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The cAMP-protein kinase A (PKA) pathway is an important intracellular signal transduction cascade that can be activated by a large variety of stimuli. Activation or inhibition of this pathway will ultimately affect the transcriptional... more
The cAMP-protein kinase A (PKA) pathway is an important intracellular signal transduction cascade that can be activated by a large variety of stimuli. Activation or inhibition of this pathway will ultimately affect the transcriptional regulation of various genes through distinct responsive sites. In vertebrates, the best- characterized nuclear targets of PKA are the cyclic AMP response element-binding (CREB) proteins. It is now well established that CREB is not only regulated by PKA, but many other kinases can exert an effect as well. Since CREB-like proteins were also discovered in invertebrates, several studies unraveling their physiological functions in this category of metazoans have been performed. This review will mainly focus on the presence and regulation of CREB proteins in insects. Differences in transcriptional responses to the PKA pathway and other CREB-regulating stimuli between cells, tissues, and even organisms can be partially attributed to the presence of different CREB isoforms. In addition, the regulation of CREB appears to show some important differences between insects and vertebrates. Since CREB is a basic leucine zipper (bZip) protein, other insect members of this important family of transcriptional regulators will be briefly discussed as well.
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Manduca sexta allatotropin (Manse-AT) is a multifunctional neuropeptide whose actions include the stimulation of juvenile hormone biosynthesis, myotropic stimulation, cardioacceleratory functions, and inhibition of active ion transport.... more
Manduca sexta allatotropin (Manse-AT) is a multifunctional neuropeptide whose actions include the stimulation of juvenile hormone biosynthesis, myotropic stimulation, cardioacceleratory functions, and inhibition of active ion transport. Manse-AT is a member of a structurally related peptide family that is widely found in insects and also in other invertebrates. Its precise role depends on the insect species and developmental stage. In
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Based on a receptor interaction model, simplified analogues of insect kinins were prepared. The compounds were templated on a conformationally restricted amino piperidinone carboxylate scaffold. The conformation of the analogues was... more
Based on a receptor interaction model, simplified analogues of insect kinins were prepared. The compounds were templated on a conformationally restricted amino piperidinone carboxylate scaffold. The conformation of the analogues was studied by NMR and the biological activity of the compounds was tested in a bio-assay.
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The cDNA for Tyr-Loc, a G protein-coupled receptor that clearly shows homology to a number of mammalian and fruit fly receptors for biogenic amines, was cloned from the nervous system of Locusta migratoria. Functional expression of the... more
The cDNA for Tyr-Loc, a G protein-coupled receptor that clearly shows homology to a number of mammalian and fruit fly receptors for biogenic amines, was cloned from the nervous system of Locusta migratoria. Functional expression of the cloned cDNA was obtained in cultured insect cells, i.e., in Spodoptera SF9 cells using a baculoviral expression system and in stably transformed Drosophila Schneider 2 (S2) cells. Multiple copies of the receptor expression construct are inserted into the genome of these permanently transformed cells. The expression of the receptor cDNA was driven by the upstream sequences of a Bombyx mori baculoviral immediate early gene. Tyramine shows a much higher binding affinity to this receptor than other possible endogenous ligands. It also reduces forskolin-induced cyclic AMP production in the permanently transformed S2 cells. The pharmacological profile of the Tyr-Loc receptor is distinct from that of any locust receptor-type described so far, but it is similar to that of the Drosophila tyramine/octopamine receptor. In the locust CNS, the Tyr-Loc mRNA is not present in the distal part of the optic lobes but has a widespread distribution in the brain and the ventral nerve cord.
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Research Interests: Zoology, Calcium, Drosophila melanogaster, Serotonin, Dopamine, and 16 moreHistamine, Melatonin, Drosophila, cyclic AMP, Animals, Tyramine, Insect Biochemistry and Molecular Biology, Base Sequence, Octopamine, Second Messengers, Intracellular Signaling, Schneider, Insect Biochemistry, Biochemistry and cell biology, Adenosine monophosphate, and Adenylyl Cyclase
Research Interests: Zoology, Transcription Factors, Gene expression, Drosophila, Cell line, and 10 moreAnimals, Comparative Analysis, Insect Biochemistry and Molecular Biology, Transfection, Base Sequence, DNA binding proteins, Schneider, Insect Biochemistry, Biochemistry and cell biology, and Gene Expression Regulation
Research Interests: Zoology, Reproduction, Female, Animals, Polymerase Chain Reaction, and 13 moreJuvenile Hormone, Enzyme, Sesquiterpenes, Molecular cloning, Reproductive cycle, Digestive System, Insect Biochemistry and Molecular Biology, Amino Acid Sequence, Base Sequence, Grasshoppers, Catalytic Activity, Biochemistry and cell biology, and Proteolytic activity
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The FGLamide allatostatins (FGL/ASTs) are a family of neuropeptides with pleiotropic functions, including the inhibition of juvenile hormone (JH) biosynthesis, vitellogenesis and muscle contraction. In the cockroach, Diploptera punctata,... more
The FGLamide allatostatins (FGL/ASTs) are a family of neuropeptides with pleiotropic functions, including the inhibition of juvenile hormone (JH) biosynthesis, vitellogenesis and muscle contraction. In the cockroach, Diploptera punctata, thirteen FGLa/ASTs and one allatostatin receptor (AstR) have been identified. However, the mode of action of ASTs in regulation of JH biosynthesis remains unclear. Here, we determined the tissue distribution of Dippu-AstR. And we expressed Dippu-AstR in vertebrate cell lines, and activated the receptor with the Dippu-ASTs. Our results show that all thirteen ASTs activated Dippu-AstR in a dose dependent manner, albeit with different potencies. Functional analysis of AstR in multiple cell lines demonstrated that activation of the AstR receptor resulted in elevated levels of Ca(2+) and cAMP, which suggests that Dippu-AstR can act through the Gαq and Gαs protein pathways. The study on the target of AST action reveals that FGL/AST affects JH biosynthesis...
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Methoxyfenozide (RH-2485) is a non-steroidal ecdysteroid agonist with a dibenzoylhydrazine structure, representing a group used as novel biorational insecticides in the control of insect pests. Here we report on the selection of... more
Methoxyfenozide (RH-2485) is a non-steroidal ecdysteroid agonist with a dibenzoylhydrazine structure, representing a group used as novel biorational insecticides in the control of insect pests. Here we report on the selection of Drosophila melanogaster S2 cells for resistance to inhibition of cell proliferation by methoxyfenozide by ∼1000-fold over 4 months. Cells were exposed to gradually increasing concentrations of methoxyfenozide and
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The biogenic amine octopamine and its biological precursor tyramine are thought to be the invertebrate functional homologues of the vertebrate adrenergic transmitters. Octopamine functions as a neuromodulator, neurotransmitter and... more
The biogenic amine octopamine and its biological precursor tyramine are thought to be the invertebrate functional homologues of the vertebrate adrenergic transmitters. Octopamine functions as a neuromodulator, neurotransmitter and neurohormone in insect nervous systems and prompts the whole organism to “dynamic action”. A growing number of studies suggest a prominent role for octopamine in modulating multiple physiological and behavioural processes
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Members of the pacifastin family are serine peptidase inhibitors, found in arthropods and have many members within different insect orders. Based on their structural character- istics, inhibitors of this peptide family are divided into... more
Members of the pacifastin family are serine peptidase inhibitors, found in arthropods and have many members within different insect orders. Based on their structural character- istics, inhibitors of this peptide family are divided into two groups (I and II). Members of both groups exhibit specificity towards different types of serine peptidases. In addition, group I inhibitors display species selectivity. The
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An octapeptide was isolated from 7000 brains of the desert locust. Schistocerca gregaria by screening of HPLC fractions using a RIA for Dip-AST-2 (allatostatin-2 from the cockroach). Maldi-TOF-MS revealed a mass of 921.4 Da. The primary... more
An octapeptide was isolated from 7000 brains of the desert locust. Schistocerca gregaria by screening of HPLC fractions using a RIA for Dip-AST-2 (allatostatin-2 from the cockroach). Maldi-TOF-MS revealed a mass of 921.4 Da. The primary structure of the peptide is LPVYNFGL-NH2. It is identical to the C-terminal portion of schistostatin-2 from Schistocerca gregaria. Therefore, it was designated Scg-AST-2(11-18). The chromatographic properties of the synthetic peptide are identical to these of the native peptide. The peptide is a truncated product of Scg-AST-2, suggesting that an endopeptidase which cleaves between Arg and Leu is present in the brain complex of S. gregaria. Although, Scg-AST-2(11-18) contains the same C-terminus as Dip-AST-2, it has no inhibitory activity on the corpora allata (CA) of 2-day-old virgin females of D. punctata. This suggests that Scg-AST2 (11-18) may be the result of a proteolytic inactivation mechanism and/or that it may be involved in stage-dependent d...
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Members of the tachykinin peptide family have been well conserved during evolution and are mainly expressed in the central nervous system and in the intestine of both vertebrates and invertebrates. In these animals, they act as... more
Members of the tachykinin peptide family have been well conserved during evolution and are mainly expressed in the central nervous system and in the intestine of both vertebrates and invertebrates. In these animals, they act as multifunctional messengers that exert their biological effects by specifically interacting with a subfamily of structurally related G protein-coupled receptors. Despite the identification of multiple
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Leucine-rich repeats containing G protein-coupled receptors (LGRs) constitute a unique cluster of transmembrane proteins sharing a large leucine-rich extracellular domain for hormone binding. In mammals, LGRs steer important... more
Leucine-rich repeats containing G protein-coupled receptors (LGRs) constitute a unique cluster of transmembrane proteins sharing a large leucine-rich extracellular domain for hormone binding. In mammals, LGRs steer important developmental, metabolic and reproductive processes as receptors for glycoprotein hormones and insulin/relaxin-related proteins. In insects, a receptor structurally related to human LGRs mediates the activity of the neurohormone bursicon thereby regulating wing
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Various insect species have a severe impact on human welfare and environment and thus force us to continuously develop novel agents for pest control. Neuropeptides constitute a very versatile class of bioactive messenger molecules that... more
Various insect species have a severe impact on human welfare and environment and thus force us to continuously develop novel agents for pest control. Neuropeptides constitute a very versatile class of bioactive messenger molecules that initiate and/or regulate a wide array of vital biological processes in insects by acting on their respective receptors in the plasmamembrane of target cells. These
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The ‘insulin superfamily’ is an ancient category of small, structurally related proteins, such as insulin, insulin-like growth factors (IGF) and relaxin. Insulin-like signaling molecules have also been described in different... more
The ‘insulin superfamily’ is an ancient category of small, structurally related proteins, such as insulin, insulin-like growth factors (IGF) and relaxin. Insulin-like signaling molecules have also been described in different invertebrates, including nematodes, mollusks, and insects. They initiate an evolutionary conserved signal transduction mechanism by binding to a heterotetrameric, membrane-spanning receptor tyrosine kinase. Recent physiological and genetic studies have revealed
Research Interests: Genetics, Physiology, Caenorhabditis elegans, Drosophila melanogaster, Signal Transduction, and 12 moreGrowth Hormone, Humans, Sequence alignment, Insulin, Animals, Insulin signaling, Peptides, Signal Transduction Pathway Models, Amino Acid Sequence, Growth Factor, Cell Size, and Receptor Tyrosine Kinase
Recently, a new serine protease inhibitor family has been described in arthropods. Eight members were purified from locusts and 13 peptides have been identified by cDNA cloning. The peptides share a conserved cysteine array... more
Recently, a new serine protease inhibitor family has been described in arthropods. Eight members were purified from locusts and 13 peptides have been identified by cDNA cloning. The peptides share a conserved cysteine array (Cys-Xaa9–12-Cys-Asn-Xaa-Cys-Xaa-Cys-Xaa2–3-Gly-Xaa3–6-Cys-Thr-Xaa3-Cys) with nine inhibitory domains (PLDs) of the light chain of the crayfish protease inhibitor, pacifastin. A molecular identification of a pacifastin-related precursor (SGPP-5) with three
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Locusts have fascinated researchers for several decades, because they have the remarkable ability to undergo phase transition from the harmless solitary to the swarm-forming gregarious phase. However, the physiological and endocrine... more
Locusts have fascinated researchers for several decades, because they have the remarkable ability to undergo phase transition from the harmless solitary to the swarm-forming gregarious phase. However, the physiological and endocrine mechanisms, underlying phase polymorphism, are only partially unravelled. Nevertheless, besides the ‘classical’ hormones, pacifastin-related peptides have been suggested to play a role in phase transition. Here, we present the