Precipitation by lanthanum ions: A straightforward approach to isolating phosphoproteins

Pink, Mario; Verma, Nisha; Polato, F.; Bonn, Günther K.; Baba, Hideo A.; Rettenmeier, Albert W.; Schmitz‐Spanke, Simone

doi:10.1016/j.jprot.2011.08.001

Cited by 20 publications

(22 citation statements)

References 34 publications

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“…In another study, precipitation of phosphoproteins by lanthanum ions was found to be compatible with gel electrophoresis in combination with MALDI-TOF MS for the identification of phosphoproteins from human liver tissue and pig urothelial cells [67][68][69]. In 2012, Güzel et al introduced trivalent europium, terbium and erbium cations for the co-precipitation of phosphorylated proteins in the presence of phosphate ions [70].…”

Section: Selective Precipitation Of Phosphoproteins By Trivalent Lantmentioning

confidence: 99%

Enrichment of Phosphorylated Peptides and Proteins by Selective Precipitation Methods

Rainer

Bonn

2015

Bioanalysis

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Protein phosphorylation is one of the most prominent post-translational modifications involved in the regulation of cellular processes. Fundamental understanding of biological processes requires appropriate bioanalytical methods for selectively enriching phosphorylated peptides and proteins. Most of the commonly applied enrichment approaches include chromatographic materials including Fe(3+)-immobilized metal-ion affinity chromatography or metal oxides. In the last years, the introduction of several non-chromatographic isolation technologies has increasingly attracted the interest of many scientists. Such approaches are based on the selective precipitation of phosphorylated peptides and proteins by applying various metal cations. The excellent performance of precipitation-based enrichment methods can be explained by the absence of any stationary phase, resin or sorbent, which usually leads to unspecific binding. This review provides an overview of recently published methods for the selective precipitation of phosphorylated peptides and proteins.

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Section: Selective Precipitation Of Phosphoproteins By Trivalent Lantmentioning

confidence: 99%

Enrichment of Phosphorylated Peptides and Proteins by Selective Precipitation Methods

Rainer

Bonn

2015

Bioanalysis

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“…Phosphorylation is a PTM that is particularly challenging, as it is present in lowstoichiometry amounts in samples, therefore enrichment techniques are usually required prior to mass spectrometry analysis, as reviewed by Leitner et al (2011). Presently, there are several techniques effective and available for this purpose, namely IMAC, titanium dioxide, among others, and recently a highly efficient new enrichment technique using lathanum ions for the precipitation of this type of modified peptides was developed (Pink et al, 2011). The advantage of the lanthanum enrichment is that it is based on a single step precipitation and phosphoproteins can be isolated from frozen tissue or cells, after cell lysis, using several buffer systems compatible with tandem mass spectrometry analysis.…”

Section: Post-translational Modifications Of Proteins and Peptides Comentioning

confidence: 99%

Tandem Mass Spectrometry of Peptides

Soares¹,

Pires²,

Almeida³

et al. 2012

Tandem Mass Spectrometry - Applications and Principles

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“…Methods for the enrichment of phosphoproteins by precipitation using calcium and barium phosphate have recently been published [34][35][36]. We have suggested the precipitation by lanthanum ions (La 31 ) for enrichment prior to 2-DE separation and MS identification of the phosphorylated proteins [37]. Lanthanum belongs to the group of the rare earth elements.…”

Section: Phosphoproteome Profiling Of Pubecmentioning

confidence: 99%

Proteome and phosphoproteome of primary cultured pig urothelial cells

et al. 2011

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Epithelial tissue lining the inner side of the urinary bladder is the most common target for bladder cancer-related diseases. Bladders of freshly slaughtered pigs were utilised for a comprehensive analysis of the proteome and phosphoproteome of bladder epithelial cells. Following protein separation by 2-D gel electrophoresis and identification by matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry (MALDI-TOF-MS) the first proteome and phosphoproteome maps of pig urinary bladder epithelial cells (PUBEC) were established. A total of 120 selected protein spots were identified. By using the La(3+) enrichment method further developed in our laboratory we identified 31 phosphoproteins with minimal contamination by non-phosphopeptides. The 2-DE map of pig urothelial cells may prove as a useful tool for studies on uroepithelial biology, and the analysed phosphoproteins expression pattern, together with the whole cell proteome, will be helpful for identifying the proteins involved in bladder-related diseases.

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Precipitation by lanthanum ions: A straightforward approach to isolating phosphoproteins

Cited by 20 publications

References 34 publications

Enrichment of Phosphorylated Peptides and Proteins by Selective Precipitation Methods

Enrichment of Phosphorylated Peptides and Proteins by Selective Precipitation Methods

Tandem Mass Spectrometry of Peptides

Proteome and phosphoproteome of primary cultured pig urothelial cells

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