Glycoproteomics: Difference between revisions
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'''Glycoproteomics''' is a branch of [[proteomics]] that identifies, catalogs, and characterizes [[ |
'''Glycoproteomics''' is a branch of [[proteomics]] that identifies, catalogs, and characterizes [[Protein|proteins]] containing [[Carbohydrate|carbohydrates]] as a result of [[Posttranslational modification|post-translational modifications]].<ref>{{cite journal |vauthors=Tissot B, North SJ, Ceroni A, Pang PC, Panico M, Rosati F, Capone A, Haslam SM, Dell A, Morris HR |year=2009 |title=Glycoproteomics: past, present and future |journal=FEBS Lett. |volume=583 |issue=11 |pages=1728–1735 |doi=10.1016/j.febslet.2009.03.049 |pmc=2753369 |pmid=19328791}}</ref> Glycosylation is the most common post-translational modification of proteins, but continues to be the least studied on the proteome level.<ref name=":02">{{Cite journal |last=Doerr |first=Allison |date=January 2012 |title=Glycoproteomics |url=http://www.nature.com/articles/nmeth.1821 |journal=Nature Methods |language=en |volume=9 |issue=1 |pages=36–36 |doi=10.1038/nmeth.1821 |issn=1548-7091}}</ref> Mass spectrometry (MS) is an analytical technique used to improve the study of these proteins on the proteome level. Glycosylation contributes to several concerted biological mechanisms essential to maintaining physiological function. The study of the glycosylation of proteins is important to understanding certain diseases, like cancer, because a connection between a change in glycosylation and these diseases has been discovered. To study this post-translational modification of proteins, advanced mass spectrometry techniques based on glycoproteomics have been developed to help in terms of therapeutic applications and the discovery of biomarkers.<ref>{{Cite journal |last=Pan |first=Sheng |last2=Chen |first2=Ru |last3=Aebersold |first3=Ruedi |last4=Brentnall |first4=Teresa A. |date=January 2011 |title=Mass Spectrometry Based Glycoproteomics—From a Proteomics Perspective |url=https://linkinghub.elsevier.com/retrieve/pii/S1535947620313888 |journal=Molecular & Cellular Proteomics |language=en |volume=10 |issue=1 |pages=R110.003251 |doi=10.1074/mcp.R110.003251 |pmc=PMC3013464 |pmid=20736408}}</ref> |
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=== Mass Spectrometry === |
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[[Mass spectrometry|Mass spectrometry (MS)]] is commonly used to identify the sugar moieties attached, but since there are many different glycan structures attached and different locations of glycosylation, this leads to challenges when attempting to sequence glycoproteins.<ref>{{Cite journal |last=Singh |first=Arunima |date=January 2021 |title=Glycoproteomics |url=https://www.nature.com/articles/s41592-020-01028-9 |journal=Nature Methods |language=en |volume=18 |issue=1 |pages=28–28 |doi=10.1038/s41592-020-01028-9 |issn=1548-7105}}</ref> Using mass spectrometry, there are two methods for glycoprotein analysis. The first strategy is called "top-down" which uses intact glycoproteins for the MS analysis without digesting and does not require an extensive sample preparation. The second and most common method for studying glycoproteins is the "bottom-up" strategy that initially cleaves the glycans from the glycoproteins using chemicals or enzymes. The glycans, which are carbohydrates, and proteins are purified, and individually analyzed. Based on the type of linkage that these glycans use to attach to proteins, different methods are used to separate the glycan from the protein. Using MS, the glycan structures and sequences of the proteins can be determined, but where the glycans bind to on the protein is sometimes undetermined. The last approach involves glycoprotein digestion using the enzyme, endoprotease, so the digested glycoproteins can then be characterized by MS techniques. Using this method, the glycosylated sites can be identified, so these approaches are used in conjunction when trying to identify glycoproteins.<ref>{{Cite journal |last=Liu |first=Huan |last2=Zhang |first2=Ningbo |last3=Wan |first3=Debin |last4=Cui |first4=Meng |last5=Liu |first5=Zhiqiang |last6=Liu |first6=Shuying |date=December 2014 |title=Mass spectrometry-based analysis of glycoproteins and its clinical applications in cancer biomarker discovery |url=https://clinicalproteomicsjournal.biomedcentral.com/articles/10.1186/1559-0275-11-14 |journal=Clinical Proteomics |language=en |volume=11 |issue=1 |pages=14 |doi=10.1186/1559-0275-11-14 |issn=1542-6416 |pmc=PMC3984494 |pmid=24722010}}</ref> As technology progresses, glycoprotein analyses have become more accurate using high-resolution mass spectrometry instrumentations.<ref name=":02" /> |
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==See also== |
==See also== |
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==References== |
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==External links== |
==External links== |
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Revision as of 13:42, 25 April 2022
Glycoproteomics is a branch of proteomics that identifies, catalogs, and characterizes proteins containing carbohydrates as a result of post-translational modifications.[1] Glycosylation is the most common post-translational modification of proteins, but continues to be the least studied on the proteome level.[2] Mass spectrometry (MS) is an analytical technique used to improve the study of these proteins on the proteome level. Glycosylation contributes to several concerted biological mechanisms essential to maintaining physiological function. The study of the glycosylation of proteins is important to understanding certain diseases, like cancer, because a connection between a change in glycosylation and these diseases has been discovered. To study this post-translational modification of proteins, advanced mass spectrometry techniques based on glycoproteomics have been developed to help in terms of therapeutic applications and the discovery of biomarkers.[3]
Mass Spectrometry
Mass spectrometry (MS) is commonly used to identify the sugar moieties attached, but since there are many different glycan structures attached and different locations of glycosylation, this leads to challenges when attempting to sequence glycoproteins.[4] Using mass spectrometry, there are two methods for glycoprotein analysis. The first strategy is called "top-down" which uses intact glycoproteins for the MS analysis without digesting and does not require an extensive sample preparation. The second and most common method for studying glycoproteins is the "bottom-up" strategy that initially cleaves the glycans from the glycoproteins using chemicals or enzymes. The glycans, which are carbohydrates, and proteins are purified, and individually analyzed. Based on the type of linkage that these glycans use to attach to proteins, different methods are used to separate the glycan from the protein. Using MS, the glycan structures and sequences of the proteins can be determined, but where the glycans bind to on the protein is sometimes undetermined. The last approach involves glycoprotein digestion using the enzyme, endoprotease, so the digested glycoproteins can then be characterized by MS techniques. Using this method, the glycosylated sites can be identified, so these approaches are used in conjunction when trying to identify glycoproteins.[5] As technology progresses, glycoprotein analyses have become more accurate using high-resolution mass spectrometry instrumentations.[2]
See also
External links
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- ^ Tissot B, North SJ, Ceroni A, Pang PC, Panico M, Rosati F, Capone A, Haslam SM, Dell A, Morris HR (2009). "Glycoproteomics: past, present and future". FEBS Lett. 583 (11): 1728–1735. doi:10.1016/j.febslet.2009.03.049. PMC 2753369. PMID 19328791.
- ^ a b Doerr, Allison (January 2012). "Glycoproteomics". Nature Methods. 9 (1): 36–36. doi:10.1038/nmeth.1821. ISSN 1548-7091.
- ^ Pan, Sheng; Chen, Ru; Aebersold, Ruedi; Brentnall, Teresa A. (January 2011). "Mass Spectrometry Based Glycoproteomics—From a Proteomics Perspective". Molecular & Cellular Proteomics. 10 (1): R110.003251. doi:10.1074/mcp.R110.003251. PMC 3013464. PMID 20736408.
{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link) - ^ Singh, Arunima (January 2021). "Glycoproteomics". Nature Methods. 18 (1): 28–28. doi:10.1038/s41592-020-01028-9. ISSN 1548-7105.
- ^ Liu, Huan; Zhang, Ningbo; Wan, Debin; Cui, Meng; Liu, Zhiqiang; Liu, Shuying (December 2014). "Mass spectrometry-based analysis of glycoproteins and its clinical applications in cancer biomarker discovery". Clinical Proteomics. 11 (1): 14. doi:10.1186/1559-0275-11-14. ISSN 1542-6416. PMC 3984494. PMID 24722010.
{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)