scholarly journals Ribosome-inactivating proteins from the seeds of Saponaria officinalis L. (soapwort), of Agrostemma githago L. (corn cockle) and of Asparagus officinalis L. (asparagus), and from the latex of Hura crepitans L. (sandbox tree)

1983 ◽  
Vol 216 (3) ◽  
pp. 617-625 ◽  
Author(s):  
F Stirpe ◽  
A Gasperi-Campani ◽  
L Barbieri ◽  
A Falasca ◽  
A Abbondanza ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Sugar Content ◽  
Asparagus Officinalis ◽  
Inhibit Protein Synthesis ◽  
Nicotiana Glutinosa ◽  
Ribosome Inactivating Proteins ◽  
Local Lesions ◽  
Hura Crepitans ◽  
Reticulocyte Lysate ◽  
Saponaria Officinalis

Ribosome-inactivating proteins, similar to those already known [Barbieri & Stirpe (1982) Cancer Surveys 1, 489-520] were purified from the seeds of Saponaria officinalis (two proteins), of Agrostemma githago (three proteins), and of Asparagus officinalis (three proteins), and from the latex of Hura crepitans (one protein). The yield ranged from 8 to 400 mg/100 g of starting material. All proteins have an Mr of approx. 30000 and an alkaline isoelectric point. Their sugar content varies from 0 (proteins from S. officinalis) to 40% (protein from H. crepitans). The ribosome-inactivating proteins inhibit protein synthesis by rabbit reticulocyte lysate, the ID50 (concentration giving 50% inhibition) ranging from 1 ng/ml (a protein from S. officinalis) to 18 ng/ml (a protein from A. githago). Those which were tested (the proteins from S. officinalis and from A. githago) also inhibit polymerization of phenylalanine by isolated ribosomes, acting in an apparently catalytic manner. The protein from H. crepitans inhibited protein synthesis by HeLa cells, with an ID50 of 4 micrograms/ml, whereas the proteins from S. officinalis and from A. githago had an ID50 of more than 50-100 micrograms/ml. The ribosome-inactivating proteins from S. officinalis and from A. githago reduced the number of local lesions by tobacco-mosaic virus in the leaves of Nicotiana glutinosa.

scholarly journals Bryodin, a ribosome-inactivating protein from the roots of Bryonia dioica L. (white bryony)

1986 ◽  
Vol 240 (3) ◽  
pp. 659-665 ◽  
Author(s):  
F Stirpe ◽  
L Barbieri ◽  
M G Battelli ◽  
A I Falasca ◽  
A Abbondanza ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Sugar Content ◽  
Neutral Sugar ◽  
Ribosome Inactivating Protein ◽  
Equimolar Ratio ◽  
Nicotiana Glutinosa ◽  
Whole Cells ◽  
Bryonia Dioica ◽  
Local Lesions ◽  
Reticulocyte Lysate

Bryodin is a strongly basic (pI greater than or equal to 9.5) glycoprotein (neutral sugar content 6.3%) with Mr 30,000, purified from the roots of Bryonia dioica (white bryony). This protein inhibits protein synthesis by a rabbit reticulocyte lysate with and ID50 (concentration causing 50% inhibition) of 0.12 nM (3.6 ng/ml) and has much less effect on protein synthesis by whole cells, with ID50 values ranging from 46 nM to 2.27 microM (1.4-67 micrograms/ml). Bryodin acts by inactivating ribosomes, with a less-than-equimolar ratio, which suggests a catalytic action. Bryodin decreases the number of local lesions induced by tobacco mosaic virus in the leaves of Nicotiana glutinosa. From all its properties, bryodin can be considered to be a ribosome-inactivating protein, similar to those already known [reviews: Barbieri & Stirpe (1982) Cancer Surveys 1, 489-520; Stirpe & Barbieri (1986) FEBS Lett. 195, 1-8].

scholarly journals Dianthins, ribosome-damaging proteins with anti-viral properties from Dianthus caryophyllus L. (carnation)

1981 ◽  
Vol 195 (2) ◽  
pp. 399-405 ◽  
Author(s):  
F Stirpe ◽  
D G Williams ◽  
L J Onyon ◽  
R F Legg ◽  
W A Stevens
Keyword(s):  
Protein Synthesis ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Dianthus Caryophyllus ◽  
Inhibit Protein Synthesis ◽  
Equimolar Ratio ◽  
Nicotiana Glutinosa ◽  
Intact Cells ◽  
Local Lesions ◽  
Rabbit Reticulocytes

1. Dianthin 30 and dianthin 32, two proteins isolated from the leaves of Diathus caryophyllus (carnation), were purified to homogeneity by chromatography on CM-cellulose. 2. The mol.wt. of dianthin 30 is 29 500 and that of dianthin 32 is 31 700. Both dianthins are glycoproteins containing mannose. 3. Dianthins inhibit protein synthesis in a lysate of rabbit reticulocytes, with an ID50 (concentration giving 50% inhibition) of 9.15 ng/ml (dianthin 30) and 3.6 ng/ml (dianthin 32). They act by damaging ribosomes in a less-than-equimolar ratio. Protein synthesis by intact cells is partially inhibited by dianthins at a concentration of 100 microgram/ml. 4. Dianthins mixed with tobacco-mosaic virus strongly decrease the number of local lesions on leaves of Nicotiana glutinosa.

Ribosome-inactivating proteins (RIPs) and their important health promoting property

RSC Advances ◽  
2016 ◽  
Vol 6 (52) ◽  
pp. 46794-46805 ◽  
Author(s):  
Shuzhen Wang ◽  
Zhiliang Li ◽  
Shiming Li ◽  
Rong Di ◽  
Chi-Tang Ho ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Large Subunit ◽  
Ribosomal Rnas ◽  
Inhibit Protein Synthesis ◽  
Ribosome Inactivating Proteins ◽  
Important Health ◽  
Health Promoting

Ribosome-inactivating proteins (RIPs), widely present in plants, certain fungi and bacteria, can inhibit protein synthesis by removing one or more specific adenine residues from the large subunit of ribosomal RNAs (rRNAs).

scholarly journals A Neutralizing Antibody to the A Chain of Abrin Inhibits Abrin Toxicity both In Vitro and In Vivo

2008 ◽  
Vol 15 (5) ◽  
pp. 737-743 ◽  
Author(s):  
Kalpana Surendranath ◽  
Anjali A. Karande
Keyword(s):  
Monoclonal Antibody ◽  
Protein Synthesis ◽  
Neutralizing Antibody ◽  
Type Ii ◽  
Inhibit Protein Synthesis ◽  
Ribosome Inactivating Proteins ◽  
A Chain ◽  
Lethal Doses

ABSTRACT Plant ribosome-inactivating proteins (RIPs) are RNA N-glycosidases that inhibit protein synthesis in cells. Abrin, a type II RIP, is an AB type toxin, which is one of the most lethal types of toxin known. The B chain facilitates the entry of the molecule into the cell, whereas the A chain exerts the toxic effect. We have generated hybridomas secreting antibodies of the immunoglobulin G class specific to the recombinant A chain of abrin. One monoclonal antibody, namely, D6F10, rescued cells from abrin toxicity. Importantly, the antibody also protected mice from lethal doses of the toxin. The neutralizing effect of the antibody was shown to be due to interference with abrin attachment to the cell surface.

scholarly journals Ribosome-inactivating proteins from plant cells in culture

1989 ◽  
Vol 257 (3) ◽  
pp. 801-807 ◽  
Author(s):  
L Barbieri ◽  
A Bolognesi ◽  
P Cenini ◽  
A I Falasca ◽  
A Minghetti ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Phytolacca Americana ◽  
Pokeweed Antiviral Protein ◽  
Antiviral Protein ◽  
Ribosome Inactivating Protein ◽  
Intact Cells ◽  
Ribosome Inactivating Proteins ◽  
Reticulocyte Lysate ◽  
Ic50 Concentration

1. Ribosome-inactivating proteins were found in high amounts in one line of cells of Phytolacca americana (pokeweed) cultured in vitro and, in less quantity, in lines of Saponaria officinalis (soapwort) and of Zea mays (corn) cells. 2. The main ribosome-inactivating protein from pokeweed cells was purified to homogeneity. It is a protein with Mr 29,000 and basic pI, similar to the ‘pokeweed antiviral protein’ (PAP), a ribosome-inactivating protein from pokeweed leaves. We propose to call the pokeweed antiviral protein isolated from pokeweed cells PAP-C. 3. PAP-C inactivates ribosomes in a less-than-equimolar ratio, thus inhibiting protein synthesis by a rabbit reticulocyte lysate with an IC50 (concentration causing 50% inhibition) of 0.067 nM (2 ng/ml), and modifies rRNA in a manner apparently identical to that of ricin and other ribosome-inactivating proteins. It inhibits protein synthesis by intact cells with an IC50 of 0.7-3.4 microM, and is toxic to mice with an LD50 of 0.95 mg/kg.

scholarly journals Purification and properties of two lectins from the latex of the euphorbiaceous plants Hura crepitans L. (sand-box tree) and Euphorbia characias L. (Mediterranean spurge)

1983 ◽  
Vol 215 (3) ◽  
pp. 433-439 ◽  
Author(s):  
L Barbieri ◽  
A Falasca ◽  
C Franceschi ◽  
F Licastro ◽  
C A Rossi ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
B Lymphocytes ◽  
Human Blood ◽  
Plant Family ◽  
Sand Box ◽  
Purification And Properties ◽  
Euphorbia Characias ◽  
Hura Crepitans ◽  
Haemagglutinating Activity ◽  
Reticulocyte Lysate

1. From the latex of two members of the plant family Euphorbiaceae, Hura crepitans L. (sand-box tree) and Euphorbia characias L. (Mediterranean spurge), two lectins were purified by affinity chromatography on acid-treated Sepharose 6B followed by elution with D-galactose. 2. The lectin from E. characias is a single molecular species with Mr 80 000, made up of two identical subunits with Mr 40 000, and is a glycoprotein containing 11% carbohydrate. 3. The lectin from H. creptians appears as a mixture of three isolectins with Mr 140 000, consisting of four different subunits with Mr values 37 500, 35 500, 31 000, and 29 000. 4. Both lectins have haemagglutinating activity, with no specificity for human blood groups. The haemagglutinating activity is inhibited by D-galactose and by galactose-containing oligosaccharides. 5. The lectin from H. crepitans is mitogenic to human T-, but not to B-, lymphocytes. The latex of E. characias is mitogenic to T- and, to a lesser extent, to B-, lymphocytes, but the purified E. characias lectin has no mitogenic activity. 6. The lectin from H. crepitans, but not that from E. characias, inhibits protein synthesis by a rabbit reticulocyte lysate.

INHIBITION OF THYROGLOBULIN BIOSYNTHESIS AND DEGRADATION BY EXCESS IODIDE. SYNERGISM WITH LITHIUM

1976 ◽  
Vol 81 (2) ◽  
pp. 495-506 ◽  
Author(s):  
A. Radvila ◽  
R. Roost ◽  
H. Bürgi ◽  
H. Kohler ◽  
H. Studer
Keyword(s):  
Protein Synthesis ◽  
Thyroid Gland ◽  
Inhibitory Action ◽  
Inhibit Protein Synthesis ◽  
Thyrotrophic Hormone ◽  
Thyroid Glands ◽  
Pre Treatment ◽  
Excess Iodide ◽  
Kidney Liver

ABSTRACT Lithium and excess iodide inhibit the release of thyroid hormone from preformed stores. We thus tested the hypothesis that this was due to an inhibition of thyroglobulin breakdown. Rats were pre-treated with propylthiouracil (PTU) for 3 weeks in order to deplete their thyroids of thyroglobulin. While the PTU was continued, lithium chloride (0.25 mEq./100 g weight) or potassium iodide (3 mg per rat) were injected every 12 h for 3 days. Thereafter the thyroglobulin content in thyroid gland homogenates was measured. PTU pre-treatment lowered the thyroglobulin content from 4.21 to 0.22 mg/100 mg gland. Lithium caused a marked re-accumulation of thyroglobulin to 0.60 mg/100 mg within 3 days. While iodide alone had only a borderline effect, it markedly potentiated the action of lithium and a combination of the two drugs increased the thyroglobulin content to 1.04 mg/100 mg. Thyroxine was injected into similarly pre-treated animals to suppress secretion of thyrotrophic hormone. This markedly inhibited the proteolysis of thyroglobulin and 1.3 mg/100 mg gland accumulated after 3 days. Excess iodide, given in addition to thyroxine, decreased the amount of thyroglobulin accumulated to 0.75 mg/100 mg gland. To study whether this could be explained by an inhibitory action of iodide on thyroglobulin biosynthesis, thyroid glands from animals treated with excess iodide were incubated in vitro in the presence of 0.2 mm iodide for 3 h. Iodide decreased the incorporation of radioactive leucine into total thyroidal protein and into thyroglobulin by 25 and 35 % respectively. Iodide did not inhibit protein synthesis in the kidney, liver or muscle tissue. Thus, large doses of iodide selectively inhibit thyroglobulin biosynthesis.

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