An epithelial cell adhesion molecule (EpCAM) was selectively expressed in human colorectal carcinoma. Treatment with plant-derived anti-EpCAM mAb (mAbP CO17-1A) and RAW264.7 cells inhibited cell growth in the human colorectal cancer cell line SW620. In SW620 treated with mAbP CO17-1A and RAW264.7 cells, expression of p53 and p21 increased, whereas the expression of G1 phase-related proteins, cyclin D1, CDK4, cyclin E, and CDK2, decreased, similar to mammalian-derived mAb (mAbM) CO17-1A. Similar to mAbM CO17-1A, treatment with mAbP CO17-1A and RAW264.7 cell decreased the expression of anti-apoptotic protein, Bcl-2, but the expression of pro-apoptotic proteins Bax, TNF-α, caspase-3, caspase-6, caspase-8 and caspase-9, increased. Cells treated with mAbP CO17-1A and RAW264.7 cells expressed metastasis-related gangliosides, GM1 and GD1a, similar to mAbM CO17-1A. These results suggest that mAbP CO17-1A is as effective on anti-cancer activity as mAbM CO17-1A.
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Expression and in vitro function of anti-cancer mAbs in transgenic Arabidopsis thaliana.
BMB Rep
April 2020
Departments of Medicine, College of Medicine, Chung-Ang University, Seoul 06974, Korea.
The anti-colorectal cancer monoclonal antibody CO17-1A (mAb CO), which recognizes the tumor-associated antigen EpCAM, was expressed in transgenic Arabidopsis plants. PCR and western blot analyses showed the insertion and expression of heavy chain (HC)/HC fused to the KDEL ER retention modif (HCK) and light chain (LC) of mAb CO and mAb CO with HCK (mAb COK) in Arabidopsis transformants. Both plantderived mAbP CO and mAbP COK were purified from a biomass of approximately 1,000 seedlings grown in a greenhouse.
View Article and Find Full Text PDFGrowth suppression of colorectal cancer by plant-derived multiple mAb CO17-1A × BR55 via inhibition of ERK1/2 phosphorylation.
Int J Mol Sci
November 2014
Institute of Glycoscience, Wonkwang University, Iksan, Jeonbuk 570-749, Korea.
Article Synopsis
- * Treatment with the engineered multiple mAb significantly reduced the growth of SW620 cancer cells and led to increased apoptotic cell death, indicating it may be effective in inducing cancer cell death.
- * The mAb treatment also demonstrated enhanced tumor suppression in mouse models, suggesting that it works by inhibiting certain cancer-related signaling pathways, warranting further research into its effectiveness for human colon cancer therapy.
An epithelial cell adhesion molecule (EpCAM) was selectively expressed in human colorectal carcinoma. Treatment with plant-derived anti-EpCAM mAb (mAbP CO17-1A) and RAW264.7 cells inhibited cell growth in the human colorectal cancer cell line SW620.
View Article and Find Full Text PDFBiological validation of plant-derived anti-human colorectal cancer monoclonal antibody CO17-1A.
Hybridoma (Larchmt)
February 2009
1 Department of Biological Science, College of Natural Sciences, Wonkwang University, Iksan, Chonbuk 570-749, Korea.
We validated expression and biological activities of plant-derived monoclonal antibody (MAb(P)) CO17-1A for its efficacy in cancer immunotherapy. PCR and immunoblot analyses demonstrated insertion and expression of heavy and light chains of MAb CO17-1A in transgenic plants, respectively. Confocal analysis revealed that MAb(P) CO17-1A was accumulated throughout the cytoplasm near the outer membrane, suggesting its secretion to the outer membrane via a default pathway.
View Article and Find Full Text PDFInhibition of tumor growth by plant-derived mAb.
Proc Natl Acad Sci U S A
May 2005
Biotechnology Foundation Laboratories, Thomas Jefferson University, 1020 Locust Street, M-85 Jefferson Alumni Hall, Philadelphia, PA 19107-6799, USA.
The tumor-associated antigen EpCAM (GA733-2) is a highly expressed target on adenocarcinoma cells, as defined by murine mAb CO17-1A. We recently developed a transgenic plant system for the safe and inexpensive production of large quantities of mAb CO17-1A as a future source of clinical-grade protein. Although the glycosylation pattern of plant-derived mAb (mAb(P)) CO17-1A differs considerably from that of the mammalian-derived mAb (mAb(M)), we show here that the biological activity of both mAbs is quite similar.
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