NIH VideoCast - Glycoproteomics Using Mass Spectrometry and Lectin Microarrays

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Glycoproteomics Using Mass Spectrometry and Lectin Microarrays

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Air date:	Thursday, December 1, 2011, 10:00:00 AM Time displayed is Eastern Time, Washington DC Local
Views:	Total views: 353 (10 Live, 343 On-demand)
Category:	Proteomics
Runtime:	01:15:58
Closed captioning:	Check box to display CC outside of the video Note: You can drag the captioning window around and resize it
Description:	NIH Proteomics Interest Group Lecture: Glycosylation is one of the most common forms of protein modifications. Each glycoprotein can be glycosylated at different glycosites and each glycosite may be modified by different glycans. This structural heterogeneity has complicated the study of the structure-function relationships of glycoproteins. To rapid identify and quantify the glycosylation on particular glycosites from complex biological mixtures, glycan-lectin affinity chromatography and chemical immobilization are used to isolate glycopeptides containing certain glycans, followed by mass spectrometry analysis. We showed that upon the identification of disease-specific changes in glycosylation using lectin microarray technique, glycosites containing aberrant glycans were readily identifiable and quantifiable using the combination of lectins and mass spectrometry. The application of glycoproteomics may facilitate our understanding of how perturbed glycosylation impacts upon disease progression and could be used to discover glycosylated proteins that could serve as biomarkers or therapeutic targets to improve clinical outcomes of patients.

NLM Title:	Glycoproteomics using mass spectrometry and lectin microarrays / Hui Zhang.
Author:	Zhang, Hui. National Institutes of Health (U.S.). Proteomics Interest Group.
Publisher:
Abstract:	(CIT): Glycosylation is one of the most common forms of protein modifications. Each glycoprotein can be glycosylated at different glycosites and each glycosite may be modified by different glycans. This structural heterogeneity has complicated the study of the structure-function relationships of glycoproteins. To rapid identify and quantify the glycosylation on particular glycosites from complex biological mixtures, glycan-lectin affinity chromatography and chemical immobilization are used to isolate glycopeptides containing certain glycans, followed by mass spectrometry analysis. We showed that upon the identification of disease-specific changes in glycosylation using lectin microarray technique, glycosites containing aberrant glycans were readily identifiable and quantifiable using the combination of lectins and mass spectrometry. The application of glycoproteomics may facilitate our understanding of how perturbed glycosylation impacts upon disease progression and could be used to discover glycosylated proteins that could serve as biomarkers or therapeutic targets to improve clinical outcomes of patients.
Subjects:	Glycosylation Lectins Microarray Analysis--methods Proteomics Spectrum Analysis--methods
Publication Types:	Lecture Webcast

NLM Classification:	QU 55.5
NLM ID:	101574498
CIT Live ID:	10816
Permanent link:	https://videocast.nih.gov/watch=10816

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