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1.
Toxins (Basel) ; 12(9)2020 08 25.
Article in English | MEDLINE | ID: mdl-32854372

ABSTRACT

Saporin, which is extracted from Saponaria officinalis, is a protein toxin that inactivates ribosomes. Saporin itself is non-selective toxin but acquires high specificity after conjugation with different ligands such as signaling peptides or antibodies to some surface proteins expressed in a chosen cell subpopulation. The saporin-based conjugated toxins were widely adopted in neuroscience as a convenient tool to induce highly selective degeneration of desired cell subpopulation. Induction of selective cell death is one of approaches used to model neurodegenerative diseases, study functions of certain cell subpopulations in the brain, and therapy. Here, we review studies where saporin-based conjugates were used to analyze cell mechanisms of sleep, general anesthesia, epilepsy, pain, and development of Parkinson's and Alzheimer's diseases. Limitations and future perspectives of use of saporin-based toxins in neuroscience are discussed.


Subject(s)
Biomedical Research/methods , Nervous System Diseases/drug therapy , Saponaria , Saporins/isolation & purification , Saporins/therapeutic use , Animals , Brain/drug effects , Brain/metabolism , Brain/pathology , Humans , Nervous System Diseases/diagnosis , Nervous System Diseases/metabolism , Saporins/metabolism , Spinal Cord/drug effects , Spinal Cord/metabolism , Spinal Cord/pathology
2.
Phytochemistry ; 170: 112190, 2020 Feb.
Article in English | MEDLINE | ID: mdl-31731237

ABSTRACT

Rice is the most important staple food in the world, but rice production is challenged by several biotic stress factors like viruses, bacteria, fungi and pest insects. One of the most notorious pest insects is Nilaparvata lugens, commonly known as the brown planthopper, which feeds on rice phloem sap and can cause serious damage to rice fields. In order to protect themselves, plants express a wide array of defense proteins such as ribosome-inactivating proteins (RIPs). This study shows that the expression of 'OsRIP1' is highly induced in rice plants infested with N. lugens, with transcript levels more than 100-fold upregulated in infested plants compared to non-infested plants. Furthermore, recombinant OsRIP1 was toxic for brown planthoppers when administered through liquid artificial diet. OsRIP1 inactivated insect ribosomes in vitro, suggesting that its toxicity relates to the enzymatic activity of OsRIP1. Over-expression of OsRIP1 in transgenic rice plants did not affect the performance of insects reared on these plants, most likely due to insufficient concentrations of OsRIP1 in the phloem. The data obtained in this research indicate that OsRIP1 can play a role in plant defense against herbivorous insects.


Subject(s)
Hemiptera/drug effects , Oryza/chemistry , Phytochemicals/pharmacology , Saporins/metabolism , Animals , Phytochemicals/chemistry , Phytochemicals/isolation & purification , Saporins/chemistry , Saporins/isolation & purification
3.
Phytochemistry ; 157: 121-127, 2019 Jan.
Article in English | MEDLINE | ID: mdl-30399494

ABSTRACT

Ribosome-inactivating proteins (RIPs) are enzymes with N-glycosylase activity that remove adenine bases from the ribosomal RNA. In theory, one single RIP molecule internalized into a cell is sufficient to induce cell death. For this reason, RIPs are of high potential as toxic payload for anti-tumor therapy. A considerable number of RIPs are synthesized by plants that belong to the carnation family (Caryophyllaceae). Prominent examples are the RIPs saporin from Saponaria officinalis L. or dianthin from Dianthus caryophyllus L. In this study, we have isolated and characterized a novel RIP (termed gypsophilin-S) from the tiny seeds of Gypsophila elegans M. Bieb. (Caryophyllaceae). It is noteworthy that this is the first study presenting the complete amino acid sequence of a RIP from a Gypsophila species. Gypsophilin-S was isolated from the defatted seed material following ammonium sulphate precipitation and HPLC-based ion exchange chromatography. Gypsophilin-S-containing fractions were analysed by SDS-PAGE and mass spectrometry. The full amino acid sequence of gypsophilin-S was assembled by MALDI-TOF-MS-MS and PCR. Gypsophilin-S exhibited strong adenine releasing activity and its cytotoxicity in human glioblastoma cells was investigated using an impedance-based real-time assay in comparison with recombinant saporin and dianthin.


Subject(s)
Antineoplastic Agents, Phytogenic/chemistry , Antineoplastic Agents, Phytogenic/pharmacology , Caryophyllaceae/enzymology , Saporins/chemistry , Saporins/pharmacology , Seeds/enzymology , Amino Acid Sequence , Antineoplastic Agents, Phytogenic/isolation & purification , Cell Line, Tumor , Humans , Models, Molecular , Protein Conformation , Saporins/isolation & purification
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