Ribosome–inactivating proteins (RIPs) do as their name suggests: they inactivate the ribosomes crucial to protein synthesis at the cellular level, ultimately killing cells. While some are extremely toxic, ricin being the consummate example, most RIPs are not and have been found useful in a number of medical and research applications such as in cancer and neurological research.
Ribosome–Inactivating Proteins: Ricin and Related Proteins provides up–to–date information on all aspects of this broad–ranging family of proteins. The text includes comprehensive coverage of RIPs, providing detail on their distribution in nature, chemical structure, genetics, and chemical and immunological properties. The book also describes mechanistic aspects, including the enzymatic activity on various polynucleotide substrates; the interaction with and entry into cells; the toxicity to animals, pathology of poisoning; and the immunomodulatory and allergenic activity.
Ribosome–Inactivating Proteins: Ricin and Related Proteins covers biological activities with potential applications in research in biology, medicine, and applied sciences; antiviral and insecticidal properties; and the conjugates of RIPs as immunotoxins and with other carriers capable of directing them toward specific target cells. Emphasis is given to the use of immunotoxins and other conjugates in clinical trials for the therapy of cancer and intractable pain. Finally, the possible uses of toxic RIPs for criminal uses and as biological weapons for warfare and terrorist attacks are summarized.
- Covers the use of RIPs in human therapies, such as targeted tumor treatment and pain management.
- Chapters on RIP activities as they relate to applications in research, agriculture, and medicine.
- Includes chapters on RIP antiviral properties, insecticidal properties, and use in neuroscience research.
- Describes the unique characteristics of RIPs in various plant families.
- Concluding section with a timely discussion of RIPs as bioweapons.
1 Introduction and History 1Fiorenzo Stirpe
2 Occurrence and Taxonomical Distribution of Ribosome–inactivating Proteins Belonging to the Ricin/Shiga Toxin Superfamily 11Chenjing Shang, Willy J. Peumans, and Els J. M. Van Damme
3 Ribosome–inactivating Proteins from Phytolaccaceae 28Augusto Parente, Angela Chambery, Antimo Di Maro, Rosita Russo, and Valeria Severino
4 Ribosome–inactivating Proteins in Caryophyllaceae, Cucurbitaceae, and Euphorbiaceae 44Tzi Bun Ng and Jack Ho Wong
5 Non–toxic Type 2 Ribosome–inactivating Proteins 67Pilar Jiménez, Manuel José Gayoso, and Tomás Girbés
6 The Intracellular Journey of Type 2 Ribosome–inactivating Proteins 83Robert A. Spooner and J. Michael Lord
7 Shiga Toxins: The Ribosome–inactivating Proteins from Pathogenic Bacteria 97Maurizio Brigotti
8 The Structure and Action of Ribosome–inactivating Proteins 111Jon D. Robertus and Arthur F. Monzingo
9 Updated Model of the Molecular Evolution of RIP Genes 134Willy J Peumans, Chenjing Shang, and Els J. M. Van Damme
10 Enzymology of the Ribosome–inactivating Proteins 151Yaeta Endo
11 A Long Journey to the Cytosol: What do We Know about Entry of Type 1 RIPs Inside a Mammalian Cell? 161Rodolfo Ippoliti and Maria Serena Fabbrini
12 Ribosome–inactivating Proteins: Pathology from Cells to Organs 178Gareth D. Griffiths
13 Antiviral and Antifungal Properties of RIPs 198Gabriela Krivdova, Kira C. M. Neller, Bijal A. Parikh, and Katalin A. Hudak
14 Insecticidal and Antifungal Activities of Ribosome–inactivating Proteins 212Lúcia Rosane Bertholdo Vargas and Célia Regina Carlini
15 Immunology of RIPs and their Immunotoxins 223Giulio Fracasso and Marco Colombatti
16 Ribosome–inactivating Proteins in Cancer Treatment 244Douglas A. Lappi and Fiorenzo Stirpe
17 Nervous System Research with RIP Conjugates: From Determination of Function to Therapy 253Douglas A. Lappi, Jack Feldman, Dale Sengelaub, and Jill McGaughy
18 Embryotoxic and Abortifacient Activities of Ribosome–inactivating Proteins 270Wood Yee Chan, Jack Ho Wong, and Tzi Bun Ng
19 The Potential for Misuse of Ribosome–inactivating Proteins 281Gareth D. Griffiths
Color plates appear between pages 116 and 117