Polynucleotide: adenosine glycosidase activity of immunotoxins containing ribosome-inactivating proteins. 2000

L Barbieri, and A Bolognesi, and P Valbonesi, and L Polito, and F Olivieri, and F Stirpe
Dipartimento di Patologia Sperimentale dell'Università degli Studi di Bologna, Via San Giacomo 14, I-40126 Bologna, Italy.barbieri@alma.unibo.it

Polynucleotide:adenosine glycosidases (rRNA N-glycosidases, EC 3.2.2.22, more commonly known as ribosome-inactivating proteins, RIP) are a numerous family of plant and bacterial enzymes, shown to release also adenine from DNA in vitro. They are well suited for the preparation of specifically toxic conjugates with several carriers, including monoclonal antibodies (immunotoxins). Here we show that (i) immunotoxins containing various PNAG (dianthin, gelonin, momordin I, PAP-S, PDS-2, ricin A-chain, saporin-L1, saporin-S6) all act on DNA; (ii) activity on DNA in vitro is less compromised by disulphide linkage to antibody than is inhibition of cell-free protein translation; and (iii) specific cytotoxicity of immunotoxin does not correlate with substrate specificity.

UI MeSH Term Description Entries
D009699 N-Glycosyl Hydrolases A class of enzymes involved in the hydrolysis of the N-glycosidic bond of nitrogen-linked sugars. Glycoside Hydrolases, Nitrogen-linked,Hydrolases, N-Glycosyl,Nucleosidase,Nucleosidases,Nucleoside Hydrolase,Nitrogen-linked Glycoside Hydrolases,Nucleoside Hydrolases,Glycoside Hydrolases, Nitrogen linked,Hydrolase, Nucleoside,Hydrolases, N Glycosyl,Hydrolases, Nitrogen-linked Glycoside,Hydrolases, Nucleoside,N Glycosyl Hydrolases,Nitrogen linked Glycoside Hydrolases
D010940 Plant Proteins Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which PLANT PROTEINS, DIETARY is available. Plant Protein,Protein, Plant,Proteins, Plant
D011500 Protein Synthesis Inhibitors Compounds which inhibit the synthesis of proteins. They are usually ANTI-BACTERIAL AGENTS or toxins. Mechanism of the action of inhibition includes the interruption of peptide-chain elongation, the blocking the A site of ribosomes, the misreading of the genetic code or the prevention of the attachment of oligosaccharide side chains to glycoproteins. Protein Synthesis Antagonist,Protein Synthesis Antagonists,Protein Synthesis Inhibitor,Antagonist, Protein Synthesis,Antagonists, Protein Synthesis,Inhibitor, Protein Synthesis,Inhibitors, Protein Synthesis,Synthesis Antagonist, Protein,Synthesis Inhibitor, Protein
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D004247 DNA A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine). DNA, Double-Stranded,Deoxyribonucleic Acid,ds-DNA,DNA, Double Stranded,Double-Stranded DNA,ds DNA
D004305 Dose-Response Relationship, Drug The relationship between the dose of an administered drug and the response of the organism to the drug. Dose Response Relationship, Drug,Dose-Response Relationships, Drug,Drug Dose-Response Relationship,Drug Dose-Response Relationships,Relationship, Drug Dose-Response,Relationships, Drug Dose-Response
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000076985 Saporins Type 1 ribosome-inactivating proteins derived from SAPONARIA OFFICINALIS that function through endohydrolysis of the N-glycosidic bond at single ADENOSINE residues of 28S RIBOSOMAL RNA. They are used as IMMUNOTOXINS. RIP Ribosome-Inactivating Protein,Ribosome-Inactivating Protein,SAP5 Protein,SAP6 Protein,Saporin,Saporin 5 Protein,Saporin 6 Protein,Saporin Protein,Saporin-S9 Protein,Protein, RIP Ribosome-Inactivating,RIP Ribosome Inactivating Protein,Ribosome Inactivating Protein,Ribosome-Inactivating Protein, RIP,Saporin S9 Protein
D000225 Adenine A purine base and a fundamental unit of ADENINE NUCLEOTIDES. Vitamin B 4,4, Vitamin B,B 4, Vitamin

Related Publications

L Barbieri, and A Bolognesi, and P Valbonesi, and L Polito, and F Olivieri, and F Stirpe
January 1988, Cancer treatment and research,
L Barbieri, and A Bolognesi, and P Valbonesi, and L Polito, and F Olivieri, and F Stirpe
September 1989, The Biochemical journal,
L Barbieri, and A Bolognesi, and P Valbonesi, and L Polito, and F Olivieri, and F Stirpe
September 1992, Clinical and experimental immunology,
L Barbieri, and A Bolognesi, and P Valbonesi, and L Polito, and F Olivieri, and F Stirpe
March 2012, Applied biochemistry and biotechnology,
L Barbieri, and A Bolognesi, and P Valbonesi, and L Polito, and F Olivieri, and F Stirpe
November 2000, Journal of biochemistry,
L Barbieri, and A Bolognesi, and P Valbonesi, and L Polito, and F Olivieri, and F Stirpe
February 1996, International journal of cancer,
L Barbieri, and A Bolognesi, and P Valbonesi, and L Polito, and F Olivieri, and F Stirpe
August 2000, British journal of haematology,
L Barbieri, and A Bolognesi, and P Valbonesi, and L Polito, and F Olivieri, and F Stirpe
November 1996, International journal of cancer,
L Barbieri, and A Bolognesi, and P Valbonesi, and L Polito, and F Olivieri, and F Stirpe
May 1998, Biochimica et biophysica acta,
L Barbieri, and A Bolognesi, and P Valbonesi, and L Polito, and F Olivieri, and F Stirpe
April 2024, Toxins,
Copied contents to your clipboard!