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  • 1
    Electronic Resource
    Electronic Resource
    Novel ω-Conotoxins Block Dihydropyridine-Insensitive High Voltage-Activated Calcium Channels in Molluscan Neurons (1996)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 67 (1996), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: We have identified two novel peptide toxins from molluscivorous Conus species that discriminate subtypes of high voltage-activated (HVA) calcium currents in molluscan neurons. The toxins were purified using assays on HVA calcium currents in the caudodorsal cells (CDCs) of the snail Lymnaea stagnalis. The CDC HVA current consists of a rapidly inactivating, transient current that is relatively insensitive to dihydropyridines (DHPs) and a slowly inactivating, DHP-sensitive L-current. The novel toxins, designated ω-conotoxins PnVIA and PnVIB, completely and selectively block the transient HVA current in CDCs with little (PnVIA) or no (PnVIB) effect on the sustained L-type current. The block is rapid and completely reversible. It is noteworthy that both PnVIA and PnVIB reveal very steep dose dependences of the block, which may imply cooperativity in toxin action. The amino acid sequences of PnVIA (GCLEVDYFCGIPFANNGLCCSGNCVFVCTPQ) and of PnVIB (DDDCEPPGNFCGMIKIGPPCCSGWCFFACA) show very little homology to previously described ω-conotoxins, although both toxins share the typical ω-conotoxin cysteine framework but have an unusual high content of hydrophobic residues and net negative charge. These novel ω-conotoxins will facilitate selective analysis of the functions of HVA calcium channels and may enable the rational design of drugs that are selective for relevant subtypes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1996.67052155.x
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  • 2
    Electronic Resource
    Electronic Resource
    Various Isoforms of Myomodulin Identified from the Male Copulatory Organ of Lymnaea Show Overlapping yet Distinct Modulatory Effects on the Penis Muscle (1996)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 66 (1996), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Male copulatory behavior in the snail Lymnaea stagnalis is controlled by several types of peptidergic neurons, including a cluster of neurons in the ventral lobe of the right cerebral ganglion that show immunoreactivity to myomodulin-A of Aplysia and innervate the penis complex. We identified structurally myomodulin-A and three related peptides from Lymnaea and showed that they are present in a characteristic ratio in both the penis nerve and penis complex, suggesting that they are processed from a single precursor and transported from the ventral lobe to the penis complex. All four peptides decreased the relaxation time of electrically evoked contractions of the penis retractor muscle. However, their effects on the amplitude of contraction were different, ranging from no effect to an increase or a decrease in the amplitude. A mixture of the peptides in a ratio as determined by direct mass spectrometry of the penis nerve decreased the contraction time, the relaxation time, and the amplitude. These effects resemble those of one particular peptide in the mixture. The direct mass spectrometry determinations of the peptide profile in the penis nerve suggest that many more, as yet unidentified, neuropeptides are involved in modulation of muscle activities of the penis complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1996.66010321.x
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  • 3
    Electronic Resource
    Electronic Resource
    Stimulus-dependent regulation and cellular expression of genes encoding neuropeptides, prohormone convertases, α-amidating enzyme and 7B2 in identified Lymnaea neurons (2004)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 90 (2004), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Synthesis of bioactive peptides is regulated by several post-translational processing events, including cleavage of peptides from a prohormone, and chemical modifications. Using quantitative in situ hybridization and neuron-specific macro-arrays, we first demonstrated cell-type specific expression levels of transcripts encoding prohormone convertases, peptide α-amidating enzyme as well as the chaperone 7B2 in Lymnaea neurons. Second, we demonstrated a strict correlation between α-amidating enzyme and its neuropeptide substrates. However, this strict relationship of gene expression of the three prohormone convertases and types of cleavage site used is not present. Third, we showed by a physiological stimulus, i.e. clean water, which leads to a stereotyped egg-laying behaviour resulting in successful egg-mass deposition, the co-regulated induction of transcript levels of processing enzymes, 7B2, and egg-laying hormone. These data indicate that (i) these enzymes (and chaperone) are involved in egg-laying hormone neuropeptide biosynthesis, and (ii) neuropeptide release and transcript levels of both prohormones and processing enzymes are regulated in accordance with physiological demands.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.2004.02484.x
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  • 4
    Electronic Resource
    Electronic Resource
    New Sodium Channel-Blocking Conotoxins Also Affect Calcium Currents in Lymnaea Neurons (1995)
    s.l. : American Chemical Society
    Biochemistry 34 (1995), S. 5364-5371 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00016a007
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  • 5
    Electronic Resource
    Electronic Resource
    Processing of the FMRFamide Precursor Protein in the Snail Lymnaea stagnalis: Characterization and Neuronal Localization of a Novel Peptide, ‘SEEPLY’ (1993)
    Oxford, UK : Blackwell Publishing Ltd
    European journal of neuroscience 5 (1993), S. 0 
    Details
    ISSN: 1460-9568
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: In the pulmonate snail Lymnaea stagnalis, FMRFamide-like neuropeptides are encoded by a multi-exon genomic locus which is subject to regulation at the level of mRNA splicing. We aim to understand the post-translational processing of one resulting protein precursor encoding the tetrapeptide FMRFamide and a number of other putative peptides, and determine the distribution of the final peptide products in the central nervous system (CNS) and periphery of Lymnaea. We focused on two previously unknown peptide sequences predicted by molecular cloning to be encoded in the tetrapeptide protein precursor consecutively, separated by the tetrabasic cleavage site RKRR. Here we report the isolation and structural characterization of a novel non-FMRFamide-like peptide, the 22 amino acid peptide SEQPDVDDYLRDWLQSEEPLY. The novel peptide is colocalized with FMRFamide in the CNS in a number of identified neuronal systems and their peripheral motor targets, as determined by in situ hybridization and immunocytochemistry. Its detection in heart excitatory motoneurons and in nerve fibres of the heart indicated that the novel peptide may play a role, together with FMRFamide, in heart regulation in the snail. The second predicted peptide, STEAGGQSEEMTHRTA (16 amino acids), was at very low abundance in the CNS and was only occasionally detected. Our current findings, suggestive of a distinct pattern of post-translational processing, allowed the reassessment of a previously proposed hypothesis that the two equivalent sequences in the Aplysia FMRFamide gene constitute a molluscan homologue of vertebrate corticotrophin releasing factor-like peptides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1460-9568.1993.tb00952.x
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  • 6
    Electronic Resource
    Electronic Resource
    Post-translational Processing of the Alternative Neuropeptide Precursor Encoded by the FMRFamide Gene in the Pulmonate Snail Lymnaea stagnalis (1996)
    Oxford, UK : Blackwell Publishing Ltd
    European journal of neuroscience 8 (1996), S. 0 
    Details
    ISSN: 1460-9568
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The neuropeptide gene encoding FMRFamide-like peptides in the pulmonate mollusc Lymnaea is subject to alternative splicing that generates cell-specific expression of distinct sets of peptides in the CNS. In this paper, we analyse the post-translational processing of the alternative protein precursor encoded by the exon I, III–V transcript (type 2 transcript). We raised anti-peptide antisera specific to distinct segments of the precursor in order to address the pattern of endoproteolytic cleavages, specifically around the tetrabasic site RRKR. We first showed that not all peptides predicted by the precursor structure are generated as final steady-state products. We then identified a novel peptide by biochemical purification, amino acid sequencing and mass spectrometry—the 35 amino acid SDPFFRFGKQQVATDDSGELDDEILSRVSDDDKNI, which we termed the acidic peptide, previously not predicted on the basis of the precursor structure. This novel peptide, abundant in the snail brain (0.7 pmol per central nervous system), includes the N-terminal sequence SDPFFRF, which was previously considered to be a variant of the known heptapeptide SDPFLRFamide, also encoded within the same protein precursor. We showed by in situ hybridization and immunocytochemistry that the acidic peptide is produced in all cells that transcribe type 2 FMRFamide mRNA. We mapped the expression of this novel peptide in the CNS and localized it mainly in three identifiable neuronal clusters—the E, F and B groups of cells—and some additional neurons, all situated in three of the eleven central ganglia. Immunoreactive neurons included the single identifiable visceral white interneuron (VWI or VD4), a key cell of the cardiorespiratory network.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1460-9568.1996.tb01584.x
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  • 7
    Electronic Resource
    Electronic Resource
    Molecular cloning and characterization of an invertebrate homologue of a neuropeptide Y receptor (1998)
    Oxford, UK : Blackwell Science Ltd
    European journal of neuroscience 10 (1998), S. 0 
    Details
    ISSN: 1460-9568
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Neuropeptide Y is an abundant and physiologically important peptide in vertebrates having effects on food intake, sexual behaviour, blood pressure and circadian rhythms. Neuropeptide Y homologues have been found in invertebrates, where they are very likely to play similar, important roles. Although five neuropeptide Y-receptor subtypes have been identified in mammals, none has been reported from invertebrates. Here we describe the cloning of a neuropeptide Y-receptor from the brain of the snail Lymnaea stagnalis. The identity of the receptor was deduced by expressing the neuropeptide Y-receptor-encoding cDNA in Chinese Hamster Ovary cells, which were subsequently challenged with size-fractionated Lymnaea brain extracts. An active peptide, selected on the basis of its ability to induce changes in cAMP levels, was purified to homogeneity, analysed by mass spectrometry and amino acid sequence determination, and turned out to be a Lymnaea homologue of neuropeptide Y.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1460-9568.1998.00350.x
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  • 8
    Electronic Resource
    Electronic Resource
    A glia-derived acetylcholine-binding protein that modulates synaptic transmission (2001)
    [s.l.] : Macmillian Magazines Ltd.
    Nature 411 (2001), S. 261-268 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] There is accumulating evidence that glial cells actively modulate neuronal synaptic transmission. We identified a glia-derived soluble acetylcholine-binding protein (AChBP), which is a naturally occurring analogue of the ligand-binding domains of the nicotinic acetylcholine receptors (nAChRs). Like ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/35077000
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  • 9
    Electronic Resource
    Electronic Resource
    The isolation of a cDNA encoding a neuropeptide prohormone from the light yellow cells ofLymnaea stagnalis (1993)
    Springer
    Cellular and molecular neurobiology 13 (1993), S. 263-270 
    Details
    ISSN: 1573-6830
    Keywords: cDNA sequence ; preprohormone ; neuropeptides ; light yellow cells ; Lymnaea stagnalis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. The central nervous system (CNS) of the freshwater snailLymnaea stagnalis contains several clusters of neuroendocriene cells, which synthesize neuropeptides that act as neurotransmitters, neurohormones, and/or neuromo-dulators, controlling a broad range of physiological processes. Using a protein chemical approach, we have previously characterized a peptide [named LYCP-A (Hoeket al., 1992], which is produced by the neuroendocrine light yellow cells (LYC), which are present as two clusters of endogenously bursting neurons in the visceral and right parietal ganglion, respectively. 2. A differential screening technique was used to isolate the cDNA that encodes the prohormone of LYCP-A. The prohormone appeared to contain three or four putative neuropeptides, one of which is LYCP-A. The organization of the identified prohormone resembles that of the histidine-rich basic peptide precursor previously identified in the R3-14 neurons of the marine snailAplysia californica (Campanelli and Scheller, 1987). 3. In situ hybridization analysis indicates that the gene encoding the LYC prohormone is expressed in a subset of the LYC. The LYC release their peptides into the hemolymph from a neurohemal area, which is located around the CNS. In addition, the peptides are released from axonal branches in the aorta of the heart, suggesting a role in the regulation of cardiovascular functions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00733754
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