The Experts below are selected from a list of 141 Experts worldwide ranked by ideXlab platform
Ian D. Mcfarlane - One of the best experts on this subject based on the ideXlab platform.
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Coelenterate neuropeptides structure action and biosynthesis
Integrative and Comparative Biology, 1992Co-Authors: Cornelis J. P. Grimmelikhuijzen, Dorothea Darmer, C. Schmutzler, Klaus Carstensen, Angelika Moosler, Hans-peter Nothacker, Rainer K. Reinscheid, Ian D. Mcfarlane, Henning Vollert, Kenneth L. RinehartAbstract:Evolutionary “old” nervous systems such as those of Coelenterates are peptidergic: Using various radioimmunoassays we have now isolated 13 novel neuropeptides from sea anemones and several others from hydrozoan polyps and medusae. These peptides are all structurally related and contain the C-terminal sequence Arg-X-NH2 or Lys-X-NH2, where X is Ala, Asn, Ile, Phe, Pro or Trp. Three neuropeptides have a novel N-terminal L-3-phenyllactyl residue, which protects against degradation by nonspecific aminopeptidases. The neuropeptides from sea anemones are produced by different sets of neurones and have excitatory or inhibitory actions on isolated muscle preparations, suggesting that they are neurotransmitters or neuromodulators. We have also cloned the precursor protein for the sea-anemone neuropeptide Antho-RFamide (
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Coelenterate Neuropeptides: Structure, Action and Biosynthesis
American Zoologist, 1992Co-Authors: Cornelis J. P. Grimmelikhuijzen, Dorothea Darmer, C. Schmutzler, Klaus Carstensen, Angelika Moosler, Hans-peter Nothacker, Rainer K. Reinscheid, Ian D. Mcfarlane, Henning Vollert, Kenneth L. RinehartAbstract:Evolutionary “old” nervous systems such as those of Coelenterates are peptidergic: Using various radioimmunoassays we have now isolated 13 novel neuropeptides from sea anemones and several others from hydrozoan polyps and medusae. These peptides are all structurally related and contain the C-terminal sequence Arg-X-NH2 or Lys-X-NH2, where X is Ala, Asn, Ile, Phe, Pro or Trp. Three neuropeptides have a novel N-terminal L-3-phenyllactyl residue, which protects against degradation by nonspecific aminopeptidases. The neuropeptides from sea anemones are produced by different sets of neurones and have excitatory or inhibitory actions on isolated muscle preparations, suggesting that they are neurotransmitters or neuromodulators. We have also cloned the precursor protein for the sea-anemone neuropeptide Antho-RFamide (
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Chapter 11 The peptidergic nervous system of Coelenterates
Progress in brain research, 1992Co-Authors: Cornelis J. P. Grimmelikhuijzen, Dorothea Darmer, C. Schmutzler, Klaus Carstensen, Angelika Moosler, Hans-peter Nothacker, Rainer K. Reinscheid, H. Vollert, Kenneth L. Rinehart, Ian D. McfarlaneAbstract:Publisher Summary Coelenterates are well known models for developmental biologists. Because of the simplicity of their nervous systems, Coelenterates have an extremely high regeneration capacity, and nervous systems probably evolved in animals that were closely related to present-day Coelenterates. This chapter describes the peptidergic nervous system of Coelenterates, the various types of neuropeptides, and the biosynthesis of neuropeptides in Coelenterates. The presence of chemical synapses in the Coelenterate nervous system is confirmed by simultaneous intracellular recordings at both pre- and postsynaptic neurones, which display the expected excitatory postsynaptic potentials (EPSPs) with a constant latency from the presynaptic spike. The chapter discusses the first report on the Antho-RFamide precursor in sea anemones on a neuropeptide precursor in lower invertebrates, which shows that the biosynthetic machinery for neuropeptides in sea anemones has already attained a high level of efficiency. The mechanisms of neuropeptide biosynthesis in sea anemones are similar to those in higher invertebrates, such as molluscs and insects, and vertebrates. Through the study of simple nervous systems––such as Coelenterates––more about basic mechanisms in neurobiology can be learned.
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Neuropeptides in Coelenterates: a review
Hydrobiologia, 1991Co-Authors: Cornelis J. P. Grimmelikhuijzen, D Graff, Jane A. Westfall, Osamu Koizumi, Ian D. McfarlaneAbstract:Coelenterate neurones produce peptides containing an Arg-Phe-NH2(RF-amide)-like carboxyterminus. RF-amide-like peptides are located in neuronal dense-cored vesicles, indicating that they are released by exocytosis and that they might function as neurotransmitters or neurohormones. Using a radioimmunoassay for the sequence RF-amide, 3 peptides were isolated from the sea anemone Anthopleura elegantissima: < Glu-Gly-Arg-Phe-NH2(Antho-RF-amide),
Milton J Cormier - One of the best experts on this subject based on the ideXlab platform.
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isolation and expression of a cdna encoding renilla reniformis luciferase
Proceedings of the National Academy of Sciences of the United States of America, 1991Co-Authors: Walter W Lorenz, Richard O Mccann, Mathew Longiaru, Milton J CormierAbstract:Renilla reniformis is an anthozoan Coelenterate capable of exhibiting bioluminescence. Bioluminescence in Renilla results from the oxidation of Coelenterate luciferin (coelenterazine) by luciferase [Renilla-luciferin:oxygen 2-oxidoreductase (decarboxylating), EC 1.13.12.5]. In vivo, the excited state luciferin-luciferase complex undergoes the process of nonradiative energy transfer to an accessory protein, green fluorescent protein, which results in green bioluminescence. In vitro, Renilla luciferase emits blue light in the absence of any green fluorescent protein. A Renilla cDNA library has been constructed in lambda gt11 and screened by plaque hybridization with two oligonucleotide probes. We report here the isolation and characterization of a luciferase cDNA and its gene product. The recombinant luciferase expressed in Escherichia coli is identical to native luciferase as determined by SDS/PAGE, immunoblot analysis, and bioluminescence emission characteristics.
Jorge Florinchristensen - One of the best experts on this subject based on the ideXlab platform.
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the molecular basis of the self non self selectivity of a Coelenterate toxin
Biochemical and Biophysical Research Communications, 1995Co-Authors: Elsa Meinardi, Monica Florinchristensen, Gustavo Paratcha, Julio M Azcurra, Jorge FlorinchristensenAbstract:Abstract Coelenterates produce potent hemolysins inhibited by sphingomyelin (SM) Remarkably, instead of this lipid, their membrane contain a phosphono analogue of it. Using coelenterolysin (CL), a toxin produced by the sea anemone Phymactis clematis, we have examined a possible connection between these two peculiar traits. Our experiments showed that, while SM binds this lysin and inhibits its hemolytic activity, the endogenous PnSL do neither. In addition, liposomes made of bovine erythrocyte lipids are rapidly disrupted by CL, while those made of P. clematis lipids are completely resistant to it. However, if small amounts of SM are added to the P. clematis lipids, the resulting liposomes become sensitive to CL. Taken together, our results show for the first time that substitution of SM by its phosphono analogue is the molecular basis for the selectivity of an anthozoan toxin. We therefore propose that exotoxin production and membrane composition are coadapted traits that confer on the Coelenterates a significant evolutionary advantage.
Cornelis J. P. Grimmelikhuijzen - One of the best experts on this subject based on the ideXlab platform.
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Coelenterate neuropeptides structure action and biosynthesis
Integrative and Comparative Biology, 1992Co-Authors: Cornelis J. P. Grimmelikhuijzen, Dorothea Darmer, C. Schmutzler, Klaus Carstensen, Angelika Moosler, Hans-peter Nothacker, Rainer K. Reinscheid, Ian D. Mcfarlane, Henning Vollert, Kenneth L. RinehartAbstract:Evolutionary “old” nervous systems such as those of Coelenterates are peptidergic: Using various radioimmunoassays we have now isolated 13 novel neuropeptides from sea anemones and several others from hydrozoan polyps and medusae. These peptides are all structurally related and contain the C-terminal sequence Arg-X-NH2 or Lys-X-NH2, where X is Ala, Asn, Ile, Phe, Pro or Trp. Three neuropeptides have a novel N-terminal L-3-phenyllactyl residue, which protects against degradation by nonspecific aminopeptidases. The neuropeptides from sea anemones are produced by different sets of neurones and have excitatory or inhibitory actions on isolated muscle preparations, suggesting that they are neurotransmitters or neuromodulators. We have also cloned the precursor protein for the sea-anemone neuropeptide Antho-RFamide (
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Coelenterate Neuropeptides: Structure, Action and Biosynthesis
American Zoologist, 1992Co-Authors: Cornelis J. P. Grimmelikhuijzen, Dorothea Darmer, C. Schmutzler, Klaus Carstensen, Angelika Moosler, Hans-peter Nothacker, Rainer K. Reinscheid, Ian D. Mcfarlane, Henning Vollert, Kenneth L. RinehartAbstract:Evolutionary “old” nervous systems such as those of Coelenterates are peptidergic: Using various radioimmunoassays we have now isolated 13 novel neuropeptides from sea anemones and several others from hydrozoan polyps and medusae. These peptides are all structurally related and contain the C-terminal sequence Arg-X-NH2 or Lys-X-NH2, where X is Ala, Asn, Ile, Phe, Pro or Trp. Three neuropeptides have a novel N-terminal L-3-phenyllactyl residue, which protects against degradation by nonspecific aminopeptidases. The neuropeptides from sea anemones are produced by different sets of neurones and have excitatory or inhibitory actions on isolated muscle preparations, suggesting that they are neurotransmitters or neuromodulators. We have also cloned the precursor protein for the sea-anemone neuropeptide Antho-RFamide (
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Chapter 11 The peptidergic nervous system of Coelenterates
Progress in brain research, 1992Co-Authors: Cornelis J. P. Grimmelikhuijzen, Dorothea Darmer, C. Schmutzler, Klaus Carstensen, Angelika Moosler, Hans-peter Nothacker, Rainer K. Reinscheid, H. Vollert, Kenneth L. Rinehart, Ian D. McfarlaneAbstract:Publisher Summary Coelenterates are well known models for developmental biologists. Because of the simplicity of their nervous systems, Coelenterates have an extremely high regeneration capacity, and nervous systems probably evolved in animals that were closely related to present-day Coelenterates. This chapter describes the peptidergic nervous system of Coelenterates, the various types of neuropeptides, and the biosynthesis of neuropeptides in Coelenterates. The presence of chemical synapses in the Coelenterate nervous system is confirmed by simultaneous intracellular recordings at both pre- and postsynaptic neurones, which display the expected excitatory postsynaptic potentials (EPSPs) with a constant latency from the presynaptic spike. The chapter discusses the first report on the Antho-RFamide precursor in sea anemones on a neuropeptide precursor in lower invertebrates, which shows that the biosynthetic machinery for neuropeptides in sea anemones has already attained a high level of efficiency. The mechanisms of neuropeptide biosynthesis in sea anemones are similar to those in higher invertebrates, such as molluscs and insects, and vertebrates. Through the study of simple nervous systems––such as Coelenterates––more about basic mechanisms in neurobiology can be learned.
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Neuropeptides in Coelenterates: a review
Hydrobiologia, 1991Co-Authors: Cornelis J. P. Grimmelikhuijzen, D Graff, Jane A. Westfall, Osamu Koizumi, Ian D. McfarlaneAbstract:Coelenterate neurones produce peptides containing an Arg-Phe-NH2(RF-amide)-like carboxyterminus. RF-amide-like peptides are located in neuronal dense-cored vesicles, indicating that they are released by exocytosis and that they might function as neurotransmitters or neurohormones. Using a radioimmunoassay for the sequence RF-amide, 3 peptides were isolated from the sea anemone Anthopleura elegantissima: < Glu-Gly-Arg-Phe-NH2(Antho-RF-amide),
Vassilii I. Svetashev - One of the best experts on this subject based on the ideXlab platform.
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Identification, isolation and characterization of tetracosapolyenoic acids in lipids of marine Coelenterates.
Biochimica et biophysica acta, 1991Co-Authors: Mikhail V. Vysotskii, Vassilii I. SvetashevAbstract:Several tetracosapolyenoic acids (TPA) were detected in lipids of different marine Coelenterates. Two of these acids were isolated and their structures were confirmed by chemical and spectral methods as all-cis-6,9,12,15,18-tetracosapentaenoic and all-cis-6,9,12,15,18,21-tetracosahexaenoic acid. Their distribution among lipids of a number of species of different classes of Coelenterates from the northern and tropical seas, among neutral and polar lipids of these organisms was investigated. Significant quantities of TPA were found in all of the Octacorallia species studied. In some cases the sum of TPA reaches the level of 20% of total lipid fatty acids. The fatty acid composition of different Coelenterates is also discussed.