Age‐related proteome analysis of the mouse brain: a 2‐DE study

Carrette, Odile; Burkhard, Pierre; Hochstrasser, Denis F.; Sanchez, Jean‐Charles

doi:10.1002/pmic.200600084

Cited by 21 publications

(19 citation statements)

References 42 publications

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“…For example, only 40 µg of brain segment/injection was used in the study, while hundreds of micrograms of brain segment was required in general brain proteome analysis using 2-DE methods. [26][27][28][29][30] The existence of 28 regionally-specific age-related proteins in mouse brain was demonstrated in this study, seven of which have been reported for the first time. Figure 2 presents a comparison of the peak heights of each of the age-related altered proteins among three aging stages (4, 12 and 20 weeks) in Ctx.…”

Section: )mentioning

confidence: 86%

FD-LC-MS/MS Method for Determining Protein Expression and Elucidating Biochemical Events in Tissues and Cells

Ichibangase

Imai

2012

Biological & Pharmaceutical Bulletin

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To study biochemical events in tissues and cells, we have developed a novel proteomics approach, FD-LC-MS/MS, which consists of fluorogenic derivatization (FD), LC separation and detection/quantification of proteins in a biological sample, followed by the isolation and tryptic digestion of target proteins, and then their identification using nano-HPLC-MS/MS. Fluorogenic reagents such as 7-chloro-N-[2-(dimethylamino)ethyl]-2,1,3-benzoxadiazole-4-sulphonamide (DAABD-Cl) were designed to have high sensitivity for HPLC-fluorescence and -MS/MS detection and reactivity for cysteine residues in proteins. This comprehensive differential proteomics approach was applied to several tissues, such as mouse liver, mouse brain, horse muscle, breast cancer cell lines, and mouse heart, in order to study fluctuations in protein levels in tissues and cells.

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Section: )mentioning

confidence: 86%

FD-LC-MS/MS Method for Determining Protein Expression and Elucidating Biochemical Events in Tissues and Cells

Ichibangase

Imai

2012

Biological & Pharmaceutical Bulletin

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“…There have also been other similar HUPO BPP programs [8][9][10][11]. These studies have identified a total of 1,999 spots matched between all gels, among which 206 spots were differentially expressed between the different stages: 122 spots were highest in intensity in embryonic stage E16, 26 were highest in the juvenile group (P7) and 58 spots were highest in the adult stage (P56), revealing a pattern of temporal expression for the examined proteins [107].…”

Section: Current Status Of the Hupo Bpp Activitymentioning

confidence: 97%

“…It is clear that the variability in sample processing, experimental design and data analysis methods results in a limited cross-validation between studies performed in different laboratories, as pointed out by Carrette [8]. Upon the request of the HUman Proteome Organization (HUPO) Brain Proteome Project (BPP) executive committee, Carrette et al identified ten mouse brain proteins: dihydropyrimidinase-related proteins, brain FABP, stathmin, isocitrate dehydrogenase, gamma enolase, annexin V, glutamine synthetase, creatine kinase B chain, triosephosphate dehydrogenase, and malate dehydrogenase [8], most of them functioned in the metabolism of the brain.…”

Section: Proteomic Studies On the Prenatal And Postnatal Stages Of Brmentioning

confidence: 97%

“…Upon the request of the HUman Proteome Organization (HUPO) Brain Proteome Project (BPP) executive committee, Carrette et al identified ten mouse brain proteins: dihydropyrimidinase-related proteins, brain FABP, stathmin, isocitrate dehydrogenase, gamma enolase, annexin V, glutamine synthetase, creatine kinase B chain, triosephosphate dehydrogenase, and malate dehydrogenase [8], most of them functioned in the metabolism of the brain.…”

Section: Proteomic Studies On the Prenatal And Postnatal Stages Of Brmentioning

confidence: 99%

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Proteomic Studies on the Development of the Central Nervous System and Beyond

Zhang

2010

Neurochem Res

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Neuroproteomics has become a 'symbol' or even a 'sign' for neuroscientists in the post-genomic era. During the last several decades, a number of proteomic approaches have been used widely to decipher the complexity of the brain, including the study of embryonic stages of human or non-human animal brain development. The use of proteomic techniques has allowed for great scientific advancements, including the quantitative analysis of proteomic data using 2D-DIGE, ICAT and iTRAQ. In addition, proteomic studies of the brain have expanded into fields such as subproteomics, synaptoproteomics, neural plasma membrane proteomics and even mitochondrial proteomics. The rapid progress that has been made in this field will not only increase the knowledge based on the neuroproteomics of the developing brain but also help to increase the understanding of human neurological diseases. This paper will focus on proteomic studies in the central nervous system and especially those conducted on the development of the brain in order to summarize the advances in this rapidly developing field.

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“…treated OA), a class for each group was created using the software. Inter-class data analysis was based on the normalized volume (%vol) to correct for any difference in loading and/or staining [20]. For inter-class differential analysis of healthy (n = 2) vs. treated OA (n = 3) and healthy (n = 2) vs. untreated OA (n = 3), the overlap ratio of the %vol of healthy/untreated OA and healthy/treated OA was calculated for each match.…”

Section: Image Analysismentioning

confidence: 99%

Micro‐high‐performance liquid chromatography platform for the depletion of high‐abundance proteins and subsequent on‐line concentration/capturing of medium and low‐abundance proteins from serum. Application to profiling of protein expression in healthy and osteoarthritis sera by 2‐D gel electrophoresis

Jmeian

Rassi

2008

Electrophoresis

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In this investigation, an integrated microcolumn-based fluidic platform for the simultaneous depletion of high-abundance proteins and the subsequent on-line concentration/capturing of medium- and low-abundance proteins from human serum has been introduced. The platform consists of on-line coupling of tandem affinity micorcolumns to an RP microcolumn to achieve first the depletion of high-abundance proteins by the tandem affinity microcolumns followed by the concentration and capturing of medium- and low-abundance proteins by the RP microcolumn. The tandem affinity microcolumns are based on macroporous monoliths characterized by their relatively high permeability in pressure-driven flow while the RP microcolumn is packed with polymeric particles with an average particle diameter of 20 microm giving rise to a very little back pressure, thus allowing fast flow velocity across the coupled columns format and consequently short processing time of serum samples prior to analysis by 2-DE. The microcolumn-based fluidic platform was applied to serum samples from osteoarthritis (OA) donors before and after soy protein (SP) supplementation, and from healthy donors, and the resulting depleted serum samples from high-abundance proteins were profiled for protein expression by 2-DE. In general, the protein expression was lower in serum of the same OA patient after soy treatment than before soy treatment. Several proteins were down-regulated after soy treatment with transthyretin being the most affected by the SP supplementation. In addition, with respect to serum from healthy donors, the sera from OA patients showed difference in proteins expression.

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Age‐related proteome analysis of the mouse brain: a 2‐DE study

Cited by 21 publications

References 42 publications

FD-LC-MS/MS Method for Determining Protein Expression and Elucidating Biochemical Events in Tissues and Cells

FD-LC-MS/MS Method for Determining Protein Expression and Elucidating Biochemical Events in Tissues and Cells

Proteomic Studies on the Development of the Central Nervous System and Beyond

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