[186Re]-labeled mouse and chimeric monoclonal antibody 323/A3: A comparison of the efficacy in experimental human ovarian cancer

Els Kievit; Frank B. Van Gog; Hennie M M Schlüper; Guus A M S Van Dongen; Herbert M. Pinedo; Epie Boven

doi:10.1016/S0969-8051(97)00154-6

[186Re]-labeled mouse and chimeric monoclonal antibody 323/A3: A comparison of the efficacy in experimental human ovarian cancer

Els Kievit, Frank B. Van Gog, Hennie M M Schlüper, Guus A M S Van Dongen, Herbert M. Pinedo, Epie Boven

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4 Scopus citations

Abstract

We have investigated whether [¹⁸⁶-Re]-labeled chimeric monoclonal antibody 323/A3 (MAb c-323/A3) is as effective as [¹⁸⁶Re]-labeled mouse 323/A3 (m-323/A3) in the growth inhibition of human ovarian cancer xenografts OVCAR-3 and FMa. [¹⁸⁶Re] was conjugated to MAbs with the use of the chelate S-benzoylmercaptoacetyltriglycine (S-benzoyl-MAG3). The maximum number of metal-MAG3 groups that could be conjugated to one MAb molecule accepting a minimal initial increase of the blood clearance (15%) was 8.5 and 2.9 for c-323/A3 and m-323/A3, respectively. With these molar ratios the immunoreactivity of both MAbs was maintained. An inverse relationship was observed between the protein dose of c-323/A3 and its blood clearance. Both [¹⁸⁶Re]-c-323/A3 and [¹⁸⁶Re]-m-323/A3 were comparable in the inhibition of the tumor growth when higher protein doses were used. Together with the expected lower immunogenicity, our results imply that c-323/A3 is preferable for use in [¹⁸⁶Re]-radioimmunotherapy in ovarian cancer patients.

Original language	English (US)
Pages (from-to)	37-45
Number of pages	9
Journal	Nuclear Medicine and Biology
Volume	25
Issue number	1
DOIs	https://doi.org/10.1016/S0969-8051(97)00154-6
State	Published - Jan 1998
Externally published	Yes

Keywords

[Re]
Mouse and Chimeric MAb 323/A3
Ovarian cancer
Radioimmunotherapy

ASJC Scopus subject areas

Cancer Research
Molecular Medicine
Radiology Nuclear Medicine and imaging

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title = "[186Re]-labeled mouse and chimeric monoclonal antibody 323/A3: A comparison of the efficacy in experimental human ovarian cancer",

abstract = "We have investigated whether [186-Re]-labeled chimeric monoclonal antibody 323/A3 (MAb c-323/A3) is as effective as [186Re]-labeled mouse 323/A3 (m-323/A3) in the growth inhibition of human ovarian cancer xenografts OVCAR-3 and FMa. [186Re] was conjugated to MAbs with the use of the chelate S-benzoylmercaptoacetyltriglycine (S-benzoyl-MAG3). The maximum number of metal-MAG3 groups that could be conjugated to one MAb molecule accepting a minimal initial increase of the blood clearance (15%) was 8.5 and 2.9 for c-323/A3 and m-323/A3, respectively. With these molar ratios the immunoreactivity of both MAbs was maintained. An inverse relationship was observed between the protein dose of c-323/A3 and its blood clearance. Both [186Re]-c-323/A3 and [186Re]-m-323/A3 were comparable in the inhibition of the tumor growth when higher protein doses were used. Together with the expected lower immunogenicity, our results imply that c-323/A3 is preferable for use in [186Re]-radioimmunotherapy in ovarian cancer patients.",

keywords = "[Re], Mouse and Chimeric MAb 323/A3, Ovarian cancer, Radioimmunotherapy",

author = "Els Kievit and {Van Gog}, {Frank B.} and Schl{\"u}per, {Hennie M M} and {Van Dongen}, {Guus A M S} and Pinedo, {Herbert M.} and Epie Boven",

year = "1998",

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doi = "10.1016/S0969-8051(97)00154-6",

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AU - Kievit, Els

AU - Van Gog, Frank B.

AU - Schlüper, Hennie M M

AU - Van Dongen, Guus A M S

AU - Pinedo, Herbert M.

AU - Boven, Epie

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N2 - We have investigated whether [186-Re]-labeled chimeric monoclonal antibody 323/A3 (MAb c-323/A3) is as effective as [186Re]-labeled mouse 323/A3 (m-323/A3) in the growth inhibition of human ovarian cancer xenografts OVCAR-3 and FMa. [186Re] was conjugated to MAbs with the use of the chelate S-benzoylmercaptoacetyltriglycine (S-benzoyl-MAG3). The maximum number of metal-MAG3 groups that could be conjugated to one MAb molecule accepting a minimal initial increase of the blood clearance (15%) was 8.5 and 2.9 for c-323/A3 and m-323/A3, respectively. With these molar ratios the immunoreactivity of both MAbs was maintained. An inverse relationship was observed between the protein dose of c-323/A3 and its blood clearance. Both [186Re]-c-323/A3 and [186Re]-m-323/A3 were comparable in the inhibition of the tumor growth when higher protein doses were used. Together with the expected lower immunogenicity, our results imply that c-323/A3 is preferable for use in [186Re]-radioimmunotherapy in ovarian cancer patients.

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[186Re]-labeled mouse and chimeric monoclonal antibody 323/A3: A comparison of the efficacy in experimental human ovarian cancer

Abstract

Keywords

ASJC Scopus subject areas

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