Mortalin, Apoptosis, and Neurodegeneration

Londoño, Carolina; Osorio, Cristina; Gama, Vivian; Álzate, Óscar

doi:10.3390/biom2010143

Cited by 64 publications

(58 citation statements)

References 119 publications

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“…Despite belonging to the HSPs family, the expression of HSPA9 does not increase in response to heat stress. However, it is stimulated by glucose deprivation, Ca 2+ influx and some cytotoxins [39]. Although HSPA9 is associated with anti-apoptotic processes due to its chaperone activity and inhibition of pro-apoptotic factors, it has also been proposed that under conditions of excessive stress, HSPA9 could not be able to prevent cell death and would change the mitochondrial functions leading to apoptosis [39].…”

Section: Resultsmentioning

confidence: 99%

Differences in Beef Quality between Angus (Bos taurus taurus) and Nellore (Bos taurus indicus) Cattle through a Proteomic and Phosphoproteomic Approach

et al. 2017

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Proteins are the major constituents of muscle and are key molecules regulating the metabolic changes during conversion of muscle to meat. Brazil is one of the largest exporters of beef and most Brazilian cattle are composed by zebu (Nellore) genotype. Bos indicus beef is generally leaner and tougher than Bos taurus such as Angus. The aim of this study was to compare the muscle proteomic and phosphoproteomic profile of Angus and Nellore. Seven animals of each breed previously subjected the same growth management were confined for 84 days. Proteins were extracted from Longissimus lumborum samples collected immediately after slaughter and separated by two-dimensional electrophoresis. Pro-Q Diamond stain was used in phosphoproteomics. Proteins identification was performed using matrix assisted laser desorption/ionization time-of-flight mass spectrometry. Tropomyosin alpha-1 chain, troponin-T, myosin light chain-1 fragment, cytoplasmic malate dehydrogenase, alpha-enolase and 78 kDa glucose-regulated protein were more abundant in Nellore, while myosin light chain 3, prohibitin, mitochondrial stress-70 protein and heat shock 70 kDa protein 6 were more abundant in Angus (P<0.05). Nellore had higher phosphorylation of myosin regulatory light chain-2, alpha actin-1, triosephosphate isomerase and 14-3-3 protein epsilon. However, Angus had greater phosphorylation of phosphoglucomutase-1 and troponin-T (P<0.05). Therefore, proteins involved in contraction and muscle organization, myofilaments expressed in fast or slow-twitch fibers and heat shock proteins localized in mitochondria or sarcoplasmic reticulum and involved in cell flux of calcium and apoptosis might be associated with differences in beef quality between Angus and Nellore. Furthermore, prohibitin appears to be a potential biomarker of intramuscular fat in cattle. Additionally, differences in phosphorylation of myofilaments and glycolytic enzymes could be involved with differences in muscle contraction force, susceptibility to calpain, apoptosis and postmortem glycolysis, which might also be related to differences in beef quality among Angus and Nellore.

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Section: Resultsmentioning

confidence: 99%

Differences in Beef Quality between Angus (Bos taurus taurus) and Nellore (Bos taurus indicus) Cattle through a Proteomic and Phosphoproteomic Approach

et al. 2017

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“…Another protein with changed expression, 75 kDa glucose-regulated protein ( GRP75 ), is a molecular chaperone localized preferentially (but not exclusively) in mitochondria. This chaperone interacts with many proteins, including NDUS3 mentioned above (29). In mitochondria, GRP75 helps to maintain mitochondrial shape and function (30, 31).…”

Section: Discussionmentioning

confidence: 99%

Markers of Acute Toxicity in Pancreatic Beta-Cells Exposed to Lethal Doses of the Organochlorine Pollutant DDT Determined by a Proteomic Approach

Pavlíková

Šrámek

Jelínek

et al. 2020

Preprint

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Many compounds have the potential to harm pancreatic beta-cells; organochlorine pollutants belong to those compounds. In this work, we aimed to find markers of acute toxicity of p,p‘-DDT among proteins expressed in human pancreatic beta-cells NES2Y and visible at 2-D electrophoresis. We exposed NES2Y cells to a lethal dose of p,p‘-DDT (150 μM) for 24 hours and 30 hours and determined changes in protein expression using 2-D electrophoresis. We also stained the cells exposed to p,p‘-DDT to visualize the altered phenotype of the exposed cells. Among proteins with changed expression, we identified proteins involved in ER stress (GRP78, and endoplasmin), mitochondrial proteins (GRP75, ECHM, IDH3A, NDUS1, and NDUS3), proteins with potential to change the cell morphology (EFHD2, TCPA, NDRG1, and ezrin), and some other proteins (HNRPF, HNRH1, K2C8, vimentin, PBDC1, EF2, PCNA, biliverdin reductase, G3BP1, FRIL, and HSP27). These proteins can be used as markers of acute DDT toxicity.

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“…A total of 119 proteins were identified, among which mortalin, and several subunits of Complex I are notable. Mortalin belongs to the heat shock protein 70 family and plays a role in the control of cell proliferation but can also act as a chaperone [141] and associate with the protein translocation system [142,143]. Protein quality control within the cell implies intervention of many molecular chaperones and proteases [144].…”

Section: Clinical Insights From Mitochondrial Proteomicsmentioning

confidence: 99%

Clinical implications from proteomic studies in neurodegenerative diseases: lessons from mitochondrial proteins

Butterfield

Palmieri

Castegna

2016

Expert Review of Proteomics

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Mitochondria play a key role in eukaryotic cells, being mediators of energy, biosynthetic and regulatory requirements of these cells. Emerging proteomics techniques have allowed scientists to obtain the differentially expressed proteome or the proteomic redox status in mitochondria. This has unmasked the diversity of proteins with respect to subcellular location, expression and interactions. Mitochondria have become a research ‘hot spot’ in subcellular proteomics, leading to identification of candidate clinical targets in neurodegenerative diseases in which mitochondria are known to play pathological roles. The extensive efforts to rapidly obtain differentially expressed proteomes and unravel the redox proteomic status in mitochondria have yielded clinical insights into the neuropathological mechanisms of disease, identification of disease early stage and evaluation of disease progression. Although current technical limitations hamper full exploitation of the mitochondrial proteome in neurosciences, future advances are predicted to provide identification of specific therapeutic targets for neurodegenerative disorders.

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Mortalin, Apoptosis, and Neurodegeneration

Cited by 64 publications

References 119 publications

Differences in Beef Quality between Angus (Bos taurus taurus) and Nellore (Bos taurus indicus) Cattle through a Proteomic and Phosphoproteomic Approach

Differences in Beef Quality between Angus (Bos taurus taurus) and Nellore (Bos taurus indicus) Cattle through a Proteomic and Phosphoproteomic Approach

Markers of Acute Toxicity in Pancreatic Beta-Cells Exposed to Lethal Doses of the Organochlorine Pollutant DDT Determined by a Proteomic Approach

Clinical implications from proteomic studies in neurodegenerative diseases: lessons from mitochondrial proteins

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