Enrichment strategies in glycomics‐based lung cancer biomarker development. Issue 9 (6th August 2013)
- Record Type:
- Journal Article
- Title:
- Enrichment strategies in glycomics‐based lung cancer biomarker development. Issue 9 (6th August 2013)
- Main Title:
- Enrichment strategies in glycomics‐based lung cancer biomarker development
- Authors:
- Ruhaak, L. Renee
Nguyen, Uyen Thao
Stroble, Carol
Taylor, Sandra L.
Taguchi, Ayumu
Hanash, Samir M.
Lebrilla, Carlito B.
Kim, Kyoungmi
Miyamoto, Suzanne
Pierce, Michael
Taniguchi, Naoyuki - Abstract:
- <abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="prca1472-sec-0010" sec-type="section"> <title>Purpose</title> <p>There is a need to identify better glycan biomarkers for diagnosis, early detection, and treatment monitoring in lung cancer using biofluids such as blood. Biofluids are complex mixtures of proteins dominated by a few high abundance proteins that may not have specificity for lung cancer. Therefore, two methods for protein enrichment were evaluated; affinity capturing of IgG and enrichment of medium abundance proteins, thus allowing us to determine which method yields the best candidate glycan biomarkers for lung cancer.</p> </sec> <sec id="prca1472-sec-0020" sec-type="section"> <title>Experimental design</title> <p> <italic>N</italic>‐glycans isolated from plasma samples from 20 cases of lung adenocarcinoma and 20 matched controls were analyzed using nLC‐PGC‐chip‐TOF‐MS (where PGC is porous‐graphitized carbon). <italic>N</italic>‐glycan profiles were obtained for five different fractions: total plasma, isolated IgG, IgG‐depleted plasma, and the bound and flow‐through fractions of protein enrichment.</p> </sec> <sec id="prca1472-sec-0030" sec-type="section"> <title>Results</title> <p>Four glycans differed significantly (false discovery rate, FDR &lt; 0.05) between cases and controls in whole unfractionated plasma, while four other glycans differed significantly by cancer status in the IgG fraction. No significant<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <sec id="prca1472-sec-0010" sec-type="section"> <title>Purpose</title> <p>There is a need to identify better glycan biomarkers for diagnosis, early detection, and treatment monitoring in lung cancer using biofluids such as blood. Biofluids are complex mixtures of proteins dominated by a few high abundance proteins that may not have specificity for lung cancer. Therefore, two methods for protein enrichment were evaluated; affinity capturing of IgG and enrichment of medium abundance proteins, thus allowing us to determine which method yields the best candidate glycan biomarkers for lung cancer.</p> </sec> <sec id="prca1472-sec-0020" sec-type="section"> <title>Experimental design</title> <p> <italic>N</italic>‐glycans isolated from plasma samples from 20 cases of lung adenocarcinoma and 20 matched controls were analyzed using nLC‐PGC‐chip‐TOF‐MS (where PGC is porous‐graphitized carbon). <italic>N</italic>‐glycan profiles were obtained for five different fractions: total plasma, isolated IgG, IgG‐depleted plasma, and the bound and flow‐through fractions of protein enrichment.</p> </sec> <sec id="prca1472-sec-0030" sec-type="section"> <title>Results</title> <p>Four glycans differed significantly (false discovery rate, FDR &lt; 0.05) between cases and controls in whole unfractionated plasma, while four other glycans differed significantly by cancer status in the IgG fraction. No significant glycan differences were observed in the other fractions.</p> </sec> <sec id="prca1472-sec-0040" sec-type="section"> <title>Conclusions and clinical relevance</title> <p>These results confirm that the <italic>N</italic>‐glycan profile in plasma of lung cancer patients is different from healthy controls and appears to be dominated by alterations in relatively abundant proteins.</p> </sec> </abstract> … (more)
- Is Part Of:
- Proteomics. Volume 7:Issue 9/10(2013)
- Journal:
- Proteomics
- Issue:
- Volume 7:Issue 9/10(2013)
- Issue Display:
- Volume 7, Issue 9/10 (2013)
- Year:
- 2013
- Volume:
- 7
- Issue:
- 9/10
- Issue Sort Value:
- 2013-0007-NaN-0000
- Page Start:
- 664
- Page End:
- 676
- Publication Date:
- 2013-08-06
- Subjects:
- Proteomics -- Periodicals
572.605 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1862-8354 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/prca.201200131 ↗
- Languages:
- English
- ISSNs:
- 1862-8346
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6936.178500
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3446.xml