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Peter M Brophy - One of the best experts on this subject based on the ideXlab platform.
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purification and characterisation of a novel cysteine conjugate β lyase from the tapeworm Moniezia expansa
International Journal for Parasitology, 2000Co-Authors: Harriet J Adcock, Peter M Brophy, Paul H Teesdalespittle, L D BuckberryAbstract:Abstract The paper presents the first report of the purification of an invertebrate cysteine conjugate β-lyase (CCBL). CCBL activity was shown to predominate within the cytosolic fraction of tissue from the tapeworm Moniezia expansa . The monomeric cytosolic enzyme was isolated with a M r of 72 kDa and co-purified with transaminase activity towards l -aspartate. The substrate profile for M. expansa CCBL is different from that of mammalian CCBLs. Exploiting the differences in mammalian and parasite substrate profiles will facilitate the development of helminth targeted conjugates which will not be activated by host (mammalian) CCBLs.
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Cysteine conjugate β-lyase activity in three species of parasitic helminth
International Journal for Parasitology, 1999Co-Authors: Harriet J Adcock, Peter M Brophy, Paul H. Teesdale-spittle, L D BuckberryAbstract:Abstract Living organisms employ a variety of metabolic pathways when detoxifying xenobiotic compounds, including the formation of cysteine S- conjugates via glutathione conjugation. However, cysteine conjugate β-lyase (CCBL) catalysed β-cleavage, of certain cysteine conjugates, is known to cause cytotoxicity. This study represents the first investigation into the expression of CCBL and other associated enzymes in helminth species. A survey of the three major groups of parasitic helminths [cestodes ( Moniezia expansa ), digeneans ( Fasciola hepatica ) and nematodes ( Necator americanus , Heligmosomoides polygyrus )] has been made. The presence of CCBL enzymes within Moniezia expansa , Necator americanus and Heligmosomoides polygyrus has been established. Each species was screened for γ-glutamyl transpeptidase activity and transaminase activity towards l -aspartate, l -alanine, l -albizziin and l -phenylalanine. Aspartate and alanine aminotransferase activity were detected in all four species tested. γ-Glutamyl transpeptidase activity was only detected in Moniezia expansa and Necator americanus .
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characterisation and properties of an intracellular lipid binding protein from the tapeworm Moniezia expansa
FEBS Journal, 1997Co-Authors: J Barrett, Nahid Saghir, Anna Timanova, Katie Clarke, Peter M BrophyAbstract:The tapeworm Moniezia expansa contains an extremely abundant cytoplasmic lipid-binding protein (LBP). It is a small protein consisting of 66 amino acids with a molecular mass of 7943 ± 1.5Da. The amino acid sequence has been established by Edman degradation and confirmed by PCR analysis. The Moniezia LBP shows no sequence similarity with any previously described binding protein, but does show similarity with antigen B from Echinococcus glanulosus and Echinococcus multilocularis and with Taenia crassiceps antigen. The predicted structure for Moniezia LBP shows four helices and a putative tyrosine kinase site on the loop between helix 1 and 2. Each of the four helices has a well defined hydrophobic face. Studies with fluorescent probes suggest a single hydrophobic binding site. Results indicate that the single tryptophan residue in the molecule (Trp41) is involved in ligand binding, and calculation of the Stern-Volmer quenching constant shows that Trp41 is in a relatively hydrophobic environment.
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a novel nadph nadh dependent aldehyde reduction enzyme isolated from the tapeworm Moniezia expansa
FEBS Letters, 1990Co-Authors: Peter M Brophy, Paul Crowley, J BarrettAbstract:Abstract An aldehyde reduction enzyme has been purified from the cytosol of the tapeworm, Moniezia expansa , by chromatofocusing and Reactive-Red chromatography. The enzyme is monomeric (subunit 34 kDa) and can utilise NADH and NADPH as co-factors. Substrates of the enzyme include alkanals, alka-2,4-dienals and alk-2-enals, established secondary products of lipid peroxidation. The enzyme reduced methylglyoxal, another possible natural substrate ( M. expansa lacks glyoxalase I activity). The parasite enzyme may help form a final line of defence against cytotoxic aldehydes arising from host immune initiated lipid peroxidation.
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A novel NADPH/NADH-dependent aldehyde reduction enzyme isolated from the tapeworm Moniezia expansa
FEBS Letters, 1990Co-Authors: Peter M Brophy, Paul Crowley, J BarrettAbstract:Abstract An aldehyde reduction enzyme has been purified from the cytosol of the tapeworm, Moniezia expansa , by chromatofocusing and Reactive-Red chromatography. The enzyme is monomeric (subunit 34 kDa) and can utilise NADH and NADPH as co-factors. Substrates of the enzyme include alkanals, alka-2,4-dienals and alk-2-enals, established secondary products of lipid peroxidation. The enzyme reduced methylglyoxal, another possible natural substrate ( M. expansa lacks glyoxalase I activity). The parasite enzyme may help form a final line of defence against cytotoxic aldehydes arising from host immune initiated lipid peroxidation.
J Barrett - One of the best experts on this subject based on the ideXlab platform.
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characterisation and properties of an intracellular lipid binding protein from the tapeworm Moniezia expansa
FEBS Journal, 1997Co-Authors: J Barrett, Nahid Saghir, Anna Timanova, Katie Clarke, Peter M BrophyAbstract:The tapeworm Moniezia expansa contains an extremely abundant cytoplasmic lipid-binding protein (LBP). It is a small protein consisting of 66 amino acids with a molecular mass of 7943 ± 1.5Da. The amino acid sequence has been established by Edman degradation and confirmed by PCR analysis. The Moniezia LBP shows no sequence similarity with any previously described binding protein, but does show similarity with antigen B from Echinococcus glanulosus and Echinococcus multilocularis and with Taenia crassiceps antigen. The predicted structure for Moniezia LBP shows four helices and a putative tyrosine kinase site on the loop between helix 1 and 2. Each of the four helices has a well defined hydrophobic face. Studies with fluorescent probes suggest a single hydrophobic binding site. Results indicate that the single tryptophan residue in the molecule (Trp41) is involved in ligand binding, and calculation of the Stern-Volmer quenching constant shows that Trp41 is in a relatively hydrophobic environment.
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the purification and properties of glutathione reductase from the cestode Moniezia expansa
The International Journal of Biochemistry & Cell Biology, 1995Co-Authors: Mora J Mccallum, J BarrettAbstract:Abstract Glutathione reductase has a central role in glutathione metabolism and as such is a potential target for chemotherapy. The aim of the work was to purify and characterise glutathione reductase from the cestode Moniezia expansa and to compare the properties of the helminth enzyme with its mammalian counterpart. The enzyme was purified by a combination of anion exchange and affinity chromatography and further characterized by chromatofocusing and gel electrophoresis. Analysis revealed a single isoenzyme of glutathione reductase in Moniezia expansa, with a pI of 5.8. The enzyme was a homodimer of native molecular weight 114 kDa, subunit weight 63 kDa. Enzyme activity was affected by buffer concentration and the presence of monovalent sodium salts. The pH optimum was 7.4 with NADPH as cofactor and 5 with NADH. The Kma for oxidized glutathione was 76 μM and for NADPH and NADH, 21 and 350 μM respectively. In addition to oxidized glutathione only the mixed disulphide between CoA and glutathione (CoASSG) showed any significant activity as substrate. The cestode enzyme was inhibited by a variety of compounds including arsonic derivatives, 2,4,6 trinitrobenzene sulfonate 1,3-bis (2-chlorethyl)-1-nitrosourea and oxidized glutathione. In conclusion the glutathione reductase of M. expansa resembles the mammalian enzyme in its general physical properties and its substrate and inhibitor profile. However, the parasite enzyme shows an unusually high activity with the mixed disulphide of coenzyme A and glutathione (CoASSG) and appears to be more sensitive to inhibition by sodium ions.
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a novel nadph nadh dependent aldehyde reduction enzyme isolated from the tapeworm Moniezia expansa
FEBS Letters, 1990Co-Authors: Peter M Brophy, Paul Crowley, J BarrettAbstract:Abstract An aldehyde reduction enzyme has been purified from the cytosol of the tapeworm, Moniezia expansa , by chromatofocusing and Reactive-Red chromatography. The enzyme is monomeric (subunit 34 kDa) and can utilise NADH and NADPH as co-factors. Substrates of the enzyme include alkanals, alka-2,4-dienals and alk-2-enals, established secondary products of lipid peroxidation. The enzyme reduced methylglyoxal, another possible natural substrate ( M. expansa lacks glyoxalase I activity). The parasite enzyme may help form a final line of defence against cytotoxic aldehydes arising from host immune initiated lipid peroxidation.
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A novel NADPH/NADH-dependent aldehyde reduction enzyme isolated from the tapeworm Moniezia expansa
FEBS Letters, 1990Co-Authors: Peter M Brophy, Paul Crowley, J BarrettAbstract:Abstract An aldehyde reduction enzyme has been purified from the cytosol of the tapeworm, Moniezia expansa , by chromatofocusing and Reactive-Red chromatography. The enzyme is monomeric (subunit 34 kDa) and can utilise NADH and NADPH as co-factors. Substrates of the enzyme include alkanals, alka-2,4-dienals and alk-2-enals, established secondary products of lipid peroxidation. The enzyme reduced methylglyoxal, another possible natural substrate ( M. expansa lacks glyoxalase I activity). The parasite enzyme may help form a final line of defence against cytotoxic aldehydes arising from host immune initiated lipid peroxidation.
Aaron G Maule - One of the best experts on this subject based on the ideXlab platform.
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The nervous system of Tricladida. I. Neuroanatomy ofProcerodes littoralis (Maricola, Procerodidae): An immunocytochemical study
Invertebrate Neuroscience, 1995Co-Authors: Maria Reuter, Aaron G Maule, Margaretha K. S. Gustafsson, Cecilia Sahlgren, David W. Halton, Chris ShawAbstract:The organization of the nervous system of Procerodes littoralis (Tricladida, Maricola, Procerodidae) was studied by immunocytochemistry, using antibodies to authentic flatworm neuropeptide F (NPF) ( Moniezia expansa ). Compared to earlier investigations of the neuroanatomy of tricladid flatworms, the pattern of NPF immunoreactivity in Procerodes littoralis reveals differences in the following respects: 1. Shape and structure of the brain. 2. Number and composition of longitudinal nerve cords. 3. Shape of branches of, and transverse connections between, main ventral nerve cords. 4. Composition of the pharyngeal nervous system. The rich innervation by NPF immunoreactive (IR) fibres and cells of the subepithelial muscle layer, the pharynx musculature and the musculature of the male copulatory apparatus indicates a neurotransmitter or neuromodulatory influence on muscular activity.
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gnffrfamide a novel fmrfamide immunoreactive peptide isolated from the sheep tapeworm Moniezia expansa
Biochemical and Biophysical Research Communications, 1993Co-Authors: Aaron G Maule, C Shaw, D W Halton, L ThimAbstract:Abstract The widespread distribution of FMRFamide-immunoreactivity in platyhelminth nervous systems has been demonstrated immunocytochemically. Here we report the isolation and primary structure of the first platyhelminth FMRFamide-related peptide (FaRP) from the tapeworm, Moniezia expansa. The peptide was found to have a molecular mass of 785 Da and a primary structure of Gly-Asn-Phe-Phe-Arg-Phe-NH2 (GNFFRFamide). Acid alcohol extracts of this platyhelminth contained only this single FaRP which had a phenylalanyl (F) residue in the variable position 3 from the C-terminal occupied by either methionyl (M), leucyl (L) or isoleucyl (I) residues in most other FaRPs.
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the cholinergic serotoninergic and peptidergic components of the nervous system of Moniezia expansa cestoda cyclophyllidea
Parasitology, 1993Co-Authors: Aaron G Maule, C Shaw, D W Halton, C F JohnstonAbstract:The central (CNS) and peripheral (PNS) nervous systems of the cyclophyllidean tapeworm, Moniezia expansa, were examined for the presence of cholinergic, serotoninergic and peptidergic elements using enzyme cytochemical and immunocytochemical techniques in conjunction with light and confocal scanning laser microscopv. Cholinesterase activity and 5-hydroxytryptamine- and regulatory peptide-immunoreactivities (IRs) were localized to the nerve fibres and cell bodies of all of the major neuronal components in the CNS of the worm, including the cerebral ganglia and connecting commissure, the 10 longitudinal nerve cords and associated transverse ring commissures
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distribution and immunochemical characteristics of neuropeptide f npf Moniezia expansa immunoreactivity in proteocephalus pollanicola cestoda proteocephalidea
Comparative Biochemistry and Physiology Part C: Comparative Pharmacology, 1993Co-Authors: Nicola Marks, Aaron G Maule, C Shaw, D W Halton, C F JohnstonAbstract:1. Using immunocytochemical techniques and confocal scanning laser microscopy, the proteocephalidean cestode, Proteocephalus pollanicola from Lough Neagh pollan (Coregonus autumnalis) was examined for the presence of the native platyhelminth neuropeptide, neuropeptide F (NPF). 2. An antiserum specific for whole-molecule NPF(1–39) (Moniezia expansa) did not immunostain nerve processes in P. pollanicola. A C-terminally-directed NPF(30–39) (M. expansa) antiserum immunostained nerve fibres and cell bodies of both the central and peripheral nervous systems, including innervation associated with the female reproductive system. 3. The pattern of immunoreactivity was identical to that obtained using antisera to the C-terminal region of mammalian NPY-superfamily peptides and the invertebrate neuropeptide, FMRFamide. 4. Under radioimmunoassay conditions, only the C-terminally-directed NPF antiserum cross-reacted with the P. pollanicola peptide and detected 58.74 ngg wet weight of NPF-IR in extracts of the worm. 5. Chromatographic characterisation of P. pollanicola NPF-immunoreactivity indicated an apparent molecular weight of 4400–4700 Da, similar to that of NPF (M. expansa). 6. Further analytical HPLC characterisation identified two molecular forms of P. pollanicola NPF-immunoreactivity, both of which had different retention times from those of NPF (M. expansa) and NPF (Artioposthia triangulata). 7. These data suggest that P. pollanicola possesses a neuropeptide which is homologous in its C-terminal region to NPF (M. expansa) but diners in its mid- to N-terminal region.
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neuropeptide f Moniezia expansa localization and characterization using specific antisera
Parasitology, 1992Co-Authors: Aaron G Maule, C Shaw, D W Halton, C F Johnston, Gerard Brennan, S MooreAbstract:Immunocytochemical techniques used in conjunction with confocal scanning laser microscopy (CSLM) and electron microscopy have been used to demonstrate, for the first time, the distribution of the parasitic platyhelminth neuropeptide, neuropeptide F (NPF) in the cestode, Moniezia expansa . Antisera were raised to intact NPF(1–39) and to the C-terminal decapeptide of NPF(30–39). These antisera were characterized and validated for use in both immunocytochemistry and radioimmunoassay (RIA). NPF immunoreactivity (IR) was detected using both antisera throughout all of the major components of the central and peripheral nervous systems of the worm. The pattern of NPF-IR was found to mirror the IR obtained using a C-terminally directed pancreatic polypeptide (PP) antiserum and FMRFamide antisera; blocking studies using these antisera revealed that FMRFamide and PP antisera cross-react with NPF( M. expansa ). RIA of acid-alcohol extracts of the worm measured 114 ng/g using the C-terminal NPF antiserum and 56 ng/g using the whole-molecule-directed antiserum. While the C-terminally-directed NPF antiserum cross-reacts with NPF-related peptides from other invertebrates, the whole-molecule-directed NPF antiserum is specific for NPF( M. expansa ). The C-terminal NPF antiserum has potential for use in the identification and purification of NPF analogues from other platyhelminth parasites.
Iva Langrova - One of the best experts on this subject based on the ideXlab platform.
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effect of lead in water on the absorption of copper iron manganese and zinc by sheep ovis aries infected with sheep tapeworm Moniezia expansa
Experimental Parasitology, 2012Co-Authors: Ivana Jankovska, J Vadlejch, Jiřina Szakova, Iva Langrova, Zuzana Cadkova, D Lukesova, Petr Valek, Miloslav PetrtýlAbstract:The sheep tapeworm (Moniezia expansa) and its host Ovis aries were analyzed by inductively coupled plasma optical emission spectrometry (ICP-OES) for their copper, iron, manganese, zinc and lead levels. Element concentrations in cestode parasites were compared to those in various organs (liver, kidney, and muscle) of sheep. Tapeworms in the small intestine of sheep that were administered 2 g of Pb(CH3COO)2 per os daily (7 days) had significantly higher lead concentrations than sheep tissues. Cu levels significantly increased after Pb administration in sheep muscle and sheep tapeworms. Contrarily, Zn content significantly decreased in sheep muscle, but significantly increased in sheep tapeworms. However, Mn content significantly decreased after Pb administration in sheep tapeworms. Furthermore, Fe content significantly decreased after Pb administration in sheep liver and kidneys.
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experimental studies on the cadmium accumulation in the cestode Moniezia expansa cestoda anoplocephalidae and its final host ovis aries
Experimental Parasitology, 2010Co-Authors: Ivana Jankovska, J Vadlejch, Jiřina Szakova, D Miholova, P Kunc, I Knižkova, Zuzana Cadkova, Iva LangrovaAbstract:Abstract The tapeworm Moniezia expansa and naturally infected sheep were investigated with respect to their cadmium accumulation. Cadmium chloride (CdCl2, 0.2 g) was added to 10 ml of distilled water and administered orally to the sheep every day for a period of 1 week. The cadmium content of M. expansa was lower than that in the liver tissues of sheep, although this difference was not significant. The highest mean cadmium concentrations were found in the liver of sheep infected with M. expansa (24.5 ± 11.5 mg kg−1 dry weight). The mean cadmium concentration measured in M. expansa was 21.5 ± 19.2 mg kg−1 dry weight, which was 31 and 1.5 times higher than levels determined in the muscle and kidney of the host, respectively, but 0.9 times lower than levels determined in the liver of host. Sheeps with M. expansa infection always had higher cadmium concentrations in the tissues (with the exception of the blood) than their uninfected conspecifics.
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experimental studies on the lead accumulation in the cestode Moniezia expansa cestoda anoplocephalidae and its final host ovis aries
Ecotoxicology, 2010Co-Authors: Ivana Jankovska, J Vadlejch, Jiřina Szakova, D Miholova, P Kunc, I Knižkova, Iva LangrovaAbstract:The tapeworm Moniezia expansa and naturally infected sheep were investigated with respect to their lead accumulation. Lead—Pb(CH3COO)2 was added to the distilled water and administered orally to the sheep every day for a period of 1 week. After the exposure period the sheep were killed and the metal levels were determined in the muscle, liver, kidney and blood of the sheep as well as in the cestode parasites (Moniezia expansa). The impact of an infection with the cestode Moniezia expansa and a simultaneous Pb exposure, on the concentrations of heavy metals in the host kidney, liver, muscle, blood and cestodes was studied. The concentration of lead in the cestodes was on average 458, 5 and 4-fold higher in the cestodes than in the muscle, liver and kidney of the host, respectively. Parasitised sheep accumulated significantly less lead in their tissues than their uninfected conspecifics (ANOVA test, P ≤ 0.05). Also the differences between host′s tissues and tapeworms were found to be significant (ANOVA test, P ≤ 0.05). Thus, this study reveals that lead accumulation also occurs in cestodes parasitizing mammals. The host-parasite-system sheep-Moniezia expansa appears to be a useful and promising bioindication system especially in farming (rural, agricultural) and the natural ecosystem.
C Shaw - One of the best experts on this subject based on the ideXlab platform.
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gnffrfamide a novel fmrfamide immunoreactive peptide isolated from the sheep tapeworm Moniezia expansa
Biochemical and Biophysical Research Communications, 1993Co-Authors: Aaron G Maule, C Shaw, D W Halton, L ThimAbstract:Abstract The widespread distribution of FMRFamide-immunoreactivity in platyhelminth nervous systems has been demonstrated immunocytochemically. Here we report the isolation and primary structure of the first platyhelminth FMRFamide-related peptide (FaRP) from the tapeworm, Moniezia expansa. The peptide was found to have a molecular mass of 785 Da and a primary structure of Gly-Asn-Phe-Phe-Arg-Phe-NH2 (GNFFRFamide). Acid alcohol extracts of this platyhelminth contained only this single FaRP which had a phenylalanyl (F) residue in the variable position 3 from the C-terminal occupied by either methionyl (M), leucyl (L) or isoleucyl (I) residues in most other FaRPs.
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The cholinergic, serotoninergic and peptidergic components of the nervous system of Moniezia expansa (Cestoda, Cyclophyllidea).
Parasitology, 1993Co-Authors: A G Maule, C Shaw, D W Halton, C F JohnstonAbstract:The central (CNS) and peripheral (PNS) nervous systems of the cyclophyllidean tapeworm, Moniezia expansa, were examined for the presence of cholinergic, serotoninergic and peptidergic elements using enzyme cytochemical and immunocytochemical techniques in conjunction with light and confocal scanning laser microscopy. Cholinesterase activity and 5-hydroxytryptamine- and regulatory peptide-immunoreactivities (IRs) were localized to the nerve fibres and cell bodies of all of the major neuronal components in the CNS of the worm, including the cerebral ganglia and connecting commissure, the 10 longitudinal nerve cords and associated transverse ring commissures. Although each of the 3 systems appeared well developed and comprised a significant portion of the nervous system, the serotoninergic constituent was the most highly developed, consisting of a vast array of nerve fibres and cell bodies distributed throughout the strobila of the worm. A close association of cholinesterase reactivity and peptide-IRs was evident throughout the CNS, indicating the possible co-localization of acetylcholine and neuropeptides. Within the PNS, cholinergic activity and serotoninergic- and peptidergic-IRs occurred in the subtegumental network of nerve fibres and somatic musculature. Although all 3 neurochemical elements were present in the acetabula, they were found in different nerve fibres; only cholinergic and peptidergic cell bodies were found. The common genital opening, vagina and ootype regions of the reproductive system displayed a rich innervation of all 3 types of neuronal populations. Within the peptidergic system, immunostaining with antisera raised to the C-terminus of the neuropeptide Y superfamily of peptides and the invertebrate peptides, neuropeptide F (M. expansa) and FMRFamide was the most prevalent. Limited positive-IR for substance P and neurokinin A were also recorded in the CNS of the worm.
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the cholinergic serotoninergic and peptidergic components of the nervous system of Moniezia expansa cestoda cyclophyllidea
Parasitology, 1993Co-Authors: Aaron G Maule, C Shaw, D W Halton, C F JohnstonAbstract:The central (CNS) and peripheral (PNS) nervous systems of the cyclophyllidean tapeworm, Moniezia expansa, were examined for the presence of cholinergic, serotoninergic and peptidergic elements using enzyme cytochemical and immunocytochemical techniques in conjunction with light and confocal scanning laser microscopv. Cholinesterase activity and 5-hydroxytryptamine- and regulatory peptide-immunoreactivities (IRs) were localized to the nerve fibres and cell bodies of all of the major neuronal components in the CNS of the worm, including the cerebral ganglia and connecting commissure, the 10 longitudinal nerve cords and associated transverse ring commissures
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distribution and immunochemical characteristics of neuropeptide f npf Moniezia expansa immunoreactivity in proteocephalus pollanicola cestoda proteocephalidea
Comparative Biochemistry and Physiology Part C: Comparative Pharmacology, 1993Co-Authors: Nicola Marks, Aaron G Maule, C Shaw, D W Halton, C F JohnstonAbstract:1. Using immunocytochemical techniques and confocal scanning laser microscopy, the proteocephalidean cestode, Proteocephalus pollanicola from Lough Neagh pollan (Coregonus autumnalis) was examined for the presence of the native platyhelminth neuropeptide, neuropeptide F (NPF). 2. An antiserum specific for whole-molecule NPF(1–39) (Moniezia expansa) did not immunostain nerve processes in P. pollanicola. A C-terminally-directed NPF(30–39) (M. expansa) antiserum immunostained nerve fibres and cell bodies of both the central and peripheral nervous systems, including innervation associated with the female reproductive system. 3. The pattern of immunoreactivity was identical to that obtained using antisera to the C-terminal region of mammalian NPY-superfamily peptides and the invertebrate neuropeptide, FMRFamide. 4. Under radioimmunoassay conditions, only the C-terminally-directed NPF antiserum cross-reacted with the P. pollanicola peptide and detected 58.74 ngg wet weight of NPF-IR in extracts of the worm. 5. Chromatographic characterisation of P. pollanicola NPF-immunoreactivity indicated an apparent molecular weight of 4400–4700 Da, similar to that of NPF (M. expansa). 6. Further analytical HPLC characterisation identified two molecular forms of P. pollanicola NPF-immunoreactivity, both of which had different retention times from those of NPF (M. expansa) and NPF (Artioposthia triangulata). 7. These data suggest that P. pollanicola possesses a neuropeptide which is homologous in its C-terminal region to NPF (M. expansa) but diners in its mid- to N-terminal region.
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neuropeptide f Moniezia expansa localization and characterization using specific antisera
Parasitology, 1992Co-Authors: Aaron G Maule, C Shaw, D W Halton, C F Johnston, Gerard Brennan, S MooreAbstract:Immunocytochemical techniques used in conjunction with confocal scanning laser microscopy (CSLM) and electron microscopy have been used to demonstrate, for the first time, the distribution of the parasitic platyhelminth neuropeptide, neuropeptide F (NPF) in the cestode, Moniezia expansa . Antisera were raised to intact NPF(1–39) and to the C-terminal decapeptide of NPF(30–39). These antisera were characterized and validated for use in both immunocytochemistry and radioimmunoassay (RIA). NPF immunoreactivity (IR) was detected using both antisera throughout all of the major components of the central and peripheral nervous systems of the worm. The pattern of NPF-IR was found to mirror the IR obtained using a C-terminally directed pancreatic polypeptide (PP) antiserum and FMRFamide antisera; blocking studies using these antisera revealed that FMRFamide and PP antisera cross-react with NPF( M. expansa ). RIA of acid-alcohol extracts of the worm measured 114 ng/g using the C-terminal NPF antiserum and 56 ng/g using the whole-molecule-directed antiserum. While the C-terminally-directed NPF antiserum cross-reacts with NPF-related peptides from other invertebrates, the whole-molecule-directed NPF antiserum is specific for NPF( M. expansa ). The C-terminal NPF antiserum has potential for use in the identification and purification of NPF analogues from other platyhelminth parasites.