Abstract
We report a new tumor-directed immunoRNase, a chimeric protein made up of an antibody fragment (single-chain Fv fragment) directed to ErbB2, a cell surface receptor, and a non-toxic, human ribonuclease, which upon cell internalization becomes cytotoxic. The immunoRNase is active as a ribonuclease, specifically binds and selectively kills ErbB2-positive cells. ErbB2 is one of the most specific tumor-associated antigens identified so far, overexpressed on tumor cells of different origin. Its choice as target antigen and that of a non-toxic, human RNase as the killer moiety makes this immunoRNase a new, potentially attractive anticancer agent.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Antigens, Neoplasm / genetics
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Antigens, Neoplasm / metabolism
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Antineoplastic Agents / chemistry
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Antineoplastic Agents / pharmacology
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Cell Survival / drug effects
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Cell Survival / genetics
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Gene Expression
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Genes, erbB-2*
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Humans
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Immunoconjugates / chemistry
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Immunoconjugates / genetics
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Immunoconjugates / pharmacology*
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Receptor, ErbB-2 / genetics
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Receptor, ErbB-2 / metabolism
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / pharmacology
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Ribonucleases / chemistry
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Ribonucleases / genetics
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Ribonucleases / pharmacology*
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Tumor Cells, Cultured
Substances
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Antigens, Neoplasm
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Antineoplastic Agents
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Immunoconjugates
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Recombinant Fusion Proteins
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Receptor, ErbB-2
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Ribonucleases