Different behaviour of mouse‐human chimeric antibody F(ab')2 fragments of IgG1, IgG2 and IgG4 sub‐class in vivo

Mouse‐human chimeric monoclonal antibodies (MAbs) of 3 different human IgG sub‐classes directed against carcinoembryonic antigen (CEA) have been produced in SP‐0 cells trans‐ fected with genomic chimeric DNA. F(ab')2 fragments were obtained by pepsin digestion of the purified chimeric MAbs of h...

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Veröffentlicht in:International journal of cancer 1992-02, Vol.50 (3), p.416-422
Hauptverfasser: Buchegger, Franz, Pèlegrin, Andre, Hardman, Norman, Heusser, Christoph, Lukas, John, Dolci, Wanda, Mach, Jean‐Pierre
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container_end_page 422
container_issue 3
container_start_page 416
container_title International journal of cancer
container_volume 50
creator Buchegger, Franz
Pèlegrin, Andre
Hardman, Norman
Heusser, Christoph
Lukas, John
Dolci, Wanda
Mach, Jean‐Pierre
description Mouse‐human chimeric monoclonal antibodies (MAbs) of 3 different human IgG sub‐classes directed against carcinoembryonic antigen (CEA) have been produced in SP‐0 cells trans‐ fected with genomic chimeric DNA. F(ab')2 fragments were obtained by pepsin digestion of the purified chimeric MAbs of human IgG1, IgG2 and IgG4 sub‐class and of parental mouse MAb IgG. The 4 F(ab')2 fragments exhibit similar molecular weight by SDS‐PAGE. They were labelled with 125I or 131I and high binding (80 to 87%) to purified unsolubilized CEA was observed. In vivo, double labelling experiments indicate that the longest biological half‐life and the highest tumour‐localization capacity is obtained with F(ab')2 from chimeric MAb of human IgG2 sub‐class, whereas F(ab')2 from chimeric MAb IgG4 give very low values for these 2 parameters. F(ab')2 from chimeric MAb IgG1 and from parental mouse MAb yield intermediate results in vivo. Our findings should help to select the appropriate human IgG sub‐class to produce chimeric or reshaped MAb F(ab')2 to be used for tumour detection by immunoscintigraphy and for radioimmunotherapy.
doi_str_mv 10.1002/ijc.2910500316
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F(ab')2 fragments were obtained by pepsin digestion of the purified chimeric MAbs of human IgG1, IgG2 and IgG4 sub‐class and of parental mouse MAb IgG. The 4 F(ab')2 fragments exhibit similar molecular weight by SDS‐PAGE. They were labelled with 125I or 131I and high binding (80 to 87%) to purified unsolubilized CEA was observed. In vivo, double labelling experiments indicate that the longest biological half‐life and the highest tumour‐localization capacity is obtained with F(ab')2 from chimeric MAb of human IgG2 sub‐class, whereas F(ab')2 from chimeric MAb IgG4 give very low values for these 2 parameters. F(ab')2 from chimeric MAb IgG1 and from parental mouse MAb yield intermediate results in vivo. Our findings should help to select the appropriate human IgG sub‐class to produce chimeric or reshaped MAb F(ab')2 to be used for tumour detection by immunoscintigraphy and for radioimmunotherapy.</description><subject>Animals</subject><subject>Antibodies, Monoclonal - chemistry</subject><subject>Antibodies, Monoclonal - genetics</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibody Affinity</subject><subject>Carcinoembryonic Antigen - immunology</subject><subject>Colonic Neoplasms - immunology</subject><subject>Humans</subject><subject>Immunoglobulin Fab Fragments - chemistry</subject><subject>Immunoglobulin Fab Fragments - immunology</subject><subject>Immunoglobulin G - genetics</subject><subject>Immunoglobulin G - immunology</subject><subject>Immunoglobulin G - metabolism</subject><subject>Mice</subject><subject>Mice, Nude</subject><subject>Neoplasm Transplantation</subject><subject>Recombinant Fusion Proteins - immunology</subject><subject>Structure-Activity Relationship</subject><issn>0020-7136</issn><issn>1097-0215</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFUctKAzEUDaLUWt26E7LyAU7NnUdillJtrRTc6Hq4ySRtZB510ql05yf4jX6JKRa6uQ_OA-49hJwDGwJj8Z370MNYAssYS4AfkD4wKSIWQ3ZI-oHAIgEJPyYn3n8wBpCxtEd6IJKMA_SJf3TWmtbUK6rMAteu6VraWFo1nTe_3z-LrsKa6oWrTOs0xXrlVFNs6Pga1dVNTG2L8yqo_VY0nU_gdlvjQCy2Q0p9p4KNLtF76mq6duvmlBxZLL052_UBeR8_vY2eo9nrZDp6mEVLEMAjQFmgUmmBOjXG8rjgXGeCocJ7K5AnoFIQWvGAWZ2lUoNMDEKijJXIIRmQy3_fZdt8dsav8sp5bcoSaxPOy0UsJLuXPBAvdsROVabIl62rsN3kuy8FXP7jX640mz3M8m0EeYgg30eQT19G-y35A4J8e8Y</recordid><startdate>19920201</startdate><enddate>19920201</enddate><creator>Buchegger, Franz</creator><creator>Pèlegrin, Andre</creator><creator>Hardman, Norman</creator><creator>Heusser, Christoph</creator><creator>Lukas, John</creator><creator>Dolci, Wanda</creator><creator>Mach, Jean‐Pierre</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19920201</creationdate><title>Different behaviour of mouse‐human chimeric antibody F(ab')2 fragments of IgG1, IgG2 and IgG4 sub‐class in vivo</title><author>Buchegger, Franz ; 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F(ab')2 fragments were obtained by pepsin digestion of the purified chimeric MAbs of human IgG1, IgG2 and IgG4 sub‐class and of parental mouse MAb IgG. The 4 F(ab')2 fragments exhibit similar molecular weight by SDS‐PAGE. They were labelled with 125I or 131I and high binding (80 to 87%) to purified unsolubilized CEA was observed. In vivo, double labelling experiments indicate that the longest biological half‐life and the highest tumour‐localization capacity is obtained with F(ab')2 from chimeric MAb of human IgG2 sub‐class, whereas F(ab')2 from chimeric MAb IgG4 give very low values for these 2 parameters. F(ab')2 from chimeric MAb IgG1 and from parental mouse MAb yield intermediate results in vivo. 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subjects Animals
Antibodies, Monoclonal - chemistry
Antibodies, Monoclonal - genetics
Antibodies, Monoclonal - immunology
Antibody Affinity
Carcinoembryonic Antigen - immunology
Colonic Neoplasms - immunology
Humans
Immunoglobulin Fab Fragments - chemistry
Immunoglobulin Fab Fragments - immunology
Immunoglobulin G - genetics
Immunoglobulin G - immunology
Immunoglobulin G - metabolism
Mice
Mice, Nude
Neoplasm Transplantation
Recombinant Fusion Proteins - immunology
Structure-Activity Relationship
title Different behaviour of mouse‐human chimeric antibody F(ab')2 fragments of IgG1, IgG2 and IgG4 sub‐class in vivo
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