J 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
Name: Studium proteinů z patogenů zapojených do rozpoznávání hostitelského organismu
Investor: Czech Science Foundation
LQ1601, research and development project
Name: CEITEC 2020 (Acronym: CEITEC2020)
Investor: Ministry of Education, Youth and Sports of the CR