ADRIANA MACHADO SALDIBA DE LIMA

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LIM/10 - Laboratório de Lípides, Hospital das Clínicas, Faculdade de Medicina

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  • article 14 Citação(ões) na Scopus
    Glycated human serum albumin isolated from poorly controlled diabetic patients impairs cholesterol efflux from macrophages: an investigation by mass spectrometry
    (2015) CASTILHO, Gabriela; SARTORI, Camila H.; MACHADO-LIMA, Adriana; NAKANDAKARE, Edna R.; CORREA-GIANNELLA, Maria Lucia C.; ROVERSO, Marco; PORCU, Simona; LAPOLLA, Annunziata; TRALDI, Pietro; PASSARELLI, Marisa
    Advanced glycation end-products impair ABCA-1-mediated cholesterol efflux by eliciting inflammation, the generation of reactive oxygen species and endoplasmatic reticulum (ER) stress. The glycation level of human serum albumin (HSA) from type 1 and type 2 diabetic patients was determined by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry and related to possible impairment of ER function and cellular cholesterol efflux. Comparison of the MALDI spectra from healthy and diabetic subjects allowed us to determine an increased HSA mean mass of 1297 Da for type 1 and 890 Da for type 2. These values reflect a mean condensation of at least 8 glucose units and 5 glucose units, respectively. Mouse peritoneal macrophages were treated with HSA from control, type 1 and type 2 diabetic subjects in order to measure the expression of Grp78, Grp94, protein disulfide isomerase (PDI), calreticulin (CRT), and ABCA-1. C-14-cholesterol overloaded-J774 macrophages were treated with HSA from control and diabetic subjects and further incubated with apo A-1 to determine the cholesterol efflux. Combined analyses comprising HSA from type 1 and type 2 diabetic patients were performed in cellular functional assays. In macrophages, PDI expression increased 89% and CRT 3.4 times in comparison to HSA from the control subjects. ABCA-1 protein level and apo A-I-mediated cholesterol efflux were, respectively, 50% and 60% reduced in macrophages exposed to HSA from type 1 and type 2 diabetic patients when compared to that exposed to HSA from control subjects. We provide evidence that the level of glycation that occurs in albumin in vivo damages the ER function related to the impairment in macrophage reverse cholesterol transport, and so contributes to atherosclerosis in diabetes.
  • article 29 Citação(ões) na Scopus
    In Type 2 Diabetes Mellitus Glycated Albumin Alters Macrophage Gene Expression Impairing ABCA1-Mediated Cholesterol Efflux
    (2015) MACHADO-LIMA, Adriana; IBORRA, Rodrigo T.; PINTO, Raphael S.; CASTILHO, Gabriela; SARTORI, Camila H.; OLIVEIRA, Erika R.; OKUDA, Ligia S.; NAKANDAKARE, Edna R.; GIANNELLA-NETO, Daniel; MACHADO, Ubiratan F.; CORREA-GIANNELLA, Maria Lucia C.; TRALDI, Pietro; PORCU, Simona; ROVERSO, Marco; LAPOLLA, Annunziata; PASSARELLI, Marisa
    Advanced glycation end products (AGE) are elevated in diabetes mellitus (DM) and predict the development of atherosclerosis. AGE-albumin induces oxidative stress, which is linked to a reduction in ABCA-1 and cholesterol efflux. We characterized the glycation level of human serum albumin (HSA) isolated from poorly controlled DM2 (n=11) patients compared with that of control (C, n=12) individuals and determined the mechanism by which DM2-HSA can interfere in macrophage lipid accumulation. The HSA glycation level was analyzed by MALDI/MS. Macrophages were treated for 18h with C- or DM2-HSA to measure the C-14-cholesterol efflux, the intracellular lipid accumulation and the cellular ABCA-1 protein content. Agilent arrays (44000 probes) were used to analyze gene expression, and the differentially expressed genes were validated by real-time RT-PCR. An increased mean mass was observed in DM2-HSA compared with C-HSA, reflecting the condensation of at least 5 units of glucose. The cholesterol efflux mediated by apo AI, HDL3, and HDL2 was impaired in DM2-HSA-treated cells, which was related to greater intracellular lipid accumulation. DM2-HSA decreased Abcg1 mRNA expression by 26%. Abca1 mRNA was unchanged, although the final ABCA-1 protein content decreased. Compared with C-HAS-treated cells, NADPH oxidase 4 mRNA expression increased in cells after DM2-HSA treatment. Stearoyl-Coenzyme A desaturase 1, janus kinase 2, and low density lipoprotein receptor mRNAs were reduced by DM2-HSA. The level of glycation that occurs in vivo in DM2-HSA-treated cells selectively alters macrophage gene expression, impairing cholesterol efflux and eliciting intracellular lipid accumulation, which contribute to atherogenesis, in individuals with DM2. J. Cell. Physiol. XXXX: XX-XX, 2015. (c) 2015 Wiley Periodicals, Inc. J. Cell. Physiol. 230: 1250-1257, 2015. (c) 2014 Wiley Periodicals, Inc., A Wiley Company