Vongchan P, Linhardt RJ. Characterization of a new monoclonal anti-glypican-3 antibody specific to the hepatocellular carcinoma cell line, HepG2. World J Hepatol 2017; 9(7): 368-384 [PMID: 28321273 DOI: 10.4254/wjh.v9.i7.368]
Corresponding Author of This Article
Preeyanat Vongchan, PhD, Department of Medical Technology, Faculty of Associated Medical Sciences, Chiang Mai University, 239 Huay Kaew Road, Muang District, Chiang Mai 50200, Thailand. preeyanat.v@cmu.ac.th
Research Domain of This Article
Immunology
Article-Type of This Article
Basic Study
Open-Access Policy of This Article
This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
World J Hepatol. Mar 8, 2017; 9(7): 368-384 Published online Mar 8, 2017. doi: 10.4254/wjh.v9.i7.368
Characterization of a new monoclonal anti-glypican-3 antibody specific to the hepatocellular carcinoma cell line, HepG2
Preeyanat Vongchan, Robert J Linhardt
Preeyanat Vongchan, Department of Medical Technology, Faculty of Associated Medical Sciences, Chiang Mai University, Chiang Mai 50200, Thailand
Robert J Linhardt, Rensselaer Polytechnic Institute, Departments of Chemistry, Biology, Chemical and Biomedical Engineering, Troy, NY 12180, United States
Author contributions: Vongchan P (primary investigator) performed research, analyzed the data and prepared manuscript; Linhardt RJ contributed reagents and analytical tools, and revised manuscript.
Supported byNational Research Council of Thailand (NRCT), No. 2559A10402115.
Institutional review board statement: Not available.
Institutional animal care and use committee statement: Not available.
Conflict-of-interest statement: The authors declare that there are no conflicts of interest.
Data sharing statement: No additional are available.
Open-Access: This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
Correspondence to: Preeyanat Vongchan, PhD, Department of Medical Technology, Faculty of Associated Medical Sciences, Chiang Mai University, 239 Huay Kaew Road, Muang District, Chiang Mai 50200, Thailand. preeyanat.v@cmu.ac.th
Telephone: +66-53-945080 Fax: +66-53-946042
Received: November 21, 2016 Peer-review started: November 23, 2016 First decision: December 15, 2016 Revised: December 19, 2016 Accepted: January 11, 2017 Article in press: January 14, 2017 Published online: March 8, 2017 Processing time: 105 Days and 2.4 Hours
Core Tip
Core tip: Heparan sulfate proteoglycan (HSPG) was isolated from human liver. Preliminary results showed that it was detected by rabbit anti-glypican. Monoclonal antibody, 1E4-1D9 was raised against human liver HSPG and its specific antigen was characterized. Amino acid sequence analysis revealed that the antigen recognized by mAb 1E4-1D9 specific molecule contained no transmembrane region. It has 15 cysteines and 11 putative glycosylation sites and 6 predicted N-glycosylation sites. The sequence matched to all PDZ domain proteins with an 85.6% match to glypican-3. Studies of co-expression and co-precipitation demonstrated that mAb 1E4-1D9 could compete with anti-glypican-3. It could also react with a various tumor cell lines including solid and hematopoietic cells. The findings suggested that the antigen recognized by 1E4-1D9 was glypican-3. Moreover, findings revealed that FYCO1 co-precipitated with glypican-3 using mAb 1E4-1D9, suggesting that FYCO1 is a partner molecule of glypican-3.
