Mouse-human chimeric anti-Tn IgG1 induced anti-tumor activity against Jurkat cells in vitro and in vivo.

@article{Ando2008MousehumanCA,
  title={Mouse-human chimeric anti-Tn IgG1 induced anti-tumor activity against Jurkat cells in vitro and in vivo.},
  author={Hiroshi Ando and Takefumi Matsushita and Masako Wakitani and Takashi Sato and Sachiko Kodama-Nishida and K Shibata and Kenya Shitara and So Ohta},
  journal={Biological \& pharmaceutical bulletin},
  year={2008},
  volume={31 9},
  pages={
          1739-44
        }
}
Tn-antigen (alpha-N-acetyl-galactosamine(GalNAc)-Ser/Thr) is a cancer-associated carbohydrate antigen expressed in various epithelial and hematological cancers, and although a number of anti-Tn IgG and IgM antibodies have been generated, they have not been fully validated for cancer immunotherapy. In this study, we generated a novel murine anti-Tn IgG1 monoclonal antibody, KM3413, by immunization of mucins purified from a culture supernatant of LS180: a human colon cancer cell line. The binding… 
A new murine IgG1 anti-Tn monoclonal antibody with in vivo anti-tumor activity.
TLDR
The GOD3-2C4 antibody has antibody-dependent cellular cytotoxicity activity against Jurkat cells in vitro, and for the first time, it can be shown that an anti-Tn antibody has a significant in vivo effect on a human cancer cell line grown as a xenograft in severe combined immunodeficiency mice.
A new murine IgG 1 anti-Tn monoclonal antibody with in vivo anti-tumor activity
The Tn antigen (GalNAc α-O-Ser/Thr) is heterogeneously synthesized by a variety of tumors and contains an epitope defined by lectins and antibodies as a cluster of αGalNAc carbohydrates synthesized
Production of a mouse monoclonal IgM antibody that targets the carbohydrate Thomsen-nouveau cancer antigen resulting in in vivo and in vitro tumor killing
TLDR
Kt-IgM-8 is effective in killing tumor cells at 30% cytotoxicity, and furthermore, it demonstrated approximately 40% reduction in tumor growth in the MCF-7 model.
Identification of Tn Antigen O-GalNAc-expressing glycoproteins in human carcinomas using novel anti-Tn recombinant antibodies.
TLDR
Rec recombinant Remab6 and ReBaGs6 are useful for biochemical characterization of cancer cells and IHC of tumors, and represent promising tools for Tn biomarker discovery independently of recognition of IgA1.
Renewed interest in basic and applied research involving monoclonal antibodies against an oncofetal Tn-antigen.
TLDR
The recent studies demonstrated that MLS128 significantly inhibits breast and colon cancer cell growth and Thermodynamic studies on MLS128 binding to Tn2/Tn3 revealed its unique nature of temperature-dependent binding.
Analysis of Tn antigenicity with a panel of new IgM and IgG1 monoclonal antibodies raised against leukemic cells.
TLDR
Tn antigen-Ab binding capacity is determined by the peptide context of the Tn antigen, antigenic specificity of the Ab and class of the immunoglobulin, which can be particularly interesting for the application in leukemia diagnostics and therapy.
A newly generated functional antibody identifies Tn antigen as a novel determinant in the cancer cell–lymphatic endothelium interaction
TLDR
Highly reactive monoclonal antibodies against Tn making use of synthetically produced Tn are produced and tested for in vivo imaging as well as to define their potential functional activity in tumor cell spread to suggest a novel involvement of Tn in the lymphatic dissemination of cancer cells.
Monoclonal antibodies toward different Tn-amino acid backbones display distinct recognition patterns on human cancer cells. Implications for effective immuno-targeting of cancer
TLDR
Using synthetic Tn-based vaccines, a panel of anti-Tn monoclonal antibodies is generated and it is found that the recog- nition of these glycopeptides by some of these MAbs was strongly affected by the Tn backbone, such as a S*S-S*S* specific MAb (15G9) which failed to recognize a S-T-T*T* or a T*T*,T* structure.
Monoclonal antibodies toward different Tn-amino acid backbones display distinct recognition patterns on human cancer cells. Implications for effective immuno-targeting of cancer
TLDR
An immunohistochemical analysis of human tumors showed the existence of different recognition profiles among the five antibodies evaluated, demonstrating that the aglyconic part of the Tn structure (Ser vs Thr) plays a key role in the anti-Tn specificity for breast and colon cancer detection.
Isolation and characterization of antibodies against three consecutive Tn-antigen clusters from a phage library displaying human single-chain variable fragments.
TLDR
The production of human anti-Tn-antigen antibodies with specificity similar to that of MLS128 monoclonal antibody demonstrated the potential for use of these scFvs in developing antibody therapeutics targeting colon and breast cancer.
...
1
2
3
...

References

SHOWING 1-10 OF 59 REFERENCES
Immunoglobulin G3 monoclonal antibody directed to Tn antigen (tumor-associated alpha-N-acetylgalactosaminyl epitope) that does not cross-react with blood group A antigen.
An IgG3 monoclonal antibody (CU-1) directed to the Tn glycoprotein antigen, which does not cross-react with blood group A antigen, has been established after immunization of mice with a purified Tn
Production and functional characterization of two mouse/human chimeric antibodies with specificity for the tumor-associated Tn-antigen.
TLDR
Two functional mouse/human chimeric antibodies are constructed by inserting genomic DNA fragments encoding VH and Vkappa variable regions of the murine monoclonal antibody IgMK-83D4 into mammalian expression vectors containing human mu, gamma1, and kappa constant exons, and by transfecting them into the nonsecreting mouse myeloma X-63 cell line.
Immunoreactivities of polyclonal and monoclonal anti‐T and anti‐Tn antibodies with human carcinoma cells, grown in vitro and in a xenograft model
TLDR
The results suggest the feasibility of utilizing these antibodies in immunotherapy and drug targeting, as well as suggesting the effect on viability was shown to be complement‐independent, yet it was profoundly influenced by the concentration of the serum added to the assay medium.
Blood group A cross-reacting epitope defined by monoclonal antibodies NCC-LU-35 and -81 expressed in cancer of blood group O or B individuals: its identification as Tn antigen.
TLDR
The epitope of the mucin-like glycoprotein has been identified as alpha-N-acetylgalactosaminyl residue directly linked O-glycosidically to serine or threonine residues of polypeptides, which may be one of the tumor-associated A cross-reacting antigens occurring in a wide variety of human adenocarcinomas of hosts belonging to all ABO blood groups.
Tumor-Associated Antigen Recognized by the 22-1-1 Monoclonal Antibody Encourages Colorectal Cancer Progression under the Scanty CD8+ T Cells
TLDR
Tn may encourage invasion and innidiation through a mechanism independent of CD8+ T cells in tumor progression and is a risk factor for multiple liver metastases development and an independent negative prognostic factor for colorectal cancer.
A monoclonal antibody directed to Tn antigen.
TLDR
Special non-sialylated GalNAc residue(s) attached to a certain peptide region in the antigens seems to be involved in the binding since N-acetylgalactosaminidase treatment of the antigen abolished the binding and pronase digestion diminished the binding markedly.
A Fully Synthetic Therapeutic Vaccine Candidate Targeting Carcinoma-Associated Tn Carbohydrate Antigen Induces Tumor-Specific Antibodies in Nonhuman Primates
TLDR
The preclinical evaluation of the MAG:Tn vaccine demonstrates that it represents a safe and highly promising immunotherapeutic molecularly defined tool for targeting breast, colon, and prostate cancers that express the carbohydrate Tn antigen.
Anti-Tumor Immunity Provided by a Synthetic Multiple Antigenic Glycopeptide Displaying a Tri-Tn Glycotope1
TLDR
Both the clustering of carbohydrate Ags and the way they are displayed seem to be important parameters for stimulating efficient anti-saccharide immune responses.
Dissection and optimization of immune effector functions of humanized anti-ganglioside GM2 monoclonal antibody.
TLDR
Results show that the humanized KM8969, having the optimized immune effector functions and theoretically minimal immunogenicity, is an ideal candidate to test the effectiveness of anti-GM2 MAb in human cancer therapy.
Characterization of a CD43/Leukosialin-mediated Pathway for Inducing Apoptosis in Human T-Lymphoblastoid Cells*
TLDR
The existence of a tightly regulated CD43-mediated pathway for inducing apoptosis in human T-cell lineages is demonstrated, since peripheral blood T-lymphocytes express cryptic epitopes for mAb J393.
...
1
2
3
4
5
...