scholarly journals Proteomic Analysis of Acetaminophen-Induced Changes in Mitochondrial Protein Expression Using Spectral Counting

2011 ◽  
Vol 24 (4) ◽  
pp. 549-558 ◽  
Author(s):  
Brendan D. Stamper ◽  
Isaac Mohar ◽  
Terrance J. Kavanagh ◽  
Sidney D. Nelson
Keyword(s):  
Protein Expression ◽  
Proteomic Analysis ◽  
Mitochondrial Protein ◽  
Spectral Counting ◽  
Induced Changes

Proteomic analysis of changes in mitochondrial protein expression during peach fruit ripening and senescence

2016 ◽  
Vol 147 ◽  
pp. 197-211 ◽  
Author(s):  
Xiaoqin Wu ◽  
Li Jiang ◽  
Mingliang Yu ◽  
Xiujuan An ◽  
Ruijuan Ma ◽  
...  
Keyword(s):  
Protein Expression ◽  
Fruit Ripening ◽  
Proteomic Analysis ◽  
Mitochondrial Protein ◽  
Peach Fruit

Proteomic analysis of changes in mitochondrial protein expression during fruit senescence

PROTEOMICS ◽  
2009 ◽  
Vol 9 (17) ◽  
pp. 4241-4253 ◽  
Author(s):  
Guozheng Qin ◽  
Qing Wang ◽  
Jia Liu ◽  
Boqiang Li ◽  
Shiping Tian
Keyword(s):  
Protein Expression ◽  
Proteomic Analysis ◽  
Mitochondrial Protein

62 COMPARATIVE PROTEOMIC ANALYSIS OF LIVER MITOCHONDRIA DERIVED FROM DECEASED NEWBORN CLONED CALVES AND ADULT CLONES BY TWO-DIMENSIONAL DIFFERENTIAL GEL ELECTROPHORESIS

2011 ◽  
Vol 23 (1) ◽  
pp. 137
Author(s):  
K. Takeda ◽  
M. Tasai ◽  
S. Akagi ◽  
S. Watanabe ◽  
M. Oe ◽  
...  
Keyword(s):  
Protein Expression ◽  
Somatic Cell ◽  
Proteomic Analysis ◽  
Gel Electrophoresis ◽  
Mitochondrial Protein ◽  
Two Dimensional ◽  
Cell Nuclei ◽  
Comparative Proteomic Analysis ◽  
Mitochondrial Fractions

Aberrant reprogramming of donor somatic cell nuclei may result in many severe problems in animal cloning. The inability to establish functional interactions between donor nucleus and recipient mitochondria is also likely responsible for developmental deficiency. However, an understanding of the expressed proteins in cattle is lacking. In the present study, alterations in mitochondrial protein levels between somatic cell nuclear transferred (SCNT) and control animals (mostly produced by AI) were investigated. Nuclear transfer was performed using donor cells prepared from cumulus cells (B1), ear skin, or skeletal muscle from adult Japanese Black cattle, and enucleated in vitro matured oocytes (Holstein or Japanese Black) as previously reported (Akagi et al. 2003). Liver samples were collected from postmortem SCNT calves (CB1-3; 0, 1, and 9 days postnatally) and adult SCNT cattle (CA1-4; 6, 6, 6, and 5 years of age) produced from the same cell line (B1) and preserved at –80°C. Mitochondrial fractions were prepared from the frozen–thawed liver samples by mechanical homogenization and differential centrifugation, and subjected to two-dimensional difference in gel electrophoresis (2D-DIGE) using CyDye™ dyes (Cy2, Cy3, Cy5; GE Healthcare) for specific labelling. Protein expression changes were confirmed by ImageMaster 2D Platinum software with a volume ratio greater than 2.0 (Student’s t-test; P < 0.05). The expression of 5 proteins were up-regulated in SCNT calves compared to control calves (n = 6; Day 250 fetus, 0, 4, 8, 8, and 8 days after birth; P < 0.05). Expressed protein patterning compared to control groups was different among SCNT calves. The protein spots of CB-1 showed great differences compared with other SCNT calves; 13 spots were up-regulated, and 18 spots were down-regulated. In adult SCNT cattle, the concentrations of 3 proteins were higher when compared to control cattle (n = 4; 2, 2, 6, and 8 years of age; P < 0.05). Protein expression was different among individual SCNT animals even if they were produced from the same donor cell source. For example, 9 spots were up-regulated and 7 spots were down-regulated in CA-1. In contrast, no differences were detected in 2 of the SCNT cattle (CA-3 and 4; P < 0.05). Novel proteins were not identified in any of the SCNT cattle or calves. In conclusion, alteration of mitochondrial protein expression levels were observed in non-viable neonatal SCNT calves and varied among SCNT individuals; suggesting that mitochondrial related gene expression may be implicated in early losses. Comparative proteomic analysis represents an important tool for further studies on SCNT animals. We thank Dr. C. A. Pinkert (Auburn Univ.) and Dr. Somfai (NARO) for their assistance. This work was supported by a grant from the NARO, Japan.

Proteomic analysis of erythropoietin-induced changes in neuron-like SH-SY5Y cells

2017 ◽  
Vol 42 (2) ◽  
Author(s):  
Zübeyde Erbayraktar ◽  
Zeynep Önkal ◽  
Kemal Kürşad Genç ◽  
Şermin Genç
Keyword(s):  
Proteomic Analysis ◽  
Mitochondrial Protein ◽  
Neuroblastoma Cells ◽  
Cellular Level ◽  
Cytoskeletal Proteins ◽  
Protein Species ◽  
Treatment Regimes ◽  
Proteomics Approach ◽  
Cellular Pathways ◽  
Induced Changes

AbstractObjective:Erythropoietin (EPO) is widely used for treatment of anemia associated with different diseases; however, its adverse effects limit its use in clinical practice. Therefore, understanding the effects of EPO at the molecular and cellular level is crucial to adjust treatment regimes, and to develop non-hematopoietic EPO derivatives. In this study, we used a proteomics approach to identify how EPO treatment modifies the cellular proteome.Methods:SH-SY5Y neuroblastoma cells were used as the model system to analyze the effects of EPO treatment at different time points (24 h and 48 h). Proteomic analysis revealed changes in 74 proteins after EPO treatment. Following proteomics analysis, Reactome pathway analysis were carried out to identify the affected cellular pathways.Results:According to results, EPO alters the levels of 74 protein species (40 were increased, 34 were decreased). The levels of 35 proteins were changed by 24 h EPO incubation, whereas 17 protein species were altered by 48 h EPO incubation. Levels of 22 protein species were altered by both of the incubation periods (24 h and 48 h).Conclusion:Overall, our results suggest that EPO mainly affects protein species in glucose metabolism, protein and RNA metabolism, cytoskeletal proteins, and mitochondrial protein species.

Mass Spectrometry-based Label-free Quantitative Proteomic Analysis of CCl4-induced Acute Liver Injury in Mice Intervened by Total Glycosides from Ligustri Lucidi Fructus

2020 ◽  
Vol 17 ◽  
Author(s):  
Qian Lu ◽  
Hai-Zhu Xing ◽  
Nian-Yun Yang
Keyword(s):  
Insulin Resistance ◽  
Liver Injury ◽  
Protein Expression ◽  
Signaling Pathway ◽  
Proteomic Analysis ◽  
Acute Liver Injury ◽  
Liver Cells ◽  
Differentially Expressed ◽  
Liver Protein ◽  
Differentially Expressed Proteins

Background: CCl4 acute liver injury (ALI) is a classical model for experimental research. However, there are few reports involved in the fundamental research of CCl4-induced ALI Ligustri Lucidi Fructus (LLF) are and its prescription have been used to treat hepatitis illness clinically. LLF and its active ingredients displayed anti-hepatitis effects, but the mechanism of function has not been fully clarified Objective: To investigate the proteomic analysis of CCl4-induced ALI, and examine the effects of active total glycosides (TG) from LLF on ALI of mice4, including histopathological survey and proteomic changes of liver tissues, and delineate the possible underlying mechanism. Methods: CCl4 was used to produce ALI mice model. The model mice were intragastrically administrated with TG and the liver his-topathological changes of mice were examined. At the end of test, mice liver samples were collected, after protein denaturation, re-duction, desalination and enzymatic hydrolysis, identification was carried out by nano LC-ESI-OrbiTrap MS/MS technology. The data was processed by Maxquant software. The differentially-expressed proteins were screened and identified, and their biological information was also analyzed based on GO and KEGG analysis. Key protein expression was validated by Western blot analysis Results: A total of 705 differentially-expressed proteins were identified during the normal, model and administration group. 9 signifi-cant differential proteins were focused based on analysis. Liver protein expression changes of CCl4-induced ALI mice were mainly involved in several important signal channels, namely FoxO signaling pathway, autophagy-animal, insulin signaling pathway. TG has anti-liver damnification effect in ALI mice, the mechanism of which is related to FoxO1 and autophagy pathways Conclusion: CCl4 inhibited expression of insulin-Like growth factor 1 (Igf1) and 3-phosphoinositide-dependent protein kinase 1 (Pdpk1) in liver cells and induced insulin resistance, thus interfered with mitochondrial autophagy and regeneration of liver cells and the metabolism of glucose and lipid, and caused hepatic necrosis in mice. TG resisted liver injury in mice. TG adjusted the expression level of key proteins Igf1 and Pdpk1 after liver injury and improved insulin resistance, thus promoted autophagy and resisted the liver damage

scholarly journals Quantitative Proteomic Analysis of Plasma after Remote Ischemic Conditioning in a Rhesus Monkey Ischemic Stroke Model

Biomolecules ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 1164
Author(s):  
Siying Song ◽  
Linlin Guo ◽  
Di Wu ◽  
Jingfei Shi ◽  
Yunxia Duan ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Rhesus Monkey ◽  
Proteomic Analysis ◽  
Complement C3 ◽  
Protective Effects ◽  
Plasma Proteome ◽  
Remote Ischemic Conditioning ◽  
Ischemic Conditioning ◽  
Metabolism Regulation ◽  
Induced Changes

Background: Animal and clinical studies have shown that remote ischemic conditioning (RIC) has protective effects for cerebral vascular diseases, with induced humoral factor changes in the peripheral blood. However, many findings are heterogeneous, perhaps due to differences in the RIC intervention schemes, enrolled populations, and sample times. This study aimed to examine the RIC-induced changes in the plasma proteome using rhesus monkey models of strokes. Methods: Two adult rhesus monkeys with autologous blood clot-induced middle cerebral artery (MCA) occlusion underwent RIC interventions twice a week for five consecutive weeks. Each RIC treatment included five cycles of five minutes of ischemia alternating with five minutes of reperfusion of the forearm. The blood samples were taken from the median cubital vein of the monkeys at baseline and immediately after each week’s RIC stimulus. The plasma samples were isolated for a proteomic analysis using mass spectrometry (MS). Results: Several proteins related to lipid metabolism (Apolipoprotein A-II and Apolipoprotein C-II), coagulation (Fibrinogen alpha chain and serpin), immunoinflammatory responses (complement C3 and C1), and endovascular hemostasis (basement membrane-specific heparan sulfate proteoglycan) were significantly modulated after the RIC intervention. Many of these induced changes, such as in the lipid metabolism regulation and anticoagulation responses, starting as early as two weeks following the RIC intervention. The complementary activation and protection of the endovascular cells occurred more than three weeks postintervention. Conclusions: Multiple protective effects were induced by RIC and involved lipid metabolism regulation (anti-atherogenesis), anticoagulation (antithrombosis), complement activation, and endovascular homeostasis (anti-inflammation). In conclusion, this study indicates that RIC results in significant modulations of the plasma proteome. It also provides ideas for future research and screening targets.

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