Proteomic analysis of mitochondrial proteins in the guinea pig heart following long-term normobaric hyperoxia

Lichardusová, Lucia; Tatarková, Zuzana; Čalkovská, Andrea; Mokrá, Daniela; Engler, Ivan; Račay, Peter; Lehotský, Ján; Kaplán, Peter

doi:10.1007/s11010-017-3037-6

Cited by 4 publications

(3 citation statements)

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“…Pyruvate phosphate dikinase is the key enzyme in cellular energy metabolism; it catalyzes the ATP-and phosphate (P i )-dependent conversion of pyruvate to phosphoenol pyruvate in C4 plants (Ciupka and Gohlke., 2017). Aconitate hydratase catalyzes the conversion of citrate to cis-aconitate (Lichardusova et al, 2017). Isocitrate dehydrogenase catalyzes oxidative decarboxylation of isocitrate (Mhamdi and Noctor, 2015).…”

Section: Discussionmentioning

confidence: 99%

Peer Review #1 of "Comparative transcriptome analysis of differentially expressed genes related to the physiological changes of yellow-green leaf mutant of maize (v0.2)"

2021

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Chlorophylls, green pigments in chloroplasts, are essential for photosynthesis. Reduction in chlorophyll content may result in retarded growth, dwarfism, and sterility. In this study, a yellow-green leaf mutant of maize, indicative of abnormity in chlorophyll content, was identified. The physiological parameters of this mutant were measured. Next, global gene expression of this mutant was determined using transcriptome analysis and compared to that of wild-type maize plants. The yellow-green leaf mutant of maize was found to contain lower contents of chlorophyll a, chlorophyll b and carotenoid compounds. It contained fewer active PSII centers and displayed lower values of original chlorophyll fluorescence parameters than the wild-type plants. The real-time fluorescence yield, the electron transport rate, and the net photosynthetic rate of the mutant plants showed reduction as well. In contrast, the maximum photochemical quantum yield of PSII of the mutant plants was similar to that of the wild-type plants. Comparative transcriptomic analysis of the mutant plants and wild-type plants led to the identification of differentially expressed 1122 genes, of which 536 genes were up-regulated and 586 genes down-regulated in the mutant. Five genes in chlorophyll metabolism pathway, nine genes in the tricarboxylic acid cycle and seven genes related to the conversion of sucrose to starch displayed downregulated expression. In contrast, genes encoding a photosystem II reaction center PsbP family protein and the PGR5-like protein 1A (PGRL1A) exhibited increased transcript abundance.

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Section: Discussionmentioning

confidence: 99%

Peer Review #1 of "Comparative transcriptome analysis of differentially expressed genes related to the physiological changes of yellow-green leaf mutant of maize (v0.2)"

2021

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“…Pyruvate phosphate dikinase is the key enzyme in cellular energy metabolism; it catalyzes the ATP-and phosphate (P i )-dependent conversion of pyruvate to phosphoenol pyruvate in C4 plants [27]. Aconitate hydratase catalyzes the conversion of citrate to cis-aconitate [28]. Isocitrate dehydrogenase catalyzes oxidative decarboxylation of isocitrate [29].…”

Section: Discussionmentioning

confidence: 99%

Physiological and transcriptomic characterization of a yellow-green leaf mutant of maize

Li¹,

Yang²,

Lu³

et al. 2020

Preprint

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Background Chlorophylls, green pigments in chloroplasts, are essential for photosynthesis. Reduction in chlorophyll contents may result in retarded growth, dwarfism, and sterility. In this study, a yellow-green leaf mutant of maize, indicative of abnormity in chlorophyll contents, was identified. The physiological parameters of this mutant were measured. Next, global gene expression of this mutant was determined using transcriptome analysis and compared to that of wild-type maize plants. Results The yellow-green leaf mutant of maize was found to contain lower contents of chlorophyll a , chlorophyll b and carotenoid compounds. It contained fewer active PSII centers and displayed lower values of original chlorophyll fluorescence parameters than the wild-type plants. The real-time fluorescence yield, the electron transport rate, and the net photosynthetic rate of the mutant plants showed reduction as well. In contrast, the maximum photochemical quantum yield of PSII of the mutant plants was similar to that of the wild-type plants. Comparative transcriptomic analysis of the mutant plants and wild-type plants led to the identification of differentially expressed1122 genes, of which 536 genes were up-regulated and 586 genes down-regulated in the mutant. Five genes in chlorophyll metabolism pathway, nine genes in the tricarboxylic acid cycle and seven genes related to the conversion of sucrose to starch displayed down-regulated expression. In contrast, genes encoding a photosystem II reaction center PsbP family protein and the PGR5-like protein 1A (PGRL1A) exhibited increased transcript abundance. Conclusions The yellow-green leaf mutant of maize contained fewer active PSII centers with lowered net photosynthesis rate, but have the similar value of the maximum photochemical quantum yield of PSII with that of the wild-type plants. Analysis of differentially expressed genes through transcriptome analysis revealed the down-regulated genes which may be responsible for chlorophyll deduction and changes of photosynthetic characteristics. The up-regulated genes would be helpful to maintain the active PSII centers of the yellow-green leaf mutant.

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“…The cardiac mitochondrial proteome has been widely explored in models of I/R [ 144 – 147 ]. Most of these studies have also relied on redox approaches (see Redox Mitoproteomics Section in this review), since mitochondrial RNOS generation has been described as a double-edged sword contributing to myocardial infarction and stroke as well as ischemic preconditioning [ 148 ].…”

Section: Addressing Mitochondrial Dysfunction Through High-throughmentioning

confidence: 99%

Mitoproteomics: Tackling Mitochondrial Dysfunction in Human Disease

Gómez-Serrano

Camafeita

Loureiro

et al. 2018

Oxidative Medicine and Cellular Longevity

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Mitochondria are highly dynamic and regulated organelles that historically have been defined based on their crucial role in cell metabolism. However, they are implicated in a variety of other important functions, making mitochondrial dysfunction an important axis in several pathological contexts. Despite that conventional biochemical and molecular biology approaches have provided significant insight into mitochondrial functionality, innovative techniques that provide a global view of the mitochondrion are still necessary. Proteomics fulfils this need by enabling accurate, systems-wide quantitative analysis of protein abundance. More importantly, redox proteomics approaches offer unique opportunities to tackle oxidative stress, a phenomenon that is intimately linked to aging, cardiovascular disease, and cancer. In addition, cutting-edge proteomics approaches reveal how proteins exert their functions in complex interaction networks where even subtle alterations stemming from early pathological states can be monitored. Here, we describe the proteomics approaches that will help to deepen the role of mitochondria in health and disease by assessing not only changes to mitochondrial protein composition but also alterations to their redox state and how protein interaction networks regulate mitochondrial function and dynamics. This review is aimed at showing the reader how the application of proteomics approaches during the last 20 years has revealed crucial mitochondrial roles in the context of aging, neurodegenerative disorders, metabolic disease, and cancer.

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Proteomic analysis of mitochondrial proteins in the guinea pig heart following long-term normobaric hyperoxia

Cited by 4 publications

References 50 publications

Peer Review #1 of "Comparative transcriptome analysis of differentially expressed genes related to the physiological changes of yellow-green leaf mutant of maize (v0.2)"

Peer Review #1 of "Comparative transcriptome analysis of differentially expressed genes related to the physiological changes of yellow-green leaf mutant of maize (v0.2)"

Physiological and transcriptomic characterization of a yellow-green leaf mutant of maize

Mitoproteomics: Tackling Mitochondrial Dysfunction in Human Disease

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