Pip Research Papers - Academia.edu (original) (raw)

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- Computer Science, Human Computer Interaction, Educational Technology, Computer Science Education
- by Dan Stewart
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- Pediatrics, Pregnancy, Humans, Placenta
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- Organic Chemistry, Solar Cell, Fullerenes, NHS
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- by francesco Vizza
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- by Wendy Boss
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- by Eduardo M Cilli and +1
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- by Robert T.c Brownlee
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- Chemistry, Inorganic Chemistry, Coordination Chemistry, Nuclear Magnetic Resonance
- by francesco Vizza
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- Inorganic Chemistry, Medicinal Chemistry, Coordination Chemistry, PET
- by Wolfram Windisch and +1
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- Respiratory Medicine, Reference, Millimeter Waves, Masks
- by Jasper Dingemanse
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- Pediatrics, Modeling and Simulation, Pharmaceutics, Pip
- by August Stich
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- Organic Chemistry, Animals, Drug Resistance, NIP

D type phospholipases (PLD) are enzymes that hydrolyze the head group of phospholipids to produce phosphatidic acid. This activity is ubiquitous in plant tissues, and has been isolated and characterized from different species and organs. Several families of these proteins have been described in plants on the basis of their gene sequences (PLD α, β, γ, δ, ζ and ε). They have been shown to be involved in many metabolic events, such as response to abiotic stress, signal transduction, and membrane lipid turnover and degradation. In the present study, PLD activity was measured in the soluble fractions isolated from different organs of this plant. A PLD of α type was cloned from leaf cDNA that was responsible for most of this activity. The gene encoding this 810 aa protein was heterologously expressed in E. coli. This protein was not lethal for the eukaryotic host, although it altered its phospholipid profile. PLDα was purified to almost homogeneity by His-tag affinity chromatography, displaying an optimum pH of 6.5 and strong dependence on the presence of Ca2+ and SDS in the assay medium. The enzyme was active towards phosphatidylcholine, Phosphatidylethanolamine and phosphatidylglycerol. Furthermore, the HaPLDα gene was found to be expressed at high levels in leaf and stem tissues.

- by Rafael Garces
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- Plant Biology, Abiotic Stress, Gene expression, Signal Transduction
- by francesco Vizza
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- Inorganic Chemistry, Medicinal Chemistry, Coordination Chemistry, PET
- by Luigi Giannini
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- Italy, Humans, Female, Resuscitation
- by Clovis Nakaie
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- Organic Chemistry, AI, Bioorganic Chemistry, HPLC
- by Valeria Nicolini
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- Genetic Engineering, Humans, VEGF, Animals
- by Angel Gonzalez and +2
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- Organic Chemistry, Molecular Dynamics, Computer Simulation, Computer Model
- by Jorge Bravo
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- Chemistry, Inorganic Chemistry, Medicinal Chemistry, Coordination Chemistry
- by Balazs Sarkadi
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- Chemical Engineering, Calcium, Biological Sciences, Thrombin
- by Abul Kalam Azad
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- Chemical Engineering, Water, Kinetics, Macromolecular X-Ray Crystallography
- by Theresa Filtz
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- Fluorescence, Cell line, In Vitro, PLC
- by Adrie Verhoeven
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- Thrombin, Humans, Platelet aggregation, Collagen
- by Aldo Bancalari and +2
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- Humans, Female, Male, The
- by Christophe Rouillon
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- Molecular Biology, DNA replication, Molecular, Mutation
- by Seyed Hasnain
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- Cell Signaling, Lipids, Lipid Membranes, Ac
- by Marin Van Heel
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- Thermodynamics, Molecular Biology, EM, Macromolecular X-Ray Crystallography
- by Vassiliki Magafa
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- Organic Chemistry, Oxytocin, In Vitro, Humans
- by Ovidio Bussolati and +2
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- Kinetics, Molecular, Humans, Endothelial Cells

Ca2+ dependent polyphosphoinositide phospholipase C (PLC) activity in cardiac sarcolemma hydrolyzed both endogenous and exogenous phosphatidylinositol 4-phosphate (PIP) and phosphatidylinositol 4,5-bisphosphate (PIP2) with an associated increase in inositol bisphosphate (IP2). Dialyzed cytosol and certain fractions of cytosol isolated by anion exchange or gel filtration chromatography activated sarcolemmal PLC activity by approx. 100%. The PLC activator eluted with an apparent molecular weight of 160 Kdal on a Sephacryl 300 column and was destroyed by heat or trypsin treatment. Exogenous 3H-PIP2 was not hydrolyzed by cytosolic fractions containing sarcolemmal PLC activator. These studies demonstrate that the polyphosphoinositide PLC in cardiac sarcolemma is regulated by a cytosolic protein.

- by Jennifer Sampson
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- Kinetics, Calcium, IP, PLC
- by Lucio van Rooijen
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- Chemistry, Epilepsy, Medicine, High Voltage
- by Paolo Biban
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- Pediatrics, Biology, Medicine, Prospective studies
- by Haim Breitbart
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- Biological Sciences, Female, Animals, Male
- by Y. Hanba
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- Water, Photosynthesis, Plant Biology, Ecology
- by adrie verhoeven
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- Metabolism, Medical Microbiology, Biological Sciences, Platelet
- by Christian Roy
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- Humans, Glutathione, Liposomes, Pi
- by Charlotte Beurskens
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- Electron Microscopy, Cytokines, Inflammation, SEM
- by Giulio Ruffini
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- Physics, GPS, GNSS, Paris
- by Amelia Cataldi
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- Signal Transduction, Cellular Signalling, PLC, Prolactin
- by Susana Boso
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- Biology, Cultivar, Clones, Pip
- by Yoshizumi Ishino
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- Molecular Biology, DNA damage, Molecular, Phylogeny