Radiolabeled monoclonal antibody B72.3 localization in metastatic lesions of colorectal cancer patients

Colcher, David; Carrasquillo, Jorge A.; Esteban, José M.; Sugarbaker, Paul H.; Reynolds, James C.; Siler, Kathleen; Bryant, G.; Larson, Steven M.; Schlom, Jeffrey

doi:10.1016/0883-2897(87)90049-3

Cited by 25 publications

(26 citation statements)

References 21 publications

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“…The mucin was then eluted with 0.05 M sodium phosphate, plH 7.2, containing 5 M sodium chloride. After extensive dialysis the material was lyophilized and the homogeneity examined by polyacrylamide gel electrophoresis in a 4%/7.5% discontinuous gel (Weber and Osborn, 1969), with silver staining for protein and carbohydrate (Dubray and Bezard, 1982). Immunlostaining of mucin was performed in situ as follows.…”

Section: Preparation Of Mucinsmentioning

confidence: 99%

Characterization of monoclonal antibody PAM4 reactive with a pancreatic cancer mucin

Gold

Lew

Maliniak

et al. 1994

Intl Journal of Cancer

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A monoclonal antibody (MAb), PAM4, having reactivity with pancreatic carcinoma has been developed. PAM4 is an IgG1 immunoglobulin produced by immunization of mice with mucin purified from the xenografted RIP1 human pancreatic carcinoma. An immunohistochemical study of normal adult tissues showed the PAM4 reactive epitope to be restricted to the gastrointestinal tract and absent from normal pancreas. In neoplastic tissue, PAM4 was reactive with 85% of the pancreatic carcinomas, approximately half of the colon cancers and none of the breast, ovarian, prostate, renal and liver cancers. PAM4 was, in general, non-reactive with pancreatitis specimens whereas CA19.9 and DUPAN2 were strongly reactive with each one. Treatment of the mucin antigen by heating, reduction of disulfide bonds, or protease digestion abolished immunoreactivity with PAM4. Treatment of the mucin by neuraminidase or periodate oxidation reduced immunoreactivity but did not completely abolish it. Our data are consistent with the proposal that the PAM4 epitope is a conformationally dependent peptide epitope and that certain carbohydrate structures are necessary in order to maintain the correct peptide conformation. The high specificity and intense reactivity of PAM4 with pancreatic carcinoma tissue suggests that the antibody may prove useful for in vitro diagnostic assays as well as in vivo targeting of diagnostic and therapeutic agents.

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Section: Preparation Of Mucinsmentioning

confidence: 99%

Characterization of monoclonal antibody PAM4 reactive with a pancreatic cancer mucin

Gold

Lew

Maliniak

et al. 1994

Intl Journal of Cancer

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“…We have therefore focused on introducing an O-glycosyl moiety synthetically to b-peptides, mainly using the monosaccharide N-acetyl-galactosamine (GalNAc) as a glycosyl donor (Norgren and Arvidsson, 2005). In combination with either serine (Ser) or threonine (Thr), this residue represents the tumor-associated Tnantigen, found in human colon cancer, ovarian cancer, and breast cancer (Itzkowitz et al, 1989;Springer, 1995;Colcher et al, 1987;Gallinger et al, 1993) as well as a residue found in the envelope glycoprotein gp120 of the human immunodeficiency virus (HIV) (Hansen et al, 1990;Hansen et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

Biomolecular recognition of glycosylated β³‐peptides by GalNAc specific lectins

Norgren

Geitmann

Danielson

et al. 2007

J of Molecular Recognition

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The molecular recognition of a novel kind of hybrid conjugates, composed of artificial biomimetic beta-peptide oligomers with an O-linked natural N-acetyl-galactosamine (the Tn-antigen) residue, by four different GalNAc specific lectins was investigated using surface plasmon biosensor technology. The influence of the peptide and the glycosyl moiety on the recognition was studied using two glycosylated beta(3)-heptapeptides, a glycosylated alpha-heptapeptide, two beta-amino acid containing dipeptides, and monomeric alphaGalNAc-O-Thr. Although all four lectins displayed a decreased affinity for the carbohydrate residue when attached to a peptide, as compared to the monomeric Tn-antigen, the peptide part was found to have distinct effects on the binding kinetics-indicating that varying degrees of protein-peptide interactions occurred in the recognition process. Likewise, the lectins did not discriminate between beta(3)-peptides and the alpha-peptide, but the beta-linkage of the galactose had a detrimental effect for at least two of the lectins.

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“…A much slower loss of labelled antibodies from tumor sites as compared to non-specific sites has been documented in both animals and humans (Colcher et al, 1984(Colcher et al, , 1987. Surgical specimens removed 10-20 days after administration still bear evidence of antibody with very high selectivity for tumor cells.…”

mentioning

confidence: 95%

In vivo labelling of biotinylated monoclonal antibodies by radioactive avidin: A strategy to increase tumor radiolocalization

Paganelli

Riva

Deleide³

et al. 1988

Int. J. Cancer

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Several monoclonal antibodies (MAbs), reactive with tumor-associated antigens, selectively persist on tumor sites in vivo for many days. If biotinylated, such highly specific tags on tumor cells could become targets for radioactive avidin, administered after suitable intervals. The proposed strategy is based on a number of assumptions concerning the ability of avidin t o preserve i t s biological properties in heterologous in vivo environments, on i t s lack of toxicity and on i t s biodistribution. A preliminary study has been carried out in rabbits, using biotinylated nitrocellulose and polystyrene targets. The results of this study indicate that in rabbits I ) avidin can be administered i.v. and i.p. without adverse reactions, 2) it does not show any preferential localization, 3) it is eliminated with a biological half-life of 24 hr, 4) i t s biological properties are not impaired by in vivo conditions, since it accumulates at biotinylated targets only, 5) CEA-bearing targets can be biotinylated in vivo by biotin-labelled anti-CEA MAbs and 6) the biotin-avidin chain can be further extended in vivo since bound avidin is still able t o bind biotinylated radioactive proteins.Several MAbs used in immunoscintigraphy of human tumors persist a long time on the surface of tumors, giving the best localization ratios at 72-96 hr after their administration (e.g., Buraggi et al., 1987). A much slower loss of labelled antibodies from tumor sites as compared to non-specific sites has been documented in both animals and humans (Colcher et al., 1984(Colcher et al., , 1987. Surgical specimens removed 10-20 days after administration still bear evidence of antibody with very high selectivity for tumor cells. Although these antibodies represent a very minute fraction of the injected dose, they can effectively tag the tumor if they are labelled with long-lived isotopes, such as 1251, a property that has been exploited to develop radio-immuno-guided surgery (Martin et al., 1985).Our purpose was to develop a method to post-label anti-tumor MAbs in vivo, exploiting their differential persistence at tumor sites. Our strategy is to biotinylate MAbs, to inject them cold and to leave an appropriate interval before the administration of radioactive avidin. The aim of the study is to evaluate if the very high affinity and specificity of the avidin-biotin reaction (Green, 1975) can be exploited in vivo in laboratory animals, as it has been widely exploited in vitro in a variety of diagnostic applications. MATERIAL AND METHODS Material and animalsImmuno-affinity-purified CEA from an hepatic metastasis, MAb F023C5 (reactive with a protein epitope of CEA) and F023C5-coated beads were from SORIN Biomedica. Pure hen egg avidin and biotinyl-eaminocaproic acid Nhydroxysuccinimide ester and MAb L16B8 (reactive with hen egg lysozyme) were from Societh Prodotti Antibiotici. Na13'I (specific activity 16 Ci/mol) and ' "InC13 were purchased from ORIS/CEA, Saclay (France) and Amersham (UK), respectively. Outbred rabbits were used for all experiments. Dep...

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Radiolabeled monoclonal antibody B72.3 localization in metastatic lesions of colorectal cancer patients

Cited by 25 publications

References 21 publications

Characterization of monoclonal antibody PAM4 reactive with a pancreatic cancer mucin

Characterization of monoclonal antibody PAM4 reactive with a pancreatic cancer mucin

Biomolecular recognition of glycosylated β³‐peptides by GalNAc specific lectins

In vivo labelling of biotinylated monoclonal antibodies by radioactive avidin: A strategy to increase tumor radiolocalization

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Radiolabeled monoclonal antibody B72.3 localization in metastatic lesions of colorectal cancer patients

Cited by 25 publications

References 21 publications

Characterization of monoclonal antibody PAM4 reactive with a pancreatic cancer mucin

Characterization of monoclonal antibody PAM4 reactive with a pancreatic cancer mucin

Biomolecular recognition of glycosylated β3‐peptides by GalNAc specific lectins

In vivo labelling of biotinylated monoclonal antibodies by radioactive avidin: A strategy to increase tumor radiolocalization

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Biomolecular recognition of glycosylated β³‐peptides by GalNAc specific lectins