Evaluation of protein kinase activities of cell lysates using peptide microarrays based on surface plasmon resonance imaging

Mori, Takeshi; Inamori, Kazuki; Inoue, Yusuke; Han, Xiaoming; Yamanouchi, Go; Niidome, Takuro; Katayama, Yoshiki

doi:10.1016/j.ab.2007.12.011

Cited by 45 publications

(23 citation statements)

References 42 publications

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“…)-biotin aminoethylcarbamoyl) pyridine-2-ylmethyl)-N,N 0 ,N 0 -tris(pyridine-2-ylmethyl)-1,3-diaminopropan-2-ol (Phos-tag biotin, see Fig. 4e) [34][35][36][37]40].…”

Section: Assays and Detectionmentioning

confidence: 99%

“…An aldehyde function at the surface of glass slides in combination with amino-oxy-acetyl moieties in the peptides [15,[26][27][28][29][30] or cysteinyl-residues [26,[31][32][33][34] was used for the preparation of peptide microarrays on glass slides. The reaction between cysteine residues and surface-bound maleimide groups was used for preparation of peptide microarrays for kinase [35][36][37][38][39][40] and protease profiling [41]. It could be demonstrated that native chemical ligation, introduced by Dawson et al [42] is wellsuited for effective attachment of kinase substrate peptides containing an N-terminal cysteine residue to thioester modified glass slides [43][44][45].…”

Section: Chemistry Of Peptide Array Preparationmentioning

confidence: 99%

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Deciphering Enzyme Function Using Peptide Arrays

2011

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Enzymes are key molecules in signal-transduction pathways. However, only a small fraction of more than 500 human kinases, 300 human proteases and 200 human phosphatases is characterised so far. Peptide microarray based technologies for extremely efficient profiling of enzyme substrate specificity emerged in the last years. This technology reduces set-up time for HTS assays and allows the identification of downstream targets. Moreover, peptide microarrays enable optimisation of enzyme substrates. Focus of this review is on assay principles for measuring activities of kinases, phosphatases or proteases and on substrate identification/optimisation for kinases. Additionally, several examples for reliable identification of substrates for lysine methyl-transferases, histone deacetylases and SUMO-transferases are given. Finally, use of high-density peptide microarrays for the simultaneous profiling of kinase activities in complex biological samples like cell lysates or lysates of complete organisms is described. All published examples of peptide arrays used for enzyme profiling are summarised comprehensively.

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“…)-biotin aminoethylcarbamoyl) pyridine-2-ylmethyl)-N,N 0 ,N 0 -tris(pyridine-2-ylmethyl)-1,3-diaminopropan-2-ol (Phos-tag biotin, see Fig. 4e) [34][35][36][37]40].…”

Section: Assays and Detectionmentioning

confidence: 99%

Section: Chemistry Of Peptide Array Preparationmentioning

confidence: 99%

Deciphering Enzyme Function Using Peptide Arrays

2011

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“…NOTE: Although desirable, highly pure protein preparations are not a must. SPR has been successfully used with less-than-perfect purifications and even with total extract 8,9 . 2.…”

Section: Protein Sample and Buffer Preparationmentioning

confidence: 99%

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)

Levanon

Vigonsky

Lewinson

2014

JoVE

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Protein-protein interactions are pivotal to most, if not all, physiological processes, and understanding the nature of such interactions is a central step in biological research. Surface Plasmon Resonance (SPR) is a sensitive detection technique for label-free study of bio-molecular interactions in real time. In a typical SPR experiment, one component (usually a protein, termed 'ligand') is immobilized onto a sensor chip surface, while the other (the 'analyte') is free in solution and is injected over the surface. Association and dissociation of the analyte from the ligand are measured and plotted in real time on a graph called a sensogram, from which pre-equilibrium and equilibrium data is derived. Being label-free, consuming low amounts of material, and providing pre-equilibrium kinetic data, often makes SPR the method of choice when studying dynamics of protein interactions. However, one has to keep in mind that due to the method's high sensitivity, the data obtained needs to be carefully analyzed, and supported by other biochemical methods.SPR is particularly suitable for studying membrane proteins since it consumes small amounts of purified material, and is compatible with lipids and detergents. This protocol describes an SPR experiment characterizing the kinetic properties of the interaction between a membrane protein (an ABC transporter) and a soluble protein (the transporter's cognate substrate binding protein). Video LinkThe video component of this article can be found at

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“…6 Recently, peptide microarrays have been extensively used for the analysis of intracellular PKs, which are enzymes used to catalyze the phosphorylation of amino acid residues (Ser, Thr, and Tyr) of specific proteins to regulate their activity to control intracellular signal transduction processes. 7,8 The analysis of intracellular PKs is an attractive application of peptide microarrays because it enables cell-based drug discovery, 5 the biochemical study to elucidate signal transduction pathways, 9,10 and diagnosis using tissue lysates. 11 Radioisotope (RI)-labeled [ 32/33 P] γ-ATP was previously used as a substrate for the detection of phosphorylation by kinase.…”

Section: Introductionmentioning

confidence: 99%

Optimization of Peptide Density on Microarray Surface for Quantitative Phosphoproteomics

et al. 2011

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Procedures to determine the density of peptides immobilized on a glass surface for the quantitative detection of phosphorylated peptides for phosphoproteomic applications of peptide microarrays are described. Two kinds of representative fluorescent probe molecules, anti-phosphotyrosine antibody (AB) and phos-tag (PT), were examined to compare their ability for the quantitative detection of phosphorylated peptides. PT is a metal complex with a binding specificity to phosphorylated amino acids, and is much smaller in size than AB. Thus, PT is quantitatively bound to the phosphorylated peptides, even at a high immobilization density without steric hindrance, making them highly suited for future microarrays requiring smaller sized peptide spots for much higher throughput.

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Evaluation of protein kinase activities of cell lysates using peptide microarrays based on surface plasmon resonance imaging

Cited by 45 publications

References 42 publications

Deciphering Enzyme Function Using Peptide Arrays

Deciphering Enzyme Function Using Peptide Arrays

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance (SPR)

Optimization of Peptide Density on Microarray Surface for Quantitative Phosphoproteomics

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