Characterization of the glycated human cerebrospinal fluid proteome

Ramírez-Boo, M.; Priego-Capote, Feliciano; Hainard, Alexandre; Gluck, Florent; Burkhard, Pierre; Sanchez, Jean‐Charles

doi:10.1016/j.jprot.2012.01.017

Cited by 18 publications

(13 citation statements)

References 72 publications

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“…Quantitative methods for the evaluation of glycation levels have been recently applied at the proteomic scale. In particular, a novel proteomic approach for qualitative and quantitative analysis of glycated proteins was developed; it simultaneously allows: (i) identification of glycated proteins; (ii) elucidation of sugar attachment sites; (iii) quantitative analysis to compare glycemic states (Priego‐Capote et al, ; Ramírez‐Boo et al, ) (Fig. ).…”

Section: Proteomic Analysis Of Protein Early and Intermediate Stage Gmentioning

confidence: 99%

“…A predictive approach was also tested to detect potential glycation sites under higher glucose concentrations. Very recently, this proteomic methods was also applied to the analysis of native glycated proteins in human cerebrospinal fluid, identifying 111 glycation sites in 48 glycated components (Ramírez‐Boo et al, ). In vitro labeling with high 13 C 6 ‐ D ‐glucose concentrations demonstrated 265 glycation sites and 101 glycated proteins as potentially modifiable under pathological conditions.…”

Section: Proteomic Analysis Of Protein Early and Intermediate Stage Gmentioning

confidence: 99%

“…Another important issue associated with shot‐gun applications regards the development of robust quantitative methods. Although preliminary approaches have been set up for the analysis of glycated proteomes (Priego‐Capote et al, ; Ramírez‐Boo et al, ), well‐consolidated quantitative technologies, such as SILAC, iTRAQ, or MRM, have to be fully adapted to the study of glycated and AGEs‐modified species. In this context, novel applications are expected in the next few years.…”

Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

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Non‐enzymatic glycation and glycoxidation protein products in foods and diseases: An interconnected, complex scenario fully open to innovative proteomic studies

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Salzano

Renzone

et al. 2013

Mass Spectrometry Reviews

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The Maillard reaction includes a complex network of processes affecting food and biopharmaceutical products; it also occurs in living organisms and has been strictly related to cell aging, to the pathogenesis of several (chronic) diseases, such as diabetes, uremia, cataract, liver cirrhosis and various neurodegenerative pathologies, as well as to peritoneal dialysis treatment. Dozens of compounds are involved in this process, among which a number of protein-adducted derivatives that have been simplistically defined as early, intermediate and advanced glycation end-products. In the last decade, various bottom-up proteomic approaches have been successfully used for the identification of glycation/glycoxidation protein targets as well as for the characterization of the corresponding adducts, including assignment of the modified amino acids. This article provides an updated overview of the mass spectrometry-based procedures developed to this purpose, emphasizing their partial limits with respect to current proteomic approaches for the analysis of other post-translational modifications. These limitations are mainly related to the concomitant sheer diversity, chemical complexity, and variable abundance of the various derivatives to be characterized. Some challenges to scientists are finally proposed for future proteomic investigations to solve main drawbacks in this research field.

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Section: Proteomic Analysis Of Protein Early and Intermediate Stage Gmentioning

confidence: 99%

Section: Proteomic Analysis Of Protein Early and Intermediate Stage Gmentioning

confidence: 99%

Section: Conclusion and Future Perspectivesmentioning

confidence: 99%

See 1 more Smart Citation

Non‐enzymatic glycation and glycoxidation protein products in foods and diseases: An interconnected, complex scenario fully open to innovative proteomic studies

Arena

Salzano

Renzone

et al. 2013

Mass Spectrometry Reviews

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“…N ‐glycosidase F pretreatment of CSF has allowed to selectively monitor 106 O‐glycopeptides by automated CID‐MS 2 /MS 3 . Moreover, 111 glycation sites corresponding to 48 glycated proteins were characterized in human CSF, using endoproteinase Glu‐C digestion and boronate affinity chromatography prior to MS phase . Recently, Guldbrandsen et al have performed the most extensive proteomic characterization of human CSF, identifying 3081 proteins (877 proteins also detected in human plasma), and 417 glycosylation sites corresponding to 520 glycoproteins .…”

Section: Proteomic Landscape Of Human Csfmentioning

confidence: 99%

Toward defining the anatomo‐proteomic puzzle of the human brain: An integrative analysis

Fernández‐Irigoyen

Labarga

Zabaleta

et al. 2015

Proteomics Clinical Apps

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The human brain is exceedingly complex, constituted by billions of neurons and trillions of synaptic connections that, in turn, define ∼900 neuroanatomical subdivisions in the adult brain (Hawrylycz et al. An anatomically comprehensive atlas of the human brain transcriptome. Nature 2012, 489, 391-399). The human brain transcriptome has revealed specific regional transcriptional signatures that are regulated in a spatiotemporal manner, increasing the complexity of the structural and molecular organization of this organ (Kang et al. Spatio-temporal transcriptome of the human brain. Nature 2011, 478, 483-489). During the last decade, neuroproteomics has emerged as a powerful approach to profile neural proteomes using shotgun-based MS, providing complementary information about protein content and function at a global level. Here, we revise recent proteome profiling studies performed in human brain, with special emphasis on proteome mapping of anatomical macrostructures, specific subcellular compartments, and cerebrospinal fluid. Moreover, we have performed an integrative functional analysis of the protein compilation derived from these large-scale human brain proteomic studies in order to obtain a comprehensive view of human brain biology. Finally, we also discuss the potential contribution of our meta-analysis to the Chromosome-centric Human Proteome Project initiative.

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“…Proteins such as β‐amyloid, tau, prions, and transthyretin involved in neurodegenerative diseases are found to be glycated in patients with AD and PD. Glycated human cerebrospinal fluid (CSF) proteins are also shown to be involved in neuro‐inflammation and neurodegenerative diseases . AD is one of the most prevalent neurodegenerative diseases with known symptoms of memory loss, along with severe confusion and disordered thinking .…”

Section: Diabetesmentioning

confidence: 99%

Glycated proteome: From reaction to intervention

Kulkarni

Korwar

Mary

et al. 2013

Proteomics Clinical Apps

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Glycation, a nonenzymatic reaction between reducing sugars and proteins, is a proteome wide phenomenon, predominantly observed in diabetes due to hyperglycemia. Glycated proteome of plasma, kidney, lens, and brain are implicated in the pathogenesis of various diseases, including diabetic complications, neurodegenerative diseases, cancer, and aging. This review discusses the strategies to characterize protein glycation, its functional implications in different diseases, and intervention strategies to protect the deleterious effects of protein glycation.

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Characterization of the glycated human cerebrospinal fluid proteome

Cited by 18 publications

References 72 publications

Non‐enzymatic glycation and glycoxidation protein products in foods and diseases: An interconnected, complex scenario fully open to innovative proteomic studies

Non‐enzymatic glycation and glycoxidation protein products in foods and diseases: An interconnected, complex scenario fully open to innovative proteomic studies

Toward defining the anatomo‐proteomic puzzle of the human brain: An integrative analysis

Glycated proteome: From reaction to intervention

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