Gel‐Based Proteomics

Righetti, Pier Giorgio; Antonioli, Paolo; Simó, Carolina; Citterio, Attilio

doi:10.1002/9780470369630.ch2

Cited by 6 publications

(10 citation statements)

References 52 publications

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“…7). For more details on solubilization of proteins before 2-DGE see the following reviews or book chapters (Rabilloud & Chevallet, 2000;Agrawal et al, 2005a;Righetti et al, 2008). However, membrane and hydrophobic proteins present problems for standard 2-DGE protocols and require different extraction procedures including the use of different detergents or organic solvents (Santoni et al, 1999b;Seigneurin-Berny et al, 1999;Santoni et al, 2000;Ferro et al, 2002;Luche, Santoni, & Rabilloud, 2003;Rolland et al, 2006;D'Andréa et al, 2007b;Rabilloud et al, 2008).…”

Section: Sample Preparationmentioning

confidence: 99%

“…The ability to display the soluble protein content of a sample as a fingerprint based on just two simple properties-apparent molecular weight and isoelectric point (pI) made this a method of choice to study the dynamics of proteomes (Görg, Weiss, & Dunn, 2004;Righetti et al, 2008;Klose, 2009) (Fig. 7).…”

Section: Two-and One-dimensional Gel Electrophoresis (2-and 1-dge)mentioning

confidence: 99%

“…Proteomics, being the study of global protein composition of an organism, cell or organelle, was first attempted over 30 years ago with the development of multidimensional separation of proteins based on the initial use of a basic proteomics tools, namely twodimensional gel electrophoresis (2-DGE), in both plant and animal systems (Klose, 1975;Scheele, 1975;Cremer & Van de Walle, 1985;Görg, 1991;Herbert et al, 2001;Righetti, Stoyanov, & Zhukov, 2001;Görg, Weiss, & Dunn, 2004). However, it should be remembered that 2-DGE has a dynamic history that can be traced back to the use of pH gradient in protein separation [the isoelectric focusing (IEF) phenomenon], which was the basis for the gel-based proteomics of today (Tiselius, 1937;Kolin, 1954;Svensson, 1961;Ornstein, 1964;Vesterberg, 1969;O'Farrell, 1975;Righetti et al, 2008). Since then, 2-DGE and its complementary arm, mass spectrometry (MS; Karas & Hillenkamp, 1988;Fenn et al, 1989;Bauer, 2001;Bergmuller, Baginsky, & Gruissem, 2008;Feng et al, 2008) have revolutionized the way we find, identify and look at proteins on a global scale today.…”

Section: Introductionmentioning

confidence: 98%

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Plant organelle proteomics: Collaborating for optimal cell function

Agrawal¹,

Bourguignon

Rolland

et al. 2010

Mass Spectrometry Reviews

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Organelle proteomics describes the study of proteins present in organelle at a particular instance during the whole period of their life cycle in a cell. Organelles are specialized membrane bound structures within a cell that function by interacting with cytosolic and luminal soluble proteins making the protein composition of each organelle dynamic. Depending on organism, the total number of organelles within a cell varies, indicating their evolution with respect to protein number and function. For example, one of the striking differences between plant and animal cells is the plastids in plants. Organelles have their own proteins, and few organelles like mitochondria and chloroplast have their own genome to synthesize proteins for specific function and also require nuclear-encoded proteins. Enormous work has been performed on animal organelle proteomics. However, plant organelle proteomics has seen limited work mainly due to: (i) inter-plant and inter-tissue complexity, (ii) difficulties in isolation of subcellular compartments, and (iii) their enrichment and purity. Despite these concerns, the field of organelle proteomics is growing in plants, such as Arabidopsis, rice and maize. The available data are beginning to help better understand organelles and their distinct and/or overlapping functions in different plant tissues, organs or cell types, and more importantly, how protein components of organelles behave during development and with surrounding environments. Studies on organelles have provided a few good reviews, but none of them are comprehensive. Here, we present a comprehensive review on plant organelle proteomics starting from the significance of organelle in cells, to organelle isolation, to protein identification and to biology and beyond. To put together such a systematic, in-depth review and to translate acquired knowledge in a proper and adequate form, we join minds to provide discussion and viewpoints on the collaborative nature of organelles in cell, their proper function and evolution.

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Section: Sample Preparationmentioning

confidence: 99%

Section: Two-and One-dimensional Gel Electrophoresis (2-and 1-dge)mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

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Plant organelle proteomics: Collaborating for optimal cell function

Agrawal¹,

Bourguignon

Rolland

et al. 2010

Mass Spectrometry Reviews

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“…In 2015, it will be 40 years since the advent of proteomics, revolutionized via the introduction of two‐dimensional gel electrophoresis (2‐DGE) (Klose, ; O'Farrell, ; Scheele, ) and later refined with the introduction of immobilized pH gradients (IPGs) (Bjellqvist et al, ; Righetti et al, ; Gianazza & Righetti, ; Görg et al, ) and MS (Aebersold & Mann, ; Yates, Ruse, & Nakorchevsky, ). Forty years can be considered a long time, but the fact is that the study of proteins within the term proteomics (Wilkins et al, ) is quite young, fluid, and diversifying as a technology.…”

Section: Plant Proteomics and Mass Spectrometry: A Decadementioning

confidence: 99%

A decade of plant proteomics and mass spectrometry: Translation of technical advancements to food security and safety issues

Agrawal¹,

Sarkar

Righetti

et al. 2013

Mass Spectrometry Reviews

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Agrawal, G.K. et al. (2013). A decade of plant proteomics and mass spectrometry: Translation of technical advancements to food security and safety issues. AbstractTremendous progress in plant proteomics driven by mass spectrometry (MS) techniques has been made since 2000 when few proteomics reports were published and plant proteomics was in its infancy. These achievements include the refinement of existing techniques and the search for new techniques to address food security, safety, and health issues. It is projected that in 2050, the world's population will reach 9-12 billion people demanding a food production increase of 34-70% (FAO, 2009) from today's food production. Provision of food in a sustainable and environmentally committed manner for such a demand without threatening natural resources, requires that agricultural production increases significantly and that postharvest handling and food manufacturing systems become more efficient requiring lower energy expenditure, a decrease in postharvest losses, less waste generation and food with longer shelf life. There is also a need to look for alternative protein sources to animal based (i.e., plant based) to be able to fulfill the increase in protein demands by 2050. Thus, plant biology has a critical role to play as a science capable of addressing such challenges. In this review, we discuss proteomics especially MS, as a platform, being utilized in plant biology research for the past 10 years having the potential to expedite the process of understanding plant biology for human benefits. The increasing application of proteomics technologies in food security, analysis, and safety is emphasized in this review. But, we are aware that no unique approach/technology is capable to address the global food issues. Proteomics-generated information/resources must be integrated and correlated with other omics-based approaches, information, and conventional programs to ensure sufficient food and resources for human development now and in the future

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“…Redox proteomics approaches for high-throughput 3NT detection were initiated through gel electrophoresisbased measurements (Righetti et al 2008 ). Figure 3 gives an overview of the gel-based approach.…”

Section: Quantitative Proteomics Antibodies and Gel Electrophoresis-bmentioning

confidence: 99%

Proteomics quantification of protein nitration

Robinson

2013

Reviews in Analytical Chemistry

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Protein tyrosine nitration is a post-translational modification (PTM) that can occur in biological systems under conditions of oxidative stress. This PTM can impact protein structure and function and has been linked to diseases such as Alzheimer ' s disease, cardiomyopathy, and arthritis. In order to understand the role that 3-nitrotyrosine (3NT) plays in disease states, a better understanding at the macromolecular level is necessary. Proteomics is a powerful approach that can simultaneously measure hundreds to thousands of proteins in normal or diseased states and thus can be helpful in the analysis of 3NT-modified proteins. Recently, some attention has been focused on the development of proteomic workflows that provide enrichment, characterization, and relative quantification of 3NT-modified proteins. These approaches rely on gel electrophoresis, liquid chromatography, and mass spectrometry (MS) techniques. This review provides an overview of current proteomics approaches for 3NT-modified proteins and highlights current MS-based methods for quantification of this PTM.

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Gel‐Based Proteomics

Cited by 6 publications

References 52 publications

Plant organelle proteomics: Collaborating for optimal cell function

Plant organelle proteomics: Collaborating for optimal cell function

A decade of plant proteomics and mass spectrometry: Translation of technical advancements to food security and safety issues

Proteomics quantification of protein nitration

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