Publication: Tumor suppressive monoclonal antibody belonging to the V<inf>H</inf>7183 family directed to the oncodevelopmental carbohydrate antigen on human hepatocellular carcinoma
Issued Date
2002-01-01
Resource Type
ISSN
13891723
Other identifier(s)
2-s2.0-0036098630
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Mahidol University
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SCOPUS
Bibliographic Citation
Journal of Bioscience and Bioengineering. Vol.93, No.3 (2002), 266-273
Suggested Citation
Duanpen Sandee, Sumalee Tungpradabkul, Kingkarn Laohathai, Boonnum Punyammalee, Katsunori Kohda, Masahiro Takagi, Tadayuki Imanaka Tumor suppressive monoclonal antibody belonging to the V<inf>H</inf>7183 family directed to the oncodevelopmental carbohydrate antigen on human hepatocellular carcinoma. Journal of Bioscience and Bioengineering. Vol.93, No.3 (2002), 266-273. doi:10.1016/S1389-1723(02)80027-5 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/20109
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Title
Tumor suppressive monoclonal antibody belonging to the V<inf>H</inf>7183 family directed to the oncodevelopmental carbohydrate antigen on human hepatocellular carcinoma
Abstract
Hep27 monoclonal antibody (Hep27 Mab) was raised by immunizing BALB/c mice with cells of the Thai human hepatocellular carcinoma (HCC) cell line HCC-S102 using hybridoma technology. The Hep27 Mab recognizes oncofetal development antigens by reacting with many HCC, other cancers, fetal and newborn liver but not adult liver. The Hep27 Mab alone markedly inhibits the growth of hepatocellular carcinoma cell lines (65% viability on the third day), suggesting its clinical usefulness. Moreover, complementary DNA (cDNA) for active variable regions of both heavy and light chains of the antibody has been cloned. Sequence analysis of the variable region of the Hep27 Mab revealed that the VHand VLgenes belong to the VH7183 and VKfamilies, respectively. We have also characterized the reactivity of the Hep27 Mab to synthetic carbohydrate epitopes and 1-phenyl-2-decanoylamino-3-morpholino-1-propanol (PDMP)-treated HCC-S102 cells. The results showed that the Hep27 Mab recognizes a neoglycolipid containing a mucin core unit and PDMP treatment reduced Hep27 Mab binding activity to HCC-S102 cells, indicating that the Hep27 Mab recognizes a glycolipid antigen on HCC-S102 cells. This Mab may be potentially useful for studying antigenic expression in hepatocellular carcinoma and as a targeting agent for radioimmunodetection and immunoconjugated therapy.