Detailed Information on Publication Record
2016
Development and application of a novel recombinant Aleuria aurantia lectin with enhanced core fucose binding for identification of glycoprotein biomarkers of hepatocellular carcinoma
NORTON, Pamela, Mary Ann COMUNALE, Harmin HERRERA, Mengjun WANG, Josef HOUSER et. al.Basic information
Original name
Development and application of a novel recombinant Aleuria aurantia lectin with enhanced core fucose binding for identification of glycoprotein biomarkers of hepatocellular carcinoma
Authors
NORTON, Pamela (840 United States of America), Mary Ann COMUNALE (840 United States of America), Harmin HERRERA (840 United States of America), Mengjun WANG (840 United States of America), Josef HOUSER (203 Czech Republic, belonging to the institution), Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution), Patrick R ROMANO (840 United States of America) and Anand MEHTA (356 India)
Edition
Proteomics, HOBOKEN, Wiley-Blackwell, 2016, 1615-9853
Other information
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
10600 1.6 Biological sciences
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Impact factor
Impact factor: 4.041
RIV identification code
RIV/00216224:14740/16:00088672
Organization unit
Central European Institute of Technology
UT WoS
000390809000010
Keywords in English
Aleuria aurantia lectin; Biomarker; Glycoproteomics; Glycosylation; Hepatocellular carcinoma; Liver cancer
Tags
Tags
International impact, Reviewed
Změněno: 14/3/2017 13:06, Mgr. Eva Špillingová
Abstract
V originále
The Aleuria aurantia lectin (AAL) derived from orange peel fungus contains five fucose-binding sites that recognizes fucose bound in -1,2, -1,3, -1,4, and -1,6 linkages to N-acetylglucosamine and galactose. Recently, we have created several recombinant AAL (rAAL) proteins that had altered binding affinity to fucose linkages. In this report, we further characterize the binding specificity of one of the mutated lectins, N224Q lectin. This lectin was characterized by lectin Western blotting, surface plasmon resonance, and glycan microarray and shown to have increased binding to fucosylated glycan. Subsequently, we used this lectin to identify secreted fucosylated glycoproteins from a fetal hepatic cell line. Proteomic analysis revealed several glycoproteins secreted by the fetal cell line that were bound by N224Q lectin. These findings were confirmed by subsequent proteomic analysis of human serum from control patients or patients with hepatocellular carcinoma. These represent candidate oncofetal markers for liver cancer.
Links
GA13-25401S, research and development project |
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LQ1601, research and development project |
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