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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
2007-12-6
pubmed:abstractText
Glycoproteins in human serum play fundamental roles in many biological processes, and also have clinical value as biomarkers for disease progression and treatment. In this study, we isolated glycoproteins from the sera of three healthy individuals and three lung adenocarcinoma patients using multilectin affinity chromatography. The recovered glycoproteins were subjected to treatment with peptide-N-glycosidase F (PNGase F) and in-gel digestion by trypsin. Tryptic peptides were analyzed by nano-LC coupled to ESI-MS/MS and the MS/MS spectra were processed by Bioworks 3.2 and an in-house bioinformatics tool, ProtAn. Approximately 90% of the proteins identified contained more than one potential glycosylation site. Comparison of the serum glycoproteome of healthy and adenocarcinoma individuals revealed 38 cancer-selective proteins. Among them, 60% have previously been reported as low abundance proteins in human sera. We identified several cancer-selective proteins that have been previously characterized as potential indicators of lung cancer in serum or plasma, including haptoglobin (HP), inter-alpha-trypsin inhibitor heavy chain 4 (ITI-H4), complement C3 precursor, and leucine-rich alpha-2-glycoprotein. In addition, plasma kallikrein (KLKB1) and inter-alpha-trypsin inhibitor heavy chain 3 (ITI-H3) were identified as being potentially elevated in the lung cancer group, and were validated by Western blot analysis. Furthermore, approximately 18 kDa plasma kallirein protein fragment was detected at high levels in 25 out of 28 adenocarcinoma patients, while one of the eight normal individuals showed moderate positive. The results suggest that KLKB1 represents a potential candidate serum biomarker of lung cancer.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1615-9853
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4292-302
pubmed:meshHeading
pubmed-meshheading:17963278-Adenocarcinoma, pubmed-meshheading:17963278-Aged, pubmed-meshheading:17963278-Alpha-Globulins, pubmed-meshheading:17963278-Blood Proteins, pubmed-meshheading:17963278-Blotting, Western, pubmed-meshheading:17963278-Chromatography, Affinity, pubmed-meshheading:17963278-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:17963278-Gene Expression, pubmed-meshheading:17963278-Glycoproteins, pubmed-meshheading:17963278-Humans, pubmed-meshheading:17963278-Lectins, pubmed-meshheading:17963278-Lung Neoplasms, pubmed-meshheading:17963278-Male, pubmed-meshheading:17963278-Middle Aged, pubmed-meshheading:17963278-Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase, pubmed-meshheading:17963278-Plasma Kallikrein, pubmed-meshheading:17963278-Reproducibility of Results, pubmed-meshheading:17963278-Tandem Mass Spectrometry, pubmed-meshheading:17963278-Tumor Markers, Biological, pubmed-meshheading:17963278-Up-Regulation
pubmed:year
2007
pubmed:articleTitle
Identification of putative serum glycoprotein biomarkers for human lung adenocarcinoma by multilectin affinity chromatography and LC-MS/MS.
pubmed:affiliation
Department of Biochemistry, School of Dentistry, Kyungpook National University, Daegu, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't