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  • P-ISSN 2233-4203
  • E-ISSN 2093-8950

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
Shin Jihoon (Wonkwang University)
Lee Jinwook (Wonkwang University)
Cho Wonryeon (Wonkwang University)
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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


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Submission Date
2018-05-15
Revised Date
2018-05-17
Accepted Date
2018-05-17
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