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Gregg T. Nagle - One of the best experts on this subject based on the ideXlab platform.
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characterization of Aplysia enticin and temptin two novel water borne protein pheromones that act in concert with attractin to stimulate mate attraction
Journal of Biological Chemistry, 2004Co-Authors: Scott F Cummins, Amy E. Nichols, Andinet Amare, Amanda B Hummon, Jonathan V Sweedler, Gregg T. NagleAbstract:Abstract Mate attraction in Aplysia involves a long-distance water-borne signal (attractin) that is released during egg laying. Other pheromones are predicted to be released during egg laying that act in concert with albumen gland attractin to stimulate attraction, but their identities are unknown. To identify other candidate water-borne pheromones, we employed differential library screening of an albumen gland cDNA library, Northern blot analysis, purification, characterization, cloning, and expression of albumen gland proteins, matrix-assisted laser desorption ionization mass spectrometry, pheromone secretion assays, behavioral bioassays, immunolocalization studies, and comparative genomics. Four genes, Alb-23, Alb-24, Alb-69, and Alb-172, were highly expressed in Aplysia californica albumen glands and encoded novel proteins. The products of the Alb-24 (“enticin”) and Alb-172 (“temptin”) precursors were soluble and highly abundant in albumen gland extracts, whereas Alb-23 and Alb-69 were membrane-associated proteins. A comparative analysis showed that the predicted Aplysia brasiliana enticin and temptin proteins were 90 and 91% identical, respectively, to their A. californica homologs. T-maze attraction bioassay studies have previously demonstrated that egg cordons alone are attractive to Aplysia but that attractin alone is not. In the present study, however, the combination of attractin, enticin, and temptin was found to be significantly attractive to potential mates and doubled the number of animals attracted to this stimulus compared with control animals. The combined data strongly suggest that enticin and temptin are novel candidate water-borne protein pheromones that act in concert with attractin to attract Aplysia to form and maintain egglaying and mating aggregations.
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A conserved heptapeptide sequence in the waterborne attractin pheromone stimulates mate attraction in Aplysia
Peptides, 2004Co-Authors: Scott F Cummins, Amy E. Nichols, Krishna Rajarathnam, Gregg T. NagleAbstract:Mate attraction in the marine mollusk Aplysia involves long-distance waterborne chemical signaling via the release of the peptide pheromone attractin during egg laying. Aplysia californica attractin attracts conspecifics, reduces the latency to mating, and stimulates hermaphroditic mating. Four additional members of the Aplysia attractin family have recently been characterized from Aplysia brasiliana, Aplysia fasciata, Aplysia depilans, and Aplysia vaccaria. The five sequences differ significantly, but share six cysteine residues and the strictly conserved sequence Ile 30 -Glu-Glu-Cys-Lys-Thr-Ser 36 . Attractin is attractive to geographically and evolutionarily distant species, suggesting that the conserved heptapeptide region may be important for mate attraction. Consistent with this prediction, a synthetic constrained cyclic peptide that contains the conserved heptapeptide sequence is significantly attractive in T-maze bioassays. The attractins are the first family of waterborne peptide pheromones characterized in invertebrates and are unique in that family members are not species-specific pheromonal attractants. © 2004 Elsevier Inc. All rights reserved.
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A conserved heptapeptide sequence in the waterborne attractin pheromone stimulates mate attraction in Aplysia.
Peptides, 2004Co-Authors: Scott F Cummins, Amy E. Nichols, Krishna Rajarathnam, Gregg T. NagleAbstract:Mate attraction in the marine mollusk Aplysia involves long-distance waterborne chemical signaling via the release of the peptide pheromone attractin during egg laying. Aplysia californica attractin attracts conspecifics, reduces the latency to mating, and stimulates hermaphroditic mating. Four additional members of the Aplysia attractin family have recently been characterized from Aplysia brasiliana, Aplysia fasciata, Aplysia depilans, and Aplysia vaccaria. The five sequences differ significantly, but share six cysteine residues and the strictly conserved sequence Ile30-Glu-Glu-Cys-Lys-Thr-Ser36. Attractin is attractive to geographically and evolutionarily distant species, suggesting that the conserved heptapeptide region may be important for mate attraction. Consistent with this prediction, a synthetic constrained cyclic peptide that contains the conserved heptapeptide sequence is significantly attractive in T-maze bioassays. The attractins are the first family of waterborne peptide pheromones characterized in invertebrates and are unique in that family members are not species-specific pheromonal attractants.
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Characterization of Aplysia carboxypeptidase E
FEBS Letters, 1997Co-Authors: Shailaja Rao Juvvadi, Gregg T. Nagle, Xuemo Fan, Lloyd D. FrickerAbstract:Abstract Carboxypeptidase E (CPE) is involved in the biosynthesis of peptide hormones and neurotransmitters. To determine whether a recently reported Aplysia californica cDNA encodes a CPE-like enzyme, this cDNA was expressed in the baculovirus system. The Aplysia CPE is optimal at pH 5.5–6.5 and is inhibited by chelating agents and by the sulfhydryl reagent p-chloromercuriphenyl sulfonate. The effect of divalent cations and active site-directed inhibitors on enzyme activity are generally similar for Aplysia and rat CPE. Western blot analysis using antisera to the N- and C-terminal regions of the Aplysia CPE show that the Aplysia CPE is present in atrial glands and ovotestis. This Aplysia CPE is purified on a p-aminobenzoyl–Arg Sepharose affinity column under conditions that selectively purify rat CPE. Taken together, these results suggest that the previously cloned cDNA represents a CPE-like enzyme that is expressed in Aplysia tissue.
Scott F Cummins - One of the best experts on this subject based on the ideXlab platform.
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characterization of Aplysia enticin and temptin two novel water borne protein pheromones that act in concert with attractin to stimulate mate attraction
Journal of Biological Chemistry, 2004Co-Authors: Scott F Cummins, Amy E. Nichols, Andinet Amare, Amanda B Hummon, Jonathan V Sweedler, Gregg T. NagleAbstract:Abstract Mate attraction in Aplysia involves a long-distance water-borne signal (attractin) that is released during egg laying. Other pheromones are predicted to be released during egg laying that act in concert with albumen gland attractin to stimulate attraction, but their identities are unknown. To identify other candidate water-borne pheromones, we employed differential library screening of an albumen gland cDNA library, Northern blot analysis, purification, characterization, cloning, and expression of albumen gland proteins, matrix-assisted laser desorption ionization mass spectrometry, pheromone secretion assays, behavioral bioassays, immunolocalization studies, and comparative genomics. Four genes, Alb-23, Alb-24, Alb-69, and Alb-172, were highly expressed in Aplysia californica albumen glands and encoded novel proteins. The products of the Alb-24 (“enticin”) and Alb-172 (“temptin”) precursors were soluble and highly abundant in albumen gland extracts, whereas Alb-23 and Alb-69 were membrane-associated proteins. A comparative analysis showed that the predicted Aplysia brasiliana enticin and temptin proteins were 90 and 91% identical, respectively, to their A. californica homologs. T-maze attraction bioassay studies have previously demonstrated that egg cordons alone are attractive to Aplysia but that attractin alone is not. In the present study, however, the combination of attractin, enticin, and temptin was found to be significantly attractive to potential mates and doubled the number of animals attracted to this stimulus compared with control animals. The combined data strongly suggest that enticin and temptin are novel candidate water-borne protein pheromones that act in concert with attractin to attract Aplysia to form and maintain egglaying and mating aggregations.
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structural and functional analysis of Aplysia attractins a family of water borne protein pheromones with interspecific attractiveness
Proceedings of the National Academy of Sciences of the United States of America, 2004Co-Authors: Sherry D Painter, Amy E. Nichols, Scott F Cummins, David B G Akalal, Catherine H Schein, Werner Braun, John S Smith, Abraham J Susswein, Miriam Levy, Pamela A C M De BoerAbstract:Mate attraction in Aplysia involves a long-distance water-borne signal (the protein pheromone attractin), which is released during egg laying. Aplysia californica attractin attracts species that produce closely related attractins, such as Aplysia brasiliana, whose geographic distribution does not overlap that of A. californica. This finding suggests that other mollusks release attractin-related pheromones to form and maintain breeding aggregations. We describe four additional members of the attractin family: A. brasiliana, Aplysia fasciata, Aplysia depilans (which aggregates with A. fasciata aggregations), and Aplysia vaccaria (which aggregates with A. californica aggregations). On the basis of their sequence similarity with A. californica attractin, the attractin proteins fall into two groups: A. californica, A. brasiliana, and A. fasciata (91-95% identity), and A. depilans and A. vaccaria (41-43% identity). The sequence similarity within the attractin family, the conserved six cysteines, and the compact fold of the NMR solution structure of A. californica attractin suggest a common fold for this pheromone family containing two antiparallel helices. The second helix contains the IEECKTS sequence conserved in Aplysia attractins. Mutating surface-exposed charged residues within this heptapeptide sequence abolishes attractin activity, suggesting that the second helix is an essential part of the receptor-binding interface.
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A conserved heptapeptide sequence in the waterborne attractin pheromone stimulates mate attraction in Aplysia
Peptides, 2004Co-Authors: Scott F Cummins, Amy E. Nichols, Krishna Rajarathnam, Gregg T. NagleAbstract:Mate attraction in the marine mollusk Aplysia involves long-distance waterborne chemical signaling via the release of the peptide pheromone attractin during egg laying. Aplysia californica attractin attracts conspecifics, reduces the latency to mating, and stimulates hermaphroditic mating. Four additional members of the Aplysia attractin family have recently been characterized from Aplysia brasiliana, Aplysia fasciata, Aplysia depilans, and Aplysia vaccaria. The five sequences differ significantly, but share six cysteine residues and the strictly conserved sequence Ile 30 -Glu-Glu-Cys-Lys-Thr-Ser 36 . Attractin is attractive to geographically and evolutionarily distant species, suggesting that the conserved heptapeptide region may be important for mate attraction. Consistent with this prediction, a synthetic constrained cyclic peptide that contains the conserved heptapeptide sequence is significantly attractive in T-maze bioassays. The attractins are the first family of waterborne peptide pheromones characterized in invertebrates and are unique in that family members are not species-specific pheromonal attractants. © 2004 Elsevier Inc. All rights reserved.
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A conserved heptapeptide sequence in the waterborne attractin pheromone stimulates mate attraction in Aplysia.
Peptides, 2004Co-Authors: Scott F Cummins, Amy E. Nichols, Krishna Rajarathnam, Gregg T. NagleAbstract:Mate attraction in the marine mollusk Aplysia involves long-distance waterborne chemical signaling via the release of the peptide pheromone attractin during egg laying. Aplysia californica attractin attracts conspecifics, reduces the latency to mating, and stimulates hermaphroditic mating. Four additional members of the Aplysia attractin family have recently been characterized from Aplysia brasiliana, Aplysia fasciata, Aplysia depilans, and Aplysia vaccaria. The five sequences differ significantly, but share six cysteine residues and the strictly conserved sequence Ile30-Glu-Glu-Cys-Lys-Thr-Ser36. Attractin is attractive to geographically and evolutionarily distant species, suggesting that the conserved heptapeptide region may be important for mate attraction. Consistent with this prediction, a synthetic constrained cyclic peptide that contains the conserved heptapeptide sequence is significantly attractive in T-maze bioassays. The attractins are the first family of waterborne peptide pheromones characterized in invertebrates and are unique in that family members are not species-specific pheromonal attractants.
Amy E. Nichols - One of the best experts on this subject based on the ideXlab platform.
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characterization of Aplysia enticin and temptin two novel water borne protein pheromones that act in concert with attractin to stimulate mate attraction
Journal of Biological Chemistry, 2004Co-Authors: Scott F Cummins, Amy E. Nichols, Andinet Amare, Amanda B Hummon, Jonathan V Sweedler, Gregg T. NagleAbstract:Abstract Mate attraction in Aplysia involves a long-distance water-borne signal (attractin) that is released during egg laying. Other pheromones are predicted to be released during egg laying that act in concert with albumen gland attractin to stimulate attraction, but their identities are unknown. To identify other candidate water-borne pheromones, we employed differential library screening of an albumen gland cDNA library, Northern blot analysis, purification, characterization, cloning, and expression of albumen gland proteins, matrix-assisted laser desorption ionization mass spectrometry, pheromone secretion assays, behavioral bioassays, immunolocalization studies, and comparative genomics. Four genes, Alb-23, Alb-24, Alb-69, and Alb-172, were highly expressed in Aplysia californica albumen glands and encoded novel proteins. The products of the Alb-24 (“enticin”) and Alb-172 (“temptin”) precursors were soluble and highly abundant in albumen gland extracts, whereas Alb-23 and Alb-69 were membrane-associated proteins. A comparative analysis showed that the predicted Aplysia brasiliana enticin and temptin proteins were 90 and 91% identical, respectively, to their A. californica homologs. T-maze attraction bioassay studies have previously demonstrated that egg cordons alone are attractive to Aplysia but that attractin alone is not. In the present study, however, the combination of attractin, enticin, and temptin was found to be significantly attractive to potential mates and doubled the number of animals attracted to this stimulus compared with control animals. The combined data strongly suggest that enticin and temptin are novel candidate water-borne protein pheromones that act in concert with attractin to attract Aplysia to form and maintain egglaying and mating aggregations.
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structural and functional analysis of Aplysia attractins a family of water borne protein pheromones with interspecific attractiveness
Proceedings of the National Academy of Sciences of the United States of America, 2004Co-Authors: Sherry D Painter, Amy E. Nichols, Scott F Cummins, David B G Akalal, Catherine H Schein, Werner Braun, John S Smith, Abraham J Susswein, Miriam Levy, Pamela A C M De BoerAbstract:Mate attraction in Aplysia involves a long-distance water-borne signal (the protein pheromone attractin), which is released during egg laying. Aplysia californica attractin attracts species that produce closely related attractins, such as Aplysia brasiliana, whose geographic distribution does not overlap that of A. californica. This finding suggests that other mollusks release attractin-related pheromones to form and maintain breeding aggregations. We describe four additional members of the attractin family: A. brasiliana, Aplysia fasciata, Aplysia depilans (which aggregates with A. fasciata aggregations), and Aplysia vaccaria (which aggregates with A. californica aggregations). On the basis of their sequence similarity with A. californica attractin, the attractin proteins fall into two groups: A. californica, A. brasiliana, and A. fasciata (91-95% identity), and A. depilans and A. vaccaria (41-43% identity). The sequence similarity within the attractin family, the conserved six cysteines, and the compact fold of the NMR solution structure of A. californica attractin suggest a common fold for this pheromone family containing two antiparallel helices. The second helix contains the IEECKTS sequence conserved in Aplysia attractins. Mutating surface-exposed charged residues within this heptapeptide sequence abolishes attractin activity, suggesting that the second helix is an essential part of the receptor-binding interface.
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A conserved heptapeptide sequence in the waterborne attractin pheromone stimulates mate attraction in Aplysia
Peptides, 2004Co-Authors: Scott F Cummins, Amy E. Nichols, Krishna Rajarathnam, Gregg T. NagleAbstract:Mate attraction in the marine mollusk Aplysia involves long-distance waterborne chemical signaling via the release of the peptide pheromone attractin during egg laying. Aplysia californica attractin attracts conspecifics, reduces the latency to mating, and stimulates hermaphroditic mating. Four additional members of the Aplysia attractin family have recently been characterized from Aplysia brasiliana, Aplysia fasciata, Aplysia depilans, and Aplysia vaccaria. The five sequences differ significantly, but share six cysteine residues and the strictly conserved sequence Ile 30 -Glu-Glu-Cys-Lys-Thr-Ser 36 . Attractin is attractive to geographically and evolutionarily distant species, suggesting that the conserved heptapeptide region may be important for mate attraction. Consistent with this prediction, a synthetic constrained cyclic peptide that contains the conserved heptapeptide sequence is significantly attractive in T-maze bioassays. The attractins are the first family of waterborne peptide pheromones characterized in invertebrates and are unique in that family members are not species-specific pheromonal attractants. © 2004 Elsevier Inc. All rights reserved.
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A conserved heptapeptide sequence in the waterborne attractin pheromone stimulates mate attraction in Aplysia.
Peptides, 2004Co-Authors: Scott F Cummins, Amy E. Nichols, Krishna Rajarathnam, Gregg T. NagleAbstract:Mate attraction in the marine mollusk Aplysia involves long-distance waterborne chemical signaling via the release of the peptide pheromone attractin during egg laying. Aplysia californica attractin attracts conspecifics, reduces the latency to mating, and stimulates hermaphroditic mating. Four additional members of the Aplysia attractin family have recently been characterized from Aplysia brasiliana, Aplysia fasciata, Aplysia depilans, and Aplysia vaccaria. The five sequences differ significantly, but share six cysteine residues and the strictly conserved sequence Ile30-Glu-Glu-Cys-Lys-Thr-Ser36. Attractin is attractive to geographically and evolutionarily distant species, suggesting that the conserved heptapeptide region may be important for mate attraction. Consistent with this prediction, a synthetic constrained cyclic peptide that contains the conserved heptapeptide sequence is significantly attractive in T-maze bioassays. The attractins are the first family of waterborne peptide pheromones characterized in invertebrates and are unique in that family members are not species-specific pheromonal attractants.
Wayne S Sossin - One of the best experts on this subject based on the ideXlab platform.
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translation of 5 terminal oligopyrimidine tract 5 top mrnas in Aplysia californica is regulated by the target of rapamycin tor
Biochemical and Biophysical Research Communications, 2011Co-Authors: Margaret Labban, Wayne S SossinAbstract:Aplysia californica is a model organism for determining the molecular basis of memory. In this system identified synaptic changes have been closely linked to behavioral memories. Long-term sensitization and long-term synaptic changes between sensory neurons and motor neurons require both gene expression followed by translational control of the newly expressed mRNAs. One important mechanism for translational control is mediated through the target of rapamycin (TOR) and one mechanism downstream of TOR is the translational control of mRNAs containing a 5′ terminal oligopyrimidine tract (5′TOP) sequence in their mRNA transcript. These include all ribosomal proteins, elongation factors and a few other translational regulators. TOR regulation of 5′TOP mRNAs in vertebrates is thought to be due to TOR dependent removal of the translational repression mediated by the 5′TOP sequence. Here, we show that this mechanism is similar in Aplysia, whereby Aplysia 5′TOP mRNAs are repressed under basal conditions and this repression is removed by serotonin in a rapamycin-sensitive manner.
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Translation of 5′ terminal oligopyrimidine tract (5′TOP) mRNAs in Aplysia Californica is regulated by the target of rapamycin (TOR)
Biochemical and Biophysical Research Communications, 2010Co-Authors: Margaret Labban, Wayne S SossinAbstract:Aplysia californica is a model organism for determining the molecular basis of memory. In this system identified synaptic changes have been closely linked to behavioral memories. Long-term sensitization and long-term synaptic changes between sensory neurons and motor neurons require both gene expression followed by translational control of the newly expressed mRNAs. One important mechanism for translational control is mediated through the target of rapamycin (TOR) and one mechanism downstream of TOR is the translational control of mRNAs containing a 5′ terminal oligopyrimidine tract (5′TOP) sequence in their mRNA transcript. These include all ribosomal proteins, elongation factors and a few other translational regulators. TOR regulation of 5′TOP mRNAs in vertebrates is thought to be due to TOR dependent removal of the translational repression mediated by the 5′TOP sequence. Here, we show that this mechanism is similar in Aplysia, whereby Aplysia 5′TOP mRNAs are repressed under basal conditions and this repression is removed by serotonin in a rapamycin-sensitive manner.
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Mnk is a negative regulator of cap‐dependent translation in Aplysia neurons
Journal of Neurochemistry, 2006Co-Authors: Gabriel Ross, John R. Dyer, Vincent F. Castellucci, Wayne S SossinAbstract:To investigate the mechanisms underlying regulation of eukaryotic initiation factor 4E (eIF4E) phosphorylation in Aplysia neurons, we have cloned the Aplysia homolog of the vertebrate eIF4E kinases, Mnk1 and -2. Aplysia Mnk shares many conserved regions with vertebrate Mnk, including putative eukaryotic initiation factor 4G binding regions, activation loop phosphorylation sites, and a carboxy-terminal anchoring site for MAP kinases. As expected, purified Aplysia Mnk phosphorylated Aplysia eIF4E at a conserved carboxy-terminal serine and over-expression of Aplysia Mnk in sensory neurons led to increased phosphorylation of endogenous eIF4E. Over-expression of Aplysia Mnk led to strong decreases in cap-dependent translation, while generally sparing internal ribosomal entry site (IRES)-dependent translation. However, decreases in cap-dependent translation seen after expression of Aplysia Mnk could only be partly explained by increases in eIF4E phosphorylation. In Aplysia sensory neurons, phosphorylation of eIF4E is reduced during intermediate memory formation. However, we found that this physiological regulation of eIF4E phosphorylation was independent of changes in Aplysia Mnk phosphorylation. We propose that changes in eIF4E phosphorylation in Aplysia neurons are a consequence of changes in cap-dependent translation that are independent of regulation of Aplysia Mnk.
Pamela A C M De Boer - One of the best experts on this subject based on the ideXlab platform.
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structural and functional analysis of Aplysia attractins a family of water borne protein pheromones with interspecific attractiveness
Proceedings of the National Academy of Sciences of the United States of America, 2004Co-Authors: Sherry D Painter, Amy E. Nichols, Scott F Cummins, David B G Akalal, Catherine H Schein, Werner Braun, John S Smith, Abraham J Susswein, Miriam Levy, Pamela A C M De BoerAbstract:Mate attraction in Aplysia involves a long-distance water-borne signal (the protein pheromone attractin), which is released during egg laying. Aplysia californica attractin attracts species that produce closely related attractins, such as Aplysia brasiliana, whose geographic distribution does not overlap that of A. californica. This finding suggests that other mollusks release attractin-related pheromones to form and maintain breeding aggregations. We describe four additional members of the attractin family: A. brasiliana, Aplysia fasciata, Aplysia depilans (which aggregates with A. fasciata aggregations), and Aplysia vaccaria (which aggregates with A. californica aggregations). On the basis of their sequence similarity with A. californica attractin, the attractin proteins fall into two groups: A. californica, A. brasiliana, and A. fasciata (91-95% identity), and A. depilans and A. vaccaria (41-43% identity). The sequence similarity within the attractin family, the conserved six cysteines, and the compact fold of the NMR solution structure of A. californica attractin suggest a common fold for this pheromone family containing two antiparallel helices. The second helix contains the IEECKTS sequence conserved in Aplysia attractins. Mutating surface-exposed charged residues within this heptapeptide sequence abolishes attractin activity, suggesting that the second helix is an essential part of the receptor-binding interface.
