Classification of Anti-CEA Monoclonal Antibodies

Corvalan, J. R. F.; Axton, C.A.; Brandon, D. R.; Smith, William K.; Woodhouse, Clive S.

doi:10.1016/b978-0-08-030764-0.50209-3

Cited by 16 publications

(15 citation statements)

References 4 publications

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“…However, all anti-CEA monoclonal antibodies will not be equally efficient for in vivo localization [2,8]. These differences may be due to different affinities of the antibodies [7] or reactivity with different epitopes of the CEA molecule and consequently different degrees of cross reactivity with non-specific cross reacting antigen (NCA) and granulocyte glycoproteins [3,9,17,22]. In addition different antibodies may show variations in in vivo survival and kinetics of tumour localization [2,8].…”

Section: Introductionmentioning

confidence: 99%

Localization of an anti-CEA monoclonal antibody in colo-rectal carcinoma xenografts

Pimm

Armitage

Perkins

et al. 1985

Cancer Immunol Immunother

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Section: Introductionmentioning

confidence: 99%

Localization of an anti-CEA monoclonal antibody in colo-rectal carcinoma xenografts

Pimm

Armitage

Perkins

et al. 1985

Cancer Immunol Immunother

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“…The antibody 11.285.14 (IgG1) is specific for carcinoembryonic antigen (CEA) (Corvalan et al, 1984). The antibodies C154 and C161 were both prepared by immunization with human colon carcinoma subcellular membranes, and C161 is reactive with the normal cross-reacting antigen, NCA-1, while C154 reacts with a wide range of normal and tumour tissues (L. Durrantunpublished findings).…”

Section: Monoclonal Antibodiesmentioning

confidence: 99%

Epitope analysis of monoclonal antibody NCRC-11 defined antigen isolated from human ovarian and breast carcinomas

Price¹,

Edwards²,

Powell³

et al. 1986

Br J Cancer

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Summary NCRC-11 is an IgM monoclonal antibody which defines an antigen found in most epithelial malignancies. The antigen has previously been shown to be a high mol. wt. glycoprotein (>400,000) and in this study, antigen preparations were isolated by immunoadsorbent chromatography from ovarian mucinous and ovarian serous cyst adenocarcinoma and from breast carcinoma. Other monoclonal antibodies, against products in normal human milk, and antibodies of the Ca series (Bramwell et al., 1985) reacted with all three antigen preparations. Tests involving epitope mapping were performed to probe the relationships of the various epitopes to that defined by the NCRC-11 antibody, and, of note, the three antigen preparations from different tumour sources were remarkably similar with respect to their relative levels of epitope expression and to their topographical distribution of epitopes. The major differences in epitope expression could be attributed to the degree of sialylation in the three antigens. The antigens from ovarian tumours expressed I(Ma) blood group determinants (defined by the antibody LICR-LON-M18) which were partially masked by sialic acid. With NCRC-11 defined antigen from breast carcinoma, this determinant was totally masked by sialic acid although neuraminidase treatment clearly exposed epitopes reactive with M18 antibodies.

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“…Monoclonal antibodies were purified from ascitic fluids by their binding to and elution from Sepharose-protein A (Pharmacia, Uppsala, Sweden). The anti-CEA monoclonal antibody, 11.285.14 [4] was supplied as a gift from Lilly Research Centre, Ltd., Windlesham, UK.…”

Section: Methodsmentioning

confidence: 99%

Mapping of monoclonal antibody-defined epitopes associated with carcinoembryonic antigen, CEA

Price

Edwards

Jacobs

et al. 1987

Cancer Immunol Immunother

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Six immunoglobulin G monoclonal antibodies reactive with carcinoembryonic antigen (CEA) were evaluated with respect to parameters implicated in their potential diagnostic application and use as tumor targeting agents for cytotoxic drugs or plant or bacterial toxins. Antibody reactivity with surface antigens of the MKN-45 gastric tumor cell line was demonstrated by flow cytofluorimetry. In a subcellular membrane binding assay, each antibody reacted preferentially with membranes isolated from colorectal tumor tissue in comparison with their reaction with membranes from adjacent, apparently normal colonic mucosa. Three of the antibodies (NCRC-23, C228, and 11.285.14) reacted specifically with CEA with little or no reaction with the cross-reacting antigen, NCA. The remaining three antibodies (C24, C161, and C198) were reactive with both CEA and NCA. Analysis of the epitopes defined by these antibodies was performed by competitive binding inhibition assays evaluating the capacity of unlabeled antibodies to compete with 125I-labeled antibodies in their binding to CEA. In addition, double determinant or 'sandwich' radioimmunoassays were employed to examine the coexpression of epitopes on CEA molecules. These studies permitted an epitope map to be constructed which describes the coincidence, overlapping, or independent expression of both CEA specific epitopes and epitopes shared between CEA and NCA. The map may be employed for the selection of antibodies for diagnostic and therapeutic use.

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Classification of Anti-CEA Monoclonal Antibodies

Cited by 16 publications

References 4 publications

Localization of an anti-CEA monoclonal antibody in colo-rectal carcinoma xenografts

Localization of an anti-CEA monoclonal antibody in colo-rectal carcinoma xenografts

Epitope analysis of monoclonal antibody NCRC-11 defined antigen isolated from human ovarian and breast carcinomas

Mapping of monoclonal antibody-defined epitopes associated with carcinoembryonic antigen, CEA

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