Pyrularia Thionin: Physical Properties, Biological Responses and Comparison to Other Thionins and Cardiotoxin

References

• Vernon L. P., Evett G. E., Zeikus R. D., Gray W. R. A Toxin Thionin from Pyrularia pubera: Purification, Properties, and Amino Acid Sequence. Arch. Biochem. Biophys. 1985; 238: 18
   PubMed Web of Science ®Google Scholar
• Osorio e Castro V. R., Vernon L. P. Hemolytic Activity of Thionin from Pyrularia Pubera Nuts and Snake Venom Toxins of Naja Naja Species: Pyrularia Thionin and Snake Venom Cardiotoxin Compete for the Same Membrane Site. Toxicon 1989; 27: 511
   PubMed Web of Science ®Google Scholar
• Vernon L. P., Rogers A. Effect of Calcium and Phosphate Ions on Hemolysis Induced by Pyrularia thionin and Naja Naja Kaouthia Cardiotoxin. Toxicon 1992, in press
   Google Scholar
• Vernon L. P., Rogers A. Binding Properties of Pyrularia Thionin and Naja Naja Kaouthia Cardiotoxin to Human and Animal Erythrocytes and P388 Cells. Toxicon 1992, in press
   Google Scholar
• Garcia-Olmedo F., Rodriguez-Palenzuela P., Hernandez-Lucas C., Ponz F., Marana C. The Thionins: A Protein Family that Includes Purothionins, Viscotoxins and Crambins. Oxford Surv. Plant Mol. Cell Biol. 1989; 6: 31
   Google Scholar
• Bohlmann H., Apel K. Thionins. Ann. Rev. Plant. Physiol. 1991; 42: 227
   Google Scholar
• Balls A. K., Hale W. S., Harris T. H. A Crystalline Protein Obtained from a Lipoprotein of Wheat Flour. Cereal Chem. 1942; 19: 279
   Google Scholar
• Jones B. L., Lookhart G. L., Mak A. S., Cooper D. B. Sequence of Purothionins and their Inheritance in Diploid, Tetraploid, and Hexaploid Wheats. J. Hered. 1982; 73: 143
   Web of Science ®Google Scholar
• Jones B. L., Mak A. S. Amino Acid Sequences of the two α-Purothionins of Hexaploid Wheat. Cereal Chem. 1977; 54: 511
   Web of Science ®Google Scholar
• Mak A. S., Jones B. L. The Amino Acid Sequence of Wheat β-Purothionin. Can. J. Biochem. 1976; 54: 835
   PubMedGoogle Scholar
• Ohtani S., Okada T., Kagamiyama H., Yoshizumi H. The Amino Acid Sequence of Purothionin A, a Lethal Toxic Protein for Brewer's Yeasts from Wheat. Agric. Biol. Chem. 1975; 39: 2269
   Web of Science ®Google Scholar
• Ohtani S., Okada T., Yoshizumi H., Kagamiyama H. Complete Primary Structures of Two Subunits of Purothionin A, a Lethal Protein for Brewer's Yeast from Wheat Flour. J. Biochem. 1977; 82: 753
   PubMed Web of Science ®Google Scholar
• Colilla F. J., Rocher A., Mendez E. γ-Purothionins: Amino Acid Sequence of Two Polypeptides of a New Family of Thionins from Wheat Endosperm. FEBS 1990; 270: 191
   PubMed Web of Science ®Google Scholar
• Bloch C., Jr, Richardson M. A New Family of Small (5kDa) Protein Inhibitors of Insect α-Amylases from Seeds or Sorghum (sorghum bicolor (L) Moench) have Sequence Homologies with Wheat γ-Purothionins. FEBS 1991; 279: 101
   PubMed Web of Science ®Google Scholar
• Hernandez-Lucas C., Royo J., Paz-Ares J., Ponz F., Garcia-Olmedo F., Carbonero P. Polyadenylation Site Heterogeneity in mRNA Encoding the Precursor of the Barley Toxin β-Hordothionin. FEBS Lett. 1986; 200: 103
   Web of Science ®Google Scholar
• Ozaki Y., Wada K., Hase T., Matsubara H., Nakanishi T., Yoshizumi H. Amino Acid Sequence of a Purothionin Homolog from Barley Flour. J. Biochem. 1980; 87: 549
   PubMed Web of Science ®Google Scholar
• Ponz F., Paz-Ares J., Hemandez-Lucas C., Garcia-Olmedo F., Carbonero P. Cloning and Nucleotide Sequence of a cDNA Encoding the Precursor of the Barley Toxin α-Hordothionin. Eur. J. Biochem. 1986; 156: 131
   PubMedGoogle Scholar
• Redman D. G., Fisher N. Fractionation and Comparison of Purothionin and Globulin Components of Wheat. J. Sci. Food Agric. 1968; 19: 651
   Web of Science ®Google Scholar
• Reimann-Philipp U., Schrader G., Martinoia E., Barkholt V., Apel K. Intracellular Thionins of Barley. A Second Group of Leaf Thionins Closely Related to but Distinct from Cell Wall-Bound Thionins. J. Biol. Chem. 1989; 264: 8978
   PubMed Web of Science ®Google Scholar
• Bekes F., Lasztity R. Isolation and Determination of Amino Acid Sequence of Avenothionin, a New Purothionin Analogue from Oat. Cereal Chem. 1981; 58: 360
   Web of Science ®Google Scholar
• Hernandez-Lucas C., Carbonero P., Garcia-Olmedo F. Identification and Purification of a Purothionin Homologue from Rye (Secale cereale L.). J. Agric. Food Chem. 1978; 26: 794
   Web of Science ®Google Scholar
• Mendez E., Moreno A., Colilla F., Pelaez F., Limas G. G., Mendez R., Soriano F., Salinas M., Cesar de Haro. Primary Structure and Inhibition of Protein Synthesis in Eukaryotic Cell-Free System of a Novel Thionin, γ-Hordothionin, from Barley Endosperm. Eur. J. Biochem. 1990; 194: 533
   PubMedGoogle Scholar
• Jones B. L., Cooper D. B. Purification and Characterization of a Corn (Zea mays) Protein Similar to Purothionins. J. Agric. Food Chem. 1980; 28: 904
   PubMed Web of Science ®Google Scholar
• Winterfeld V. K., Bijl L. H. Viscotoxin, ein neuer Inhaltsstoff der Mistel (Viscum album L.). Liebigs Ann. Chem. 1949; 561: 107
   Google Scholar
• Samuelsson G. Phytochemical and Pharmacological Studies on Viscum Album L. I. Viscotoxin, its Isolation and Properties. Swed. J. Pharmacol. 1958; 62: 169
   Google Scholar
• Samuelsson G. Phytochemical and Pharmacological Studies on Viscum Album L. V. Further Improvements in the Isolation Methods for Viscotoxin. Studies on Viscotoxin from Viscum Album Growing on Tilia cordata Mill. Swed. J. Pharmacol. 1961; 65: 481
   Google Scholar
• Samuelsson G. Screening of Plants of the Family Loranthaceae for Toxic Proteins. Acta Pharmacol. Suecica 1966; 3: 353
   PubMedGoogle Scholar
• Samuelsson G. Screening of the Plants of the Family Loranthaceae for Toxic Proteins, Part II. Acta Pharmacol. Suecica 1969; 6: 441
   PubMedGoogle Scholar
• Samuelsson G. Mistletoe Toxins. Syst. Zool. 1974; 22: 566
   Google Scholar
• Samuelsson G., Jayawardene A. L. Isolation and Characterization of Viscotoxin IPs from Viscum Album L. ssp. Austriacum (Wiesb.) Vollmann, Growing on Pimus Silvestris. Acta Pharmacol. Suecica 1974; 11: 175
   PubMedGoogle Scholar
• Mellstrand S. T., Samuelsson G. Phoratoxin, a Toxic Protein from the Mistletoe Phoradendron Tomentosum subsp. Macrophyllum (Loranthaceae). The Amino Acid Sequence. Acta Pharmacol. Suecica 1974; 11: 347
   PubMedGoogle Scholar
• Thunberg E., Phoratoxin B. a Toxic Protein from the Mistletoe Phoradendron Tomentosum subsp. Macrophyllum. Acta Pharmacol. Suecica 1983; 20: 115
   Google Scholar
• Thunberg E., Samuelsson G. The Amino Acid Sequence of Ligatoxin A, from the mistletoe Phoradendron Liga. Acta Pharmacol. Suecica 1982; 19: 447
   Google Scholar
• Samuelsson G., Pettersson B. Toxic Proteins from the Mistletoe Dendrophtora Clavata. II. The Amino Acid Sequence of Denclatoxin B. Acta Pharmacol. Suecica 1977; 14: 245
   PubMedGoogle Scholar
• Daley L. S., Theriot L. J. Electrophoretic analysis, Redox Activity, and other Characteristics of Proteins Similar to Purothionins from Tomato (Lycopersicum Esculenta), Mango (Mangifera Indica), Papaya (Carica Papaya), and Walnut (Juglans Regia). J. Agric. Food Chem. 1987; 35: 680
   Web of Science ®Google Scholar
• Van Etten C. H., Nielsen H. C., Peters J. E. A Crystalline Polypeptide from the Seed of Crambe Abyssinica. Phytochemistry 1965; 4: 467
   Google Scholar
• Teeter M. M., Mazer J. A., L'Italien J. J. Primary Structure of the Hydrophobic Plant Protein Crambin. Biochemistry 1981; 20: 5437
   PubMed Web of Science ®Google Scholar
• Hendrickson W. A., Teeter M. M. Structure of the Hydrophobic Protein Crambin Determined Directly from the Anamalous Scattering of Sulphur. Nature 1981; 290: 107
   PubMed Web of Science ®Google Scholar
• Clore G. M., Nilges M., Sukumaran D. K., Brünger A. T., Karplus M., Gronenborn A. M. The Three-Dimensional Structure of α 1-Purothionin in Solution: Combined Use of Nuclear Magnetic Resonance, Distance Geometry and Restrained Molecular Dynamics. EMBO J. 1986; 5: 2729
   PubMed Web of Science ®Google Scholar
• Clore G. M., Sukamaran D. K., Gronenborn A. M., Teeter M. M., Whitlow M., Jones B. L. Nuclear Magnetic Resonance Study of the Solution Structure of α 1-Purothionin. Sequential Resonance Assignment, Secondary Structure and Low Resolution Tertiary Structure. J. Mol. Biol. 1987; 193: 571
   PubMedGoogle Scholar
• Bohlmann H., Clausen S., Behnke S., Giese H., Hiller C. Leaf-Specific thionins of Barley - a Novel Class of Cell Wall Proteins Toxic to Plant-Pathogenic Fungi and Possibly Involved in the Defense Mechanism of Plants. EMBO J. 1988; 7: 1559
   PubMed Web of Science ®Google Scholar
• Ebrahim-Nesbat F., Behnke S., Kleinhofs A., Apel K. Cultivar-Related Differences in the Distribution of Cell-Wall-Bound Thionins in Compatible and Incompatible Interactions Between Barley and Powdery Mildew. Planta 1989; 179: 203
   PubMed Web of Science ®Google Scholar
• Reimann-Philipp U., Behnke S., Batschauer A., Schäfer E., Apel K. The Effect of Light on the biosynthesis of Leaf-Specific Thionins in Barley, Hordeum Vulgare. Eur. J. Biochem. 1989; 182: 283
   PubMedGoogle Scholar
• Bohlmann H., Apel K. Isolation and Characterization of cDNAs Coding for Leaf specific Thionins Closely Related to the Endosperm-Specific Hordothionin of Barley (Hordeum Vulgare L.). Mol. Gen. Genet. 1987; 207: 446
   Google Scholar
• Gausing K. Thionin Genes Specifically Expressed in Barley Leaves. Planta 1987; 171: 241
   PubMed Web of Science ®Google Scholar
• Apel K., Bohlmann H., Reimann-Philipp U. Leaf Thionins, a Novel Class of Putative Defence Factors. Physiologia Plantarum 1990; 80: 315
   Google Scholar
• Brünger A. T., Clore G. M., Gronenborn A. M., Karplus M. Three-Dimensional Structure of Proteins Determined by Molecular Dynamics with Interproton Distance Restraints: Application to Crambin. Proc. Natl. Acad. Sci. USA 1986; 83: 3801
   PubMed Web of Science ®Google Scholar
• Brünger A. T., Campbell R. L., Clore G. M., Gronenborn A. M., Karplus M. Solution of a Protein Crystal Structure with a Model Obtained from NMR Interproton Distance Restraints. Science 1987; 235: 1049
   PubMedGoogle Scholar
• Clore G. M., Brünger A. T., Karplus M., Gronenborn A. M. Applications of Molecular Dynamics with Interproton Distance Restraints to Three-Dimensional Protein Structure Determination. A Model Study of Crambin. J. Mol. Biol. 1986; 191: 523
   PubMed Web of Science ®Google Scholar
• Williams R. W., Teeter M. M. Raman Spectroscopy of Homologous Plant Toxins: Crambin and α1- and β-Purothionin Secondary Structures, Disulfide Conformation, and Tyrosine Environment. Biochemistry 1984; 23: 6796
   Google Scholar
• Lecomte J. T. J., Jones B. L., Llinas M. Proton Magnetic Resonance Studies of Barley and Wheat Thionins: Structural Homology with Crambin. Biochemistry 1982; 21: 4843
   PubMed Web of Science ®Google Scholar
• Whitlow M., Teeter M. M. Energy Minimization for Tertiary Structure Prediction of Homologous Proteins: α1-Purothionin and Viscotoxin A3 Models from Crambin. J. Biochem. Struct. Dynam. 1985; 2: 831
   PubMed Web of Science ®Google Scholar
• Lecomte J. T. J., Kaplan D., Llinas M., Thunberg E., Samuelsson G. Proton Magnetic Resonance Characterization of Phoratoxins and Homologous Proteins Related to Crambin. Biochemistry 1987; 26: 1187
   Google Scholar
• Clore G. M., Sukumaran D. K., Nilges M., Gronenborn A. M. Three-Dimensional Structure of Phoratoxin in Solution: Combined use of Nuclear Magnetic Resonance, Distance Geometry, and Restrained Molecular Dynamics. Biochemistry 1987; 26: 1732
   Web of Science ®Google Scholar
• Teeter M. M., Ma X. -Q., Rao U., Whitlow M. Crystal Structure of a Protein-Toxin α1-Purothionin at 2.5Å and a Comparison with Predicted Models. Proteins 1990; 8: 118
   PubMedGoogle Scholar
• Fernandez de Caleya R., Gonzalez-Pascual B., Garcia-Olmedo F., Carbonero P. Susceptibility of Phytopathogenic Bacteria to Wheat Purothionins in Vitro. Appl. Microbiol. 1972; 23: 998
   PubMedGoogle Scholar
• Johnson T. C., Wada K., Buchanan B. B., Holmgren A. Reduction of Purothionin by the Wheat Seed Thioredoxin system. Plant Physiol. 1987; 85: 446
   PubMed Web of Science ®Google Scholar
• Carrasco L., Vazquez D., Hernandez-Lucas C., Carbonero P., Garcia-Olmedo F. Thionins: Plant Peptides that Modify membrane Permeability in Cultured Mammalian Cells. Eur. J. Biochem. 1981; 116: 185
   PubMedGoogle Scholar
• Evett G. E., Donaldson D. M., Vernon L. P. Biological Properties of Pyrularia Thionin Prepared from Nuts of Pyrularia Pubera. Toxicon 1986; 24: 622
   PubMed Web of Science ®Google Scholar
• Konopa J., Woynarowski J. M., Lewandowska-Gumieniak M. Isolation of Viscotoxins: Cytotoxic Basic Polypeptides from Viscum Album L. Hoppe-Seyler's Z. Physiol. Chem. 1980; 131: 1525
   Google Scholar
• Nakanishi T., Yoshizumi H., Tahara S., Hakura A., Toyoshima K. Cytotoxicity of Purothionin A on Various Animal Cells. Jpn. J. Cancer Res. 1979; 70: 323
   Google Scholar
• Osorio e Castro V. R., Van Kuiken B. A., Vernon L. P. Action of a Thionin Isolated from Nuts of Pyrularia Pubera on Human Erythrocytes. Toxicon 1989; 27: 501
   PubMed Web of Science ®Google Scholar
• Harvey A. L. Cardiotoxins from Cobra Venoms. Possible Mechanisms of Action. J. Toxicol. -Toxin Rev. 1985; 4: 41
   Web of Science ®Google Scholar
• Harvey A. L. Cardiotoxins from Cobra Venoms. Handbook of Natural Toxins, Vol. 5, Reptile and Amphibian Venoms, A. T. Tu. Marcel-Dekker, New York, 85–106
   Google Scholar
• Angerhofer C. K., Shier W. T., Vernon L. P. Phospholipase Activation in the Cytotoxic Mechanism of Thionin Purified from Nuts of Pyrularia Pubera. Toxicon 1990; 28: 547
   PubMed Web of Science ®Google Scholar
• Shier W. T. Activation of Self-Destruction as a Mechanism of Action for Cytolytic Toxins. Natural Toxins, D. Eaker, T. Wadstrom. Pergamon Press, Oxford and New York, 193–200
   Google Scholar
• Shier W. T. Toxins as Research Tools: Potentials and Pitfalls. J. Toxicol. -Toxin Reviews 1983; 2: 111
   Google Scholar
• Fletcher J. E., Jiang M. -S., Gong Q. -H. Snake Venom Cardiotoxins and bee Venom Mellitin Activate Phospholipase C Activity in Primary Cultures of Skeletal Muscle. Biochem. Cell Biol. 1991; 69: 274
   PubMed Web of Science ®Google Scholar
• Evans J. G. Ph.D. Thesis. Brigham Young University. 1990
   Google Scholar
• Judd A. M., Vemon L. P., MacLeod R. M. Pyrularia Thionin Increases Arachidonate Liberation and Prolactin and Growth Hormone Release from Anterior Pituitary Cells. Toxicon 1992, In press
   Google Scholar
• Osorio e Castro V. R., Ashwood E. R., Wood S. G., Vernon L. P. Hemolysis of Erythrocytes and fluorescence Polarization Changes Elicited by peptide toxins, Aliphatic Alcohols, Related Glycols and Benzylidene Derivatives. Biochim. Biophys. Acta 1990; 1029: 252
   PubMedGoogle Scholar
• Kashimoto T., Sakakibara R., Huynh Q. K., Wada H., Yoshizumi H. The Effect of Purothionin on Bovine Adrenal Medullary Cells. Res. Commun. Chem. Pathol. Pharmacol 1979; 26: 221
   PubMedGoogle Scholar
• Evans J., Wang Y., Shaw K. -P., Vernon L. P. Cellular Responses to Pyrularia thionin are mediated by Ca2+ Influx and Phospholipase A2 Activation and are Inhibited by Thionin Tyrosine Iodination. Proc. Natl. Acad. Sci., USA 1989; 86: 5849
   PubMed Web of Science ®Google Scholar
• Florine-Casteel K. F., Lemasters J. J., Herman B. Lipid Order in Hepatocyte Plasma membrane Blebs During ATP Depletion Measured by Digitized Video Fluorescence Polarization Microscopy. FASEB J. 1991; 5: 2078
   PubMed Web of Science ®Google Scholar
• Jones R. L., Miller J. C., Hagler H. K., Chien K. R., Willerson J. T., Buja L. M. Association Between Inhibition of Arachidonic Acid Release and Prevention of Calcium Loading During ATP Depletion in Cultured Rat Cardiac Myocytes. Am. J. Pathol 1989; 135: 541
   PubMedGoogle Scholar
• Gasanov S. E., Vemon L. P., Aripov T. F. Modification of Phospholipid Membrane Structure by the Plant Toxic Peptide Pyrularia Thionin. Biochim. Biophys. Acta, Submitted 1992
   Google Scholar
• Dufourcq J., Faucon J. -F. Specific Binding of a Cardiotoxin from Naja Mossambica Mossambica to Charged Phospholipids Detected by Intrinsic Fluorescence. Biochemistry 1978; 17: 1170
   PubMed Web of Science ®Google Scholar
• Vincent J. -P., Balerna M., Lazdunski M. Properties of Association of Cardiotoxin with Lipid Vesicles and Natural Membranes. FEBS Lett. 1978; 85: 103
   PubMed Web of Science ®Google Scholar
• Faucon J. F., Bernard E., Dufourcq J., Pezolet M., Bougis P. Perturbation of Charged Phospholipid Bilayers Induced by Melittin and Cardiotoxins. A Fluorescence, Differential Scanning Calorimetry and Raman Spectroscopy Study. Biochimie 1981; 63: 857
   Google Scholar
• Faucon J. F., Dufourcq E., Bernard J., Duchesneau L., Pezolet M. Abolition of the Thermotropic Transition of Charged Phospholipids Induced by a Cardiotoxin from Naja Mossambica Mossambica as detected by Fluorescence Polarization, Differential Scanning Calorimetry, and Raman Spectroscopy. Biochemistry 1983; 22: 2179
   Google Scholar
• Bougis P., Tessier M., Van Rietschoten J., Rochat H., Faucon J. F., Dufourcq J. Are Interactions with Phospholipids Responsible for Pharmacological Activities of Cardiotoxins. Mol. Cell. Biochem. 1983; 55: 49
   PubMedGoogle Scholar
• Dufourcq J., Faucon J. F., Bernard E., Pezolet M. Structure-Function Relationships for Cardiotoxins Interacting with Phospholipids. Toxicon 1982; 20: 165
   PubMed Web of Science ®Google Scholar
• Gatineau E., Toma F., Montenay-Garestier T., Takechi M., Fromageot P., Menez A. Role of Tyrosine and Tryptophan Residues in the Structure-Activity Relationships of a Cardiotoxin from Naja Nigrocollis Venom. Biochemistry 1987; 26: 8046
   PubMed Web of Science ®Google Scholar
• Aripov T. F., Salakhutdinov B. A., Salikhova Z. T., Sadykov A. S., Tashmukhamedov B. A. Structural Changes of Liposome Phospholipid Packing Induced by Cytotoxin of the Central Asia Cobra Venom. Gen. Physl. Biophys. 1984; 3: 489
   PubMed Web of Science ®Google Scholar
• Aripov T. F., Gasanov S. E., Salakhutdinov B. A., Rozenshtein I. A., Kamaev F. G. Central Asian Cobra Venom Cytotoxins-Induced Aggregation, Permeability and Fusion of Liposomes. Gen. Physl. Biophys. 1989; 8: 459
   Google Scholar
• Oimatov M., Lvov Yu. M., Aripov T. F., Feigin L. A. X-Ray Small-Angle Scattering Structural Studies of Model Membrane Complexes with Cytotoxin. Stud. Biophys. 1986; 112: 237
   Google Scholar
• Fracki W. S., Li D., Owen N., Perry C., Naisbitt G. H., Vernon L. P. Role of Tyr and Trp in Membrane Responses of Pyrularia Thionin Determined by Optical and NMR Spectra following Tyr Iodination and Trp Modification. Toxicon 1992, in press
   Google Scholar
• Wada K., Ozaki Y., Matsubara H., Yoshizumi H. Studies on Purothionin by Chemical Modifications. J. Biochem. 1982; 91: 257
   PubMed Web of Science ®Google Scholar
• Bell J. D., Biltonen R. L. The Temporal Sequence of Events in the Activation of Phospholipase A2 by Lipid Vesicles. J. Biol. Chem. 1989; 264: 12194
   Google Scholar
• Vernon L. P., Bell J. D. Membrane Structure, Toxins and Phospholipase A2 Activity. Pharm. Therap. 1992, in press
   Google Scholar