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The Quarterly Journal of Nuclear Medicine 1999 June;43(2):132-9

Copyright © 2000 EDIZIONI MINERVA MEDICA

language: English

Effects of genetic engineering on the pharmacokinetics of antibodies

Colcher D.*, Goel A., Pavlinkova G., Beresford G., Booth B., Batra S. K.

From the Department of Pathology and Microbiology [DC, AG, GP, GB, BB] and Department of Biochemistry and Molecular Biology [SKB] University of Nebraska Medical Center, Omaha, USA


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Monoclonal anti­bod­ies (MAbs) may be con­sid­ered ‘mag­ic ­bullets’ due to ­their abil­ity to rec­og­nize and erad­i­cate malig­nant ­cells. MAbs, how­ev­er, ­have prac­ti­cal lim­i­ta­tions for ­their rap­id appli­ca­tion in the clin­ic. The struc­ture of anti­body mole­cules can be engi­neered to mod­i­fy func­tion­al ­domains ­such as anti­gen-bind­ing ­sites and/or effec­tor func­tions. Advances in genet­ic engi­neer­ing ­have pro­vid­ed rap­id ­progress in the devel­op­ment of new immu­no­glob­u­lin con­structs of MAbs ­with ­defined ­research and ther­a­peu­tic appli­ca­tion. Recombinant anti­body con­structs are ­being engi­neered, ­such as ­human-­mouse chi­mer­ic, ­domain-dis­po­si­tioned, ­domain-delet­ed, human­ized and sin­gle-­chain Fv frag­ments. Genetically-engi­neered anti­bod­ies dif­fer in ­size and ­rate of catab­o­lism. Pharmacokinetic stud­ies ­show ­that the ­intact IgG (150 kD), enzy­mat­i­cal­ly ­derived frag­ments Fab’ (50 kD) and sin­gle ­chain Fv (28 kD) ­have dif­fer­ent clear­ance ­rates. These anti­body ­forms ­clear 50% ­from the ­blood ­pool in 2.1 ­days, 30 min­utes and 10 min­utes, respec­tive­ly. Genetically-engi­neered anti­bod­ies ­make a new ­class of immu­no­ther­a­peu­tic trac­ers for can­cer treat­ment.

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