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3. A dimeric mutant of human pancreatic ribonuclease with selective cytotoxicity toward malignant cells

Author

Daniela Spalletti-Cernia, Giuseppe D'Alessio, Renata Piccoli, Michela Grauso, Jaroslav Cinátl, Carmen Monaco, Sonia Di Gaetano, Claudia De Lorenzo, Paolo Laccetti, Josef Matoušek, Piccoli, R., DI GAETANO, S., DE LORENZO, C., Grauso, M., Monaco, C., SPALLETTI CERNIA, D., Laccetti, Paolo, Cinatl, J., Matousek, J., D'Alessio, G., Piccoli, Renata, and Laccetti, P.

Subjects
Male, Cell Survival, RNase P, Molecular Sequence Data, Mutant, Antineoplastic Agents, Apoptosis, 3T3 cells, Mice, Ribonucleases, Tumor Cells, Cultured, medicine, Animals, Humans, Cytotoxic T cell, Amino Acid Sequence, Thyroid Neoplasms, Multidisciplinary, Sequence Homology, Amino Acid, biology, Seminal Vesicles, RNA, Biological activity, 3T3 Cells, Ribonuclease, Pancreatic, Biological Sciences, Molecular biology, Recombinant Proteins, Cell Transformation, Neoplastic, medicine.anatomical_structure, Mutagenesis, Site-Directed, biology.protein, Cattle, Pancreatic ribonuclease, Drug Screening Assays, Antitumor, Dimerization, Sequence Alignment
Abstract

Monomeric human pancreatic RNase, devoid of any biological activity other than its RNA degrading ability, was engineered into a dimeric protein with a cytotoxic action on mouse and human tumor cells, but lacking any appreciable toxicity on mouse and human normal cells. This dimeric variant of human pancreas RNase selectively sensitizes to apoptotic death cells derived from a human thyroid tumor. Because of its selectivity for tumor cells, and because of its human origin, this protein represents a potentially very attractive, novel tool for anticancer therapy.

Published
1999

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