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- W2802910367 abstract "ImmunoRNases combine tumor targeting by antibodies with the cytotoxic action of ribonucleases from the RNase A superfamily. This study investigated for the first time all catalytic active human RNase A family members (1 to 8) as effector components of antibody fusion proteins. ImmunoRNase fusion pr oteins were constructed using the CD30-specific bivalent recombinant scFv-Fc antibody SH313-B5. Production of the resulting entirely human immunoRNases 1 to 8 was done in mammalian cells by secretion of active forms. The immunoRNases mediated CD30-specific cell binding and showed ribonucleolytic activity. Interestingly, immunoRNases 1 and 2 were active in the presence of up to 5-/20-fold molar excess of the pancreatic RNase inhibitor (RI), which is supposed to efficiently inhibit all human RNase A activity. ImmunoRNases 3, 4, 6 and 7 were only inhibited by several fold molar excess of RI, whereas immunoRNases 5 and 8 were already completely inactive at equimolar RI concentrations. Compared to free RNases, activity and RI sensitivity were not significantly changed by antibody fusion or dimerisation. ImmunoRNase3 and 5 mediated tumor growth inhibition at low nanomolar concentrations. Anti-tumor activity was antigen-specific and did not show any correlation with ribonucleolytic activity or RI sensitivity." @default.
- W2802910367 created "2018-05-17" @default.
- W2802910367 creator A5002473845 @default.
- W2802910367 creator A5043280562 @default.
- W2802910367 creator A5088227068 @default.
- W2802910367 date "2018-08-20" @default.
- W2802910367 modified "2023-09-23" @default.
- W2802910367 title "Antibody fusion proteins with human ribonucleases 1 to 8" @default.
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- W2802910367 doi "https://doi.org/10.3233/hab-180337" @default.
- W2802910367 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29689715" @default.
- W2802910367 hasPublicationYear "2018" @default.
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