Cloning and Functional Expression of the First Drosophila melanogaster Sulfakinin Receptor DSK-R1

Kubiak, Teresa M.; Larsen, Martha J.; Burton, Katherine J.; Bannow, Carol A.; Martin, Robin; Zantello, Marjorie R.; Lowery, David E.

doi:10.1006/bbrc.2002.6459

Cited by 111 publications

(99 citation statements)

References 24 publications

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“…The mutant Chinese hamster ovary cell line CHO-10001A (referred to hereafter as CHO cells), cell culture media, transfection, and various assay reagents were as previously described. 11,12,17,18 U-73122 (phospholipase C inhibitor) and its inactive analog U-73343 were obtained from the Upjohn/Pharmacia/Pfizer compound collection. 19 Cloning and Plasmid Preparation Molecular biological techniques followed either manufacturer's recommendations or general protocols.…”

Section: Methodsmentioning

confidence: 99%

“…23 Cell Cultures, Transfection, Stable Cell Line Generation and Membrane Preparation CHO cells were cultured and transfected as described earlier. 11,12,17,18 The flp-18R1a/pCR3.1 or flp-18R1b /pCR3.1 plasmids (5 lg DNA/10 cm plate) were used for transfections. The cells were harvested 24 h after transfection and membranes were prepared as described.…”

Section: Phylogenetic Analysismentioning

confidence: 99%

“…Assays were run using a 96-well fluorescence imaging plate reader (FLIPR) (Molecular Devices, Sunnyvale, CA) essentially as described earlier 12,18 either with clonal cell lines or cells transiently transfected with the flp-18R1a/pCR3.1 or flp-18R1b/pCR3.1 plasmids and plated at 2 3 10 4 cells/well 24 h after transfection. In experiments incorporating a 37 to 288C temperature shift, cells plated in blackwalled 96-well plates were first incubated at 378C for 24 h and then at 288C for 16-24 h before testing in complete media supplemented with 10 mM HEPES.…”

Section: Calcium Mobilization Assaymentioning

confidence: 99%

“…Cell loading was with 4 lM FLUO3 (Molecular Devices) in the presence of 2.5 mM probenecid. 12,18 In experiments with U-73122 (phospholipase C inhibitor), or its inactive analog U-73343, these compounds were added 10 min before peptide challenge (at a final concentration of 10 lM) in 10 mM HBSS/10 mM HEPES/2.5 mM probenecid containing 0.1% DMSO. In yet another experiment, plated cells were incubated with pertussis toxin (PTX, 100 ng/ml) overnight before peptide challenge.…”

Section: Calcium Mobilization Assaymentioning

confidence: 99%

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FMRFamide‐like peptides encoded on the flp‐18 precursor gene activate two isoforms of the orphan Caenorhabditis elegans G‐protein‐coupled receptor Y58G8A.4 heterologously expressed in mammalian cells

Kubiak¹,

Larsen²,

Bowman³

et al. 2008

Biopolymers

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Section: Methodsmentioning

confidence: 99%

Section: Phylogenetic Analysismentioning

confidence: 99%

Section: Calcium Mobilization Assaymentioning

confidence: 99%

Section: Calcium Mobilization Assaymentioning

confidence: 99%

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FMRFamide‐like peptides encoded on the flp‐18 precursor gene activate two isoforms of the orphan Caenorhabditis elegans G‐protein‐coupled receptor Y58G8A.4 heterologously expressed in mammalian cells

Kubiak¹,

Larsen²,

Bowman³

et al. 2008

Biopolymers

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“…Strikingly, replacement of the sulfated tyrosine residue by a standard tyrosine in the ligand resulted in a 3000 fold decrease in the activity of the receptor. 98) These findings underscore the importance of highly precise lockand-key mechanisms in FaRPs mode of action, which probably warrants a review of the classification of these peptides based solely on sequence.…”

Section: Fmrfamides and Fmrfamide-related Peptides (Farps)mentioning

confidence: 88%

Molecular physiology of crustacean and insect neuropeptides

Mercier¹,

Doucet

Retnakaran³

2007

J. Pestic. Sci.

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One of the principal hallmarks of a living organism is its ability to respond to stimuli. As the unicellular organisms evolved into multicellular metazoans, the external signals perceived had to be transduced to several other cells requiring a neuronal network with its accompanying biochemical neurotransmitters. The progressive increase in complexity of the organisms necessitated the need for an integrated signal transducing system collecting external sensory stimuli and sending them to effector systems such that a dynamic equilibrium or homeostasis, which is essential for survival, could be maintained. During the course of evolution many advanced sense organs were developed to detect various parameters in the environment, and concomitantly different internal effector systems were formed to respond to these signals received from outside to maintain homeostasis. Coordination was achieved with a network of electrical conductors in the form of an arborized nervous system and a variety of hydrophilic biochemicals that acted as neurotransmitters carrying the sensory signals to the internal effector systems. As the animal became increasingly complex, a sophisticated neurotransmission system catering to the spatial and temporal needs during growth, development and reproduction had to be in place. Parts of the nervous tissue in many locations took on a secretory role and released protein signal transducers, the neuropeptides. A panoply of such neuropeptides exist in all organisms functioning as neurohormones, neurotransmitters or neuromodulators. Aspects of neuropeptide structure and function in insects and crustaceans have been reviewed by various authors. [1][2][3][4][5][6][7][8][9][10] The neuropeptides are ligands to their cognate receptors in the ef- Organisms have to constantly respond to environmental conditions to maintain a status of dynamic homeostasis for survival. As single celled organisms evolved into multicellular animals, intercellular and inter-organ communications became indispensable not only to orchestrate homeostasis but also to control the many events punctuating metazoan development. To accomplish this need, a signal transduction system was evolved, consisting of an arborized network of nerves as well as a collection of oligopeptide neurotransmitters (neuropeptides) along with their cognate receptors. We review here the current state of our understanding of the physiology of neuropeptides in the most species-rich group of animals, the crustaceans and insects. The vast majority of neuropeptides signal through cell-surface guanosine-protein coupled receptors (GPCRs). These neuropeptide-receptor systems control a variety of physiological functions, for instance the numerous involuntary movements of internal ducts that are precisely timed for transporting reproductive, digestive and secretory materials. The rigid exoskeleton in Crustaceans and Insects require periodic molts to accomplish growth and metamorphosis and this is harmoniously regulated by a cascade of neuropeptides. Neuropeptides also regul...

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Insect Peptide Hormones

Isaac

Audsley

2009

Amino Acids, Peptides and Proteins in Organic Chemistry

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Cloning and Functional Expression of the First Drosophila melanogaster Sulfakinin Receptor DSK-R1

Cited by 111 publications

References 24 publications

FMRFamide‐like peptides encoded on the flp‐18 precursor gene activate two isoforms of the orphan Caenorhabditis elegans G‐protein‐coupled receptor Y58G8A.4 heterologously expressed in mammalian cells

FMRFamide‐like peptides encoded on the flp‐18 precursor gene activate two isoforms of the orphan Caenorhabditis elegans G‐protein‐coupled receptor Y58G8A.4 heterologously expressed in mammalian cells

Molecular physiology of crustacean and insect neuropeptides

Insect Peptide Hormones

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