] , [35] , implicating that caffeine regulates cytoplasmic translation and mRNA metabolic process.…”

Characterizations of annexin A1-interacting proteins in apical membrane and cytosolic compartments of renal tubular epithelial cells

“…In‑solution tryptic digestion and nanoLC‑ESI‑Qq-TOF MS/MS were done as previously described [39] , [40] . Details are also provided in Supplementary Methods .…”

Oxidative Modifications Switch Modulatory Activities of Urinary Proteins From Inhibiting to Promoting Calcium Oxalate Crystallization, Growth, and Aggregation

“…An equal amount of 50 μg of proteins from modified or nonmodified urine samples was tryptic digested into peptides according to the filter-aided sample preparation protocol as described previously ( 38 , 39 ). Briefly, protein samples were resuspended in 4% SDS, 100 mM DTT, and 100 mM Tris–HCl (pH 7.6) lysis buffer and were reduced by heating at 95 °C for 5 min.…”