Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

ICP-MS-based multiplex profiling of glycoproteins using lectins conjugated to lanthanide-chelating polymers.

ABSTRACT: Lectins have been increasingly important in the study of glycoproteins. Here, we report a glycoprofiling method based on the covalent attachment of metal-chelating polymers to lectins for use in an ICP-MS-based assay. The labeled lectins are able to distinguish between glycoproteins covalently attached to a microtiter plate and their binding can be directly quantified by ICP-MS. Since each conjugate contains a different lanthanide, the assays can be conducted in a single or multiplex fashion, and may be readily elaborated to many different assay formats.

SUBMITTER: Leipold MD

PROVIDER: S-EPMC2646003 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature

ACCESS DATA

Json Xml

Publications

ICP-MS-based multiplex profiling of glycoproteins using lectins conjugated to lanthanide-chelating polymers.

Leipold Michael D MD Herrera Isaac I Ornatsky Olga O Baranov Vladimir V Nitz Mark M

Journal of proteome research 20090201 2

Lectins have been increasingly important in the study of glycoproteins. Here, we report a glycoprofiling method based on the covalent attachment of metal-chelating polymers to lectins for use in an ICP-MS-based assay. The labeled lectins are able to distinguish between glycoproteins covalently attached to a microtiter plate and their binding can be directly quantified by ICP-MS. Since each conjugate contains a different lanthanide, the assays can be conducted in a single or multiplex fashion, an ...[more]

PMID: 19072657

Similar Datasets

ICP-MS analysis of lanthanide-doped nanoparticles as a non-radiative, multiplex approach to quantify biodistribution and blood clearance.

Project description:Recent advances in material science and chemistry have led to the development of nanoparticles with diverse physicochemical properties, e.g. size, charge, shape, and surface chemistry. Evaluating which physicochemical properties are best for imaging and therapeutic studies is challenging not only because of the multitude of samples to evaluate, but also because of the large experimental variability associated with in vivo studies (e.g. differences in tumor size, injected dose, subject weight, etc.). To address this issue, we have developed a lanthanide-doped nanoparticle system and analytical method that allows for the quantitative comparison of multiple nanoparticle compositions simultaneously. Specifically, superparamagnetic iron oxide (SPIO) with a range of different sizes and charges were synthesized, each with a unique lanthanide dopant. Following the simultaneous injection of the various SPIO compositions into tumor-bearing mice, inductively coupled plasma mass spectroscopy (ICP-MS) was used to quantitatively and orthogonally assess the concentration of each SPIO composition in serial blood samples and the resected tumor and organs. The method proved generalizable to other nanoparticle platforms, including dendrimers, liposomes, and polymersomes. This approach provides a simple, cost-effective, and non-radiative method to quantitatively compare tumor localization, biodistribution, and blood clearance of more than 10 nanoparticle compositions simultaneously, removing subject-to-subject variability.

| S-EPMC3237748 | biostudies-literature

A dual-functional lanthanide nanoprobe for both living cell imaging and ICP-MS quantification of active protease.

Project description:Real-time imaging and quantitative monitoring of dynamic changes in biomolecules in bioprocesses is in urgent need for biological and clinical studies. However, this goal is difficult to achieve due to the incompatibility between the commonly used imaging and quantification methods. To fulfill this need, we developed the first nanoprobe capable of both living cell imaging and ultrasensitive quantification of proteases in cancer cells by taking advantage of the characteristic luminescence and ICP-MS response of lanthanide metals. The nanoprobe is composed of a lanthanide metal-based luminescent donor/mass tag and a gold nanoparticle quencher linked by a specific peptide recognized by proteases. The protease activity in living cells is both visualized and quantified by monitoring the enzymatically released lanthanide metal using fluorescence imaging and ICP-MS. The low ppb level sensitivity of this method demonstrates its potential in the study of protease-dependent pathways and related diseases.

| S-EPMC5977404 | biostudies-literature

Bio-Functional, Lanthanide-Labeled Polymer Particles by Seeded Emulsion Polymerization and their Characterization by Novel ICP-MS Detection.

Project description:We present the synthesis and characterization of monodisperse, sub-micron poly(styrene) (PS) particles loaded with up to and including 10(7) lanthanide (Ln) ions per particle. These particles have been synthesized by seeded emulsion polymerization with a mixture of monomer and a pre-formed Ln complex, and analyzed on a particle-by-particle basis by a unique inductively coupled plasma mass cytometer. Seed particles were prepared by surfactant-free emulsion polymerization (SFEP) to obtain large particle sizes in aqueous media. Extensive surface acid functionality was introduced using the acid-functional initiator ACVA, either during seed latex synthesis or in the second stage of polymerization. The loading of particles with three different Ln ions (Eu, Tb, and Ho) has proven to be close to 100 % efficient on an individual and combined basis. Covalent attachment of metal-tagged peptides and proteins such as Neutravidin to the particle surface was shown to be successful and the number of bound species can be readily determined. We believe these particles can serve as precursors for multiplexed, bead-based bio-assays utilizing mass cytometric detection.

| S-EPMC2852895 | biostudies-literature

Species-specific isotope dilution analysis of monomethylmercury in sediment using GC/ICP-ToF-MS and comparison with ICP-Q-MS and ICP-SF-MS.

Project description:A recently introduced inductively coupled plasma-time-of-flight-mass spectrometer (ICP-ToF-MS) shows enhanced sensitivity compared to previous developments and superior isotope ratio precision compared to other ToF and commonly used single-collector ICP-MS instruments. Following this fact, an improvement for isotope dilution ICP-MS using the new instrumentation has been reported. This study aimed at investigating whether this improvement also meets the requirements of species-specific isotope dilution using GC/ICP-MS, where short transient signals are recorded. The results of the analysis of monomethylmercury (MMHg) of a sediment reference material show that isotope ratio precision of ICP-MS instruments equipped with quadrupole, sector-field, and time-of-flight mass analyzers is similar within a broad range of peak signal-to-noise ratio when analyzing one isotopic system. The procedural limit of quantification (LOQ) for MMHg, expressed as mass fraction of Hg being present as MMHg, w(Hg)MMHg, was similar as well for all investigated instruments and ranged between 0.003 and 0.016 μg/kg. Due to the simultaneous detection capability, the ICP-ToF-MS might, however, be more favorable when several isotopic systems are analyzed within one measurement. In a case study, the GC/ICP-ToF-MS coupling was applied for analysis of MMHg in sediments of Finow Canal, a historic German canal heavily polluted with mercury. Mass fractions between 0.180 and 41 μg/kg (w(Hg)MMHg) for MMHg, and 0.056 and 126 mg/kg (w(Hg)total) for total mercury were found in sediment samples taken from the canal upstream and downstream of a former chemical plant.

| S-EPMC8405517 | biostudies-literature

Intracellular lectins are involved in quality control of glycoproteins.

Project description:Glycoprotein quality control is categorized into three kinds of reactions; the folding of nascent glycoproteins, ER-associated degradation of misfolded or unassembled glycoproteins, and transport and sorting of correctly folded glycoproteins. In all three processes, N-glycans on the glycoproteins are used as tags that are recognized by intracellular lectins. We analyzed the functions of these intracellular lectins and their sugar-binding specificities. The results clearly showed that the A, B, and C-arms of high mannose-type glycans participate in the folding, transport and sorting, and degradation, respectively, of newly synthesized peptides. After correctly folded glycoproteins are transported to the Golgi apparatus, N-glycans are trimmed into Man3GlcNAc2 and then rebuilt into various complex-type glycans in the Golgi, resulting in the addition of diverse sugar structures that allow glycoproteins to play various roles outside of the cells.

| S-EPMC3948941 | biostudies-literature

Synthetic lectins for selective binding of glycoproteins in water.

Project description:Although synthetic mimics of lectins can be extremely useful in biological and biomedical research, molecular recognition of carbohydrates has been hampered by their strong solvation in water and subtle structural differences among analogues. Molecularly imprinted nanoparticle receptors were prepared with glycans directly cleaved from glycoproteins. Functionalized with boroxole groups in the binding sites, these water-soluble synthetic lectins bound the parent glycoproteins selectively in water with an association constant of Ka = 104-105 M-1. The strong binding enabled the receptors to protect the targeted glycans from enzymatic cleavage. When clicked onto magnetic nanoparticles, the receptors enabled facile isolation of glycoproteins from a mixture.

| S-EPMC7484035 | biostudies-literature

Metabolite profiling with HPLC-ICP-MS as a tool for in vivo characterization of imaging probes.

Project description:BackgroundCurrent analytical methods for characterizing pharmacokinetic and metabolic properties of positron emission tomography (PET) and single photon emission computed tomography (SPECT) probes are limited. Alternative methods to study tracer metabolism are needed. The study objective was to assess the potential of high performance liquid chromatography - inductively coupled plasma - mass spectrometry (HPLC-ICP-MS) for quantification of molecular probe metabolism and pharmacokinetics using stable isotopes.MethodsTwo known peptide-DOTA conjugates were chelated with natGa and natIn. Limit of detection of HPLC-ICP-MS for 69Ga and 115In was determined. Rats were administered 50-150 nmol of Ga- and/or In-labeled probes, blood was serially sampled, and plasma analyzed by HPLC-ICP-MS using both reverse phase and size exclusion chromatography.ResultsThe limits of detection were 0.16 pmol for 115In and 0.53 pmol for 69Ga. Metabolites as low as 0.001 %ID/g could be detected and transchelation products identified. Simultaneous administration of Ga- and In-labeled probes allowed the determination of pharmacokinetics and metabolism of both probes in a single animal.ConclusionsHPLC-ICP-MS is a robust, sensitive and radiation-free technique to characterize the pharmacokinetics and metabolism of imaging probes.

| S-EPMC5824709 | biostudies-literature

Determination of Toxic Elements and Arsenic Species in Salted Foods and Sea Salt by ICP-MS and HPLC-ICP-MS.

Project description:Toxic elements (Cd, Pb, and As) accumulate into the environment by industrialization and natural phenomena and then pass to organisms. Analysis of toxic elements in food must be accurately carried out on a regular basis so as to avoid any adverse impact. Salted foods are difficult samples and accurate analysis of As is not easy due to salt interference. In this study, analysis of As was carried without influence of salts in three types of salted foods via an analytical method, which was validated using spiking recovery experiments and by analyzing certified reference materials. As a result, toxic elements were detected in all samples but none of these exceeded the World Health Organization recommended limits. Among the As species, arsenobetaine (AsB) was the most abundant, while inorganic As was below the detection limit in all samples. All the analyzed salted food samples appeared to be safe for consumption. In addition, the analysis of sea shrimp, freshwater shrimp, and seawater verified As bioaccumulation in these organisms from the environment.

| S-EPMC8340090 | biostudies-literature

SEC ICP MS and CZE ICP MS investigation of medium and high molecular weight complexes formed by cadmium ions with phytochelatins.

Project description:Size-exclusion chromatography (SEC) and capillary zone electrophoresis (CZE) coupled with inductively coupled plasma mass spectrometry were applied to characterize low, medium, and high molecular weight cadmium complexes with glutathione and phytochelatins (PCs). The dominant stoichiometry of the complexes formed in vitro was established as 1:1 using electrospray ionization mass spectrometry. Calculated molecular masses of Cd1L1 complexes were used for calibration of the SEC and CZE methods. The results showed a lower (2 kDa) SEC column exclusion limit for cadmium complexes compared with free peptides (10 kDa), and most of the high molecular weight cadmium species were eluted in the void volume of the column. Moreover, the CZE method based on the semiempirical model of Offord to elucidate peptide migration allowed us to show a high propensity of Cd-PC complexes for polymorphism on complexation, which was also observed for extracts of Arabidopsis thaliana treated with cadmium. All the information presented is vital for understanding the mechanism of metal deactivation in plants.

| S-EPMC3637892 | biostudies-other

Enrichment of glycoproteins using nanoscale chelating concanavalin A monolithic capillary chromatography.

Project description:Immobilized lectin chromatography can be employed for glycoprotein enrichment, but commonly used columns have limitations of yield and resolution. To improve efficiency and to make the technique applicable to minimal sample material, we have developed a nanoscale chelating Concanavalin A (Con A) monolithic capillary prepared using GMA-EDMA (glycidyl methacrylate-co-ethylene dimethacrylate) as polymeric support. Con A was immobilized on Cu(II)-charged iminodiacetic acid (IDA) regenerable sorbents by forming a IDA:Cu(II):Con A sandwich affinity structure that has high column capacity, as well as stability. When compared with conventional Con A lectin chromatography, the monolithic capillary enabled the better reproducible detection of over double the number of unique N-glycoproteins in human urine samples. Utility for analysis of minimal biological samples was confirmed by the successful elucidation of glycoprotein profiles in mouse urine samples at the microliter scale. The improved efficiency of the nanoscale monolithic capillary will impact the analysis of glycoproteins in complex biological samples, especially where only limited material may be available.

| S-EPMC2759973 | biostudies-literature

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data