- P-ISSN 2233-4203
- E-ISSN 2093-8950
- Log In/Sign Up
- P-ISSN2233-4203
- E-ISSN2093-8950
- ESCI, SCOPUS, KCI
Article Detail
Home > Article Detail
Loss of Potential Biomarker Proteins Associated with Abundant Proteins during Abundant Protein Removal in Sample Pretreatment
Mass Spectrometry Letters / Mass Spectrometry Letters, (P)2233-4203; (E)2093-8950
2018, v.9 no.2, pp.51-55
https://doi.org/10.5478/MSL.2018.9.2.51
(Wonkwang University)
(Wonkwang University)
(Wonkwang University)
(Wonkwang University)
(Wonkwang University)
Shin,
J., Lee,
J., &
Cho,
W.
(2018). Loss of Potential Biomarker Proteins Associated with Abundant Proteins during Abundant Protein Removal in Sample Pretreatment. Mass Spectrometry Letters, 9(2), 51-55, https://doi.org/10.5478/MSL.2018.9.2.51
- Downloaded
- Viewed
Abstract
Capture of non-glycoproteins during lectin affinity chromatography is frequently observed, although it would seem to be anomalous. In actuality, lectin affinity chromatography works at post-translational modification (PTM) sites on a glycopro- tein which is not involved in protein-protein interactions (PPIs). In this study, serial affinity column set (SACS) using lectins fol- lowed by proteomics methods was used to identify PPI mechanisms of captured proteins in human plasma. MetaCore, STRING, Ingenuity Pathway Analysis (IPA), and IntAct were individually used to elucidate the interactions of the identified abundant pro- teins and to obtain the corresponding interaction maps. The abundant non-glycoproteins were captured with the binding to the selected glycoproteins. Therefore, depletion process in sample pretreatment for abundant protein removal should be considered with more caution because it may lose precious disease-related low abundant proteins through PPIs of the removed abundant proteins in human plasma during the depletion process in biomarker discovery. Glycoproteins bearing specific glycans are fre- quently associated with cancer and can be specifically isolated by lectin affinity chromatography. Therefore, SACS using Lycop- ersicon esculentum lectin (LEL) can also be used to study disease interactomes.
- keywords
- Serial affinity column set (SACS), Lectin, Depletion, Abundant protein removal, Protein-protein interactions (PPIs), Biomarker
Reference
1
2
Gadjeva, M.. (2014). The Complement System: Methods and Protocols:Humana Press.
3
4
5
6
7
8
Kohler, J. J.. (2013). Mass Spectrometry of Glycoproteins: Methods and Protocols:Humana Press.
9
Kim, B.. (2018). . Expert Rev. Proteomics, 15, 353-. http://dx.doi.org/10.1080/14789450.2018.1450631.
10
11
Buyuktiryaki, S.. (2016). . Sep. Sci. Technol., 51, 2080-. http://dx.doi.org/10.1080/01496395.2016.1200086.
12
13
14
15
16
Jihoon Shin. (2016). Differentiation of Glycan Diversity with Serial Affinity Column Set (SACS). Mass Spectrometry Letters, 7(3), 74-78. http://dx.doi.org/10.5478/MSL.2016.7.3.74.
17
- Submission Date
- 2018-05-15
- Revised Date
- 2018-05-17
- Accepted Date
- 2018-05-17
Other articles from this issue
- Simultaneous Quantification of 13 Ginsenosides by LC-MS/MS and its Application in Diverse Ginseng Extracts
- Effects of Temperature and Acetonitrile on Microwave-Assisted Weak Acid Protein Hydrolysis
- Loss of Potential Biomarker Proteins Associated with Abundant Proteins during Abundant Protein Removal in Sample Pretreatment
- Free Radical Initiated Peptide Sequencing Using MALDI-TOF/TOF Mass Spectrometry
- Characterization of Preclinical in Vitro and in Vivo Pharmacokinetic Properties of KPLA-012, a Benzopyranyl 1,2,3-Triazole Compound, with Anti-Angiogenetic and Anti-Tumor Progressive Effects
- more
Recommanded Articles
This website recommended the use the Chrome browser for journal website.