Academic literature on the topic 'Phospholipase D'
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Journal articles on the topic "Phospholipase D"
McDermott, Mark, Michael J. O. Wakelam, and Andrew J. Morris. "Phospholipase D." Biochemistry and Cell Biology 82, no. 1 (February 1, 2004): 225–53. http://dx.doi.org/10.1139/o03-079.
Full textDhand, Rajiv, Jared Young, Andelle Teng, Subbiah Krishnasamy, and Nicholas J. Gross. "Is dipalmitoylphosphatidylcholine a substrate for convertase?" American Journal of Physiology-Lung Cellular and Molecular Physiology 278, no. 1 (January 1, 2000): L19—L24. http://dx.doi.org/10.1152/ajplung.2000.278.1.l19.
Full textBollag, Wendy B. "Role of phospholipases in adrenal steroidogenesis." Journal of Endocrinology 229, no. 1 (April 2016): R29—R41. http://dx.doi.org/10.1530/joe-16-0007.
Full textEXTON, JOHN H. "Phospholipase D." Annals of the New York Academy of Sciences 905, no. 1 (January 25, 2006): 61–68. http://dx.doi.org/10.1111/j.1749-6632.2000.tb06538.x.
Full textExton, John H. "Phospholipase D." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1436, no. 1-2 (December 1998): 105–15. http://dx.doi.org/10.1016/s0005-2760(98)00124-6.
Full textGomez-Cambronero, Julian, and Paul Keire. "Phospholipase D." Cellular Signalling 10, no. 6 (June 1998): 387–97. http://dx.doi.org/10.1016/s0898-6568(97)00197-6.
Full textWakelam, Michael J. O., Matthew N. Hodgkin, Ashley Martin, and Khalid Saqib. "Phospholipase D." Seminars in Cell & Developmental Biology 8, no. 3 (June 1997): 305–10. http://dx.doi.org/10.1006/scdb.1997.0152.
Full textInamori, K., N. Sagawa, M. Hasegawa, H. Itoh, J. Yano, and T. Mori. "Activation of phospholipase D in cultured human amnion cells." Reproduction, Fertility and Development 7, no. 6 (1995): 1591. http://dx.doi.org/10.1071/rd9951591.
Full textMin, Do Sik. "The Functional Role of Phospholipase D Isozymes in Apoptosis." Journal of Life Science 24, no. 12 (December 30, 2014): 1378–82. http://dx.doi.org/10.5352/jls.2014.24.12.1378.
Full textAlvarez-Breckenridge, Christopher A., Kristin A. Waite, and Charis Eng. "PTEN regulates phospholipase D and phospholipase C." Human Molecular Genetics 16, no. 10 (April 3, 2007): 1157–63. http://dx.doi.org/10.1093/hmg/ddm063.
Full textDissertations / Theses on the topic "Phospholipase D"
Brown, Shea Austin. "N-Acylethanolamines and Plant Phospholipase D." Thesis, University of North Texas, 1998. https://digital.library.unt.edu/ark:/67531/metadc279270/.
Full textHodson, Jane E. "Tobacco Phospholipase D β1: Molecular Cloning and Biochemical Characterization." Thesis, University of North Texas, 2002. https://digital.library.unt.edu/ark:/67531/metadc3341/.
Full textMebarek, Azzam Saida. "La Phospholipase D, une voie de signalisation lipidique impliquée dans de multiples fonctions cellulaires : morphologie, prolifération, différenciation." Lyon, INSA, 2006. http://theses.insa-lyon.fr/publication/2006ISAL0003/these.pdf.
Full textPhospholipase D (PLD) hydrolyses phosphatidylcholine of cell membranes in response to a variety of agonists, to generate phosphatidic acid, a second messenger implicated in cell functions such as cytoskeletal reorganization. In L6 skeletal myoblasts induced to differentiate, a short-lived lowering of ceramide levels was followed by a long-lasting elevation due to de novo synthesis. Ceramide mediates a negative control of myogenic differentiation, at least in part through down-regulation of PLD1 isoform expression and inhibition of PLD1-dependent formation of stress fibers. Moreover, we show that PLD is involved in paracellular permeability of endothelial cells through actin cytoskeleton reorganization, and morphological changes. In addition, we show that disruption of membrane lipid rafts by agents specifically active on the lipids of this compartment, induces an activation of PLD and generates anti-proliferative signals in lymphocytes
Rahier-Corticchiato, Renaud. "Caractérisation biochimique des phospholipases D et de leurs domaines fonctionnels : nouvelle méthode de mesure de l’activité phospholipase D." Thesis, Lyon, 2016. http://www.theses.fr/2016LYSE1292/document.
Full textPhospholipase D (PLD) hydrolyses membrane phospholipids, leading to the formation of free polar headgroup and phosphatidic acid releasing, involved in cell signaling. To understand the biochemical properties of PLDs, this work has been made around two axes. The one first concerns the recombinant expression and purification of the PLDa of Arabidopsis thaliana (AtPLDa) in the yeast Pichia pastoris. The N-terminal sequence of the recombinant AtPLDa has been determined and found to lack its first 35 amino acids, suggesting the involvement of a maturing mechanism. However, plant PLDs exhibit a C2-lipid binding domain at their N-terminal region, which is involved in their Ca2+-dependent membrane targeting. Thus, to assess the impact of such a cleavage, whole and mature-like C2 domains of AtPLDa, as well as of AtPLDß, for the sake of comparison were studied. Thus, the characterization of their affinity for phospholipids, combined with their three-dimensional modeling have demonstrated that the differences observed in their regulation by Ca2+, observed between whole and mature-like forms, originated from the presence of a N-terminus amphipathic a helix, removed during the maturation process. The second axis concerns the development of a novel PLD assay that measure PA in a direct, specific and continuous manner, using the chelation enhanced fluorescence property of 8-hydroxyquinoline in the presence of Ca2+. Thus, this assay appears suitable for monitoring both the inhibition of PLDs as well as their substrate specificity, using natural phospholipids with different polar headgroups, and at a microplate scale
Li, Liang. "Regulation of phospholipase D in submandibular glands." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape4/PQDD_0018/NQ53062.pdf.
Full textLee, Jung Hoon. "Suppression of phospholipase D[Alpha] in soybean." Diss., Manhattan, Kan. : Kansas State University, 2008. http://hdl.handle.net/2097/828.
Full textMcKinnon, Murray. "Studies on mammalian phosphatidylcholine specific phospholipase D." Thesis, Open University, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315440.
Full textSkafi, Najwa. "Role of Phospholipase D in Vascular Calcification." Thesis, Lyon, 2017. http://www.theses.fr/2017LYSE1339/document.
Full textVascular calcification is the accumulation of calcium phosphate crystals in blood vessels via a pathological process that resembles physiological bone or cartilage formation. Calcification in the medial layer is mainly seen in diabetic and chronic kidney disease patients. Its main consequence is the loss of elasticity which is indispensable for the function of large arteries. Accordingly, vascular medial calcification was significantly associated with mortality in hemodialysis patients. Vascular calcification treatments are limited to those that correct its causative health problems, but no efficient, specific and targeted interventions are available. Therefore, a deep understanding of its molecular mechanisms is needed to find novel therapeutic targets. Phospholipase D catalyses the hydrolysis of phospholipids into phosphatidic acid and a head group. It is implicated in different cellular functions and diseases. It was found to be activated by factors involved in osteogenesis and others involved in vascular calcification. Thus, we investigated its role in vascular calcification in 3 models: an in-vitro model of murine smooth muscle cell line MOVAS cultured with ascorbic acid and β-glycerophosphate, an ex-vivo model of rat aortas cultured in high phosphate medium, and an in-vivo model of adenine-induced kidney disease in rats in which vascular calcification is induced by further administration of high phosphorus/calcium diet and active vitamin D injections. Calcification was detected in these models using different approaches including alkaline phosphatase activity, calcium dosage, and/or evaluation of osteo-chondrocytic markers expression. Pld1 expression was seen upregulated in all the three models, especially during early stages of calcification, and was accompanied with increased phospholipase D activity in the in-vitro and ex-vivo model. The inhibition of total phospholipase D activity in these two models, or that of phospholipase D1 in case of MOVAS model, abolished calcification. Phospholipase D2-specific inhibition did not induce significant effects. Two pathways by which phospholipase D can be activated were tested, protein kinase C and sphingosine 1-phosphate pathways, but they were found to be involved in calcification but not necessary for phospholipase D activation during this process. Alternatively, the preliminary results showed that PLD may be acting by activation of sphingosine kinase 2 whose activity was found necessary for calcification in the MOVAS model. Further investigations are needed to understand the mechanisms by which phospholipase D is activated and by which it is acting. Phospholipase D could be a novel target for vascular calcification especially that its inhibition in patients did not induce adverse health effects
Arhab, Yani. "Caractérisation structurale et fonctionnelle des phospholipases D." Thesis, Lyon, 2018. http://www.theses.fr/2018LYSE1225/document.
Full textPhospholipases D (PLD, EC 3.1.4.4) are ubiquitary enzymes found in prokaryotes (bacteria) as well as in eukaryotes (plant, animals and fungi). PLD catalyzes the hydrolysis of the distal phosphoester bound of phospholipids thus forming phosphatidic acid, an important cell signaling messenger implicated in numerous pathways such as cell proliferation, vesicular formation and trafficking but also transcription and cell survival. PLDs belong to a superfamily of protein which share a common catalytic site called “HKD†for HXKX4D, X is a random amino acid, containing H (Histidyl), K (lysyl) and D (aspartyl) residues. This consensus sequence is duplicated in most of the PLD superfamily members. The study of plant PLD is the best way to understand this family of proteins as they are the sole eukaryotic PLDs to be purified to homogeneity so far. This work provides a functional characterization of the most conserved residues in plant PLDs leading to a structural characterization with the crystallization of this enzyme. A second part of this work proposes the modulation of the enzyme hydrolysis activity by studying the minimal domain necessary for the activity and post-translational maturation undergone by plant PLDs. Also, we look for a new specific inhibitory molecule. Finally, we propose the cloning of a new plant PLD and the development of a new way to detect in vivo PLD activity
Heung, Yen Ming Mary. "Molecular selectivity of phospholipase D in granulocyte function." Thesis, University of Southampton, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.241935.
Full textBooks on the topic "Phospholipase D"
Clark, Joanna Mary. The regulation of human phospholipase D: Studies with recombinant phospholipase D1b and myeloid leukaemic cell lines. Birmingham: University of Birmingham, 1999.
Find full textBrown, Fraser David. The role and regulation of phospholipase D in haematopoietic cells. Birmingham: University of Birmingham, 1998.
Find full textBook chapters on the topic "Phospholipase D"
Exton, John H. "Phospholipase D." In Frontiers in Bioactive Lipids, 265–77. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4615-5875-0_35.
Full textGomez-Cambronero, Julian, and Karen M. Henkels. "Phospholipase D." In Encyclopedia of Signaling Molecules, 3999–4010. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_15.
Full textFoster, David A., and Deepak Menon. "Phospholipase D." In Encyclopedia of Cancer, 1–6. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27841-9_4540-2.
Full textLackner, K. J., and D. Peetz. "Phospholipase D." In Lexikon der Medizinischen Laboratoriumsdiagnostik, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2018. http://dx.doi.org/10.1007/978-3-662-49054-9_2426-1.
Full textExton, John H. "Phospholipase D." In Lipases and Phospholipases in Drug Development, 55–78. Weinheim, FRG: Wiley-VCH Verlag GmbH & Co. KGaA, 2005. http://dx.doi.org/10.1002/3527601910.ch4.
Full textLackner, K. J., and D. Peetz. "Phospholipase D." In Springer Reference Medizin, 1880. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_2426.
Full textDonato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "Phospholipase D." In Encyclopedia of Signaling Molecules, 1409–19. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_15.
Full textFoster, David A., and Deepak Menon. "Phospholipase D." In Encyclopedia of Cancer, 3544–49. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-46875-3_4540.
Full textSchomburg, Dietmar, and Margit Salzmann. "Phospholipase D." In Enzyme Handbook 3, 549–53. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76463-9_116.
Full textZhang, Wenhua, Xiaobo Wan, Yueyun Hong, Weiqi Li, and Xuemin Wang. "Plant Phospholipase D." In Lipid Signaling in Plants, 39–62. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-03873-0_3.
Full textConference papers on the topic "Phospholipase D"
Zhou, Mingjie, Cailan Zhang, and Richard P. Haugland. "Choline oxidase: a useful tool for high-throughput assays of acetylcholinesterase, phospholipase D, phosphatidylcholine-specific phospholipase C, and sphingomyelinase." In BiOS 2000 The International Symposium on Biomedical Optics, edited by Patrick A. Limbach, John C. Owicki, Ramesh Raghavachari, and Weihong Tan. SPIE, 2000. http://dx.doi.org/10.1117/12.380507.
Full textZhang, Z., and X. Chen. "BS3.2 - Polydiacetylene-based sensors for the activity assay of phospholipase D." In 17th International Meeting on Chemical Sensors - IMCS 2018. AMA Service GmbH, Von-Münchhausen-Str. 49, 31515 Wunstorf, Germany, 2018. http://dx.doi.org/10.5162/imcs2018/bs3.2.
Full textMao, Xiangzhao. "Efficient Expression of Phospholipase D and Its Application in Enzymatic Modification of Phospholipids." In Virtual 2021 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2021. http://dx.doi.org/10.21748/am21.207.
Full textLapetina, Eduardo G. "THE ROLE OF INOSITIDES, PHOSPHOLIPASE C AND G-PROTEINS IN RECEPTOR TRANSDUCTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644775.
Full textKrishnamachary, Balaji, Mayur Gadiya, Noriko Mori, Yelena Mironchik, Kristine Glunde, and Zaver M. Bhujwalla. "Abstract 46: Interdependence of choline kinase and phospholipase D in human breast cancer cells." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-46.
Full textWan, Sibao, Mengyun Li, Fangwei Ma, Jie Yuan, Zhanmin Liu, Weiwei Zheng, and Jicheng Zhan. "Genome-wide identification of phospholipase D (PLD) gene family and their responses to low-temperature stress in peach." In INTERNATIONAL SYMPOSIUM ON THE FRONTIERS OF BIOTECHNOLOGY AND BIOENGINEERING (FBB 2019). AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5110805.
Full textItagaki, Y., A. Suzuki, and K. Higashio. "TISSUE PLASMINOGEN ACTIVATOR (T-PA) PRODUCTION BY HUMAN EMBRYONIC FIBROBLASTS, IMR-90, STIMULATED BY PROTEOSE PEPTONE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644392.
Full textCuller, Mitchell, Eric Decker, and Ipek Bayram. "Enzymatic modification of lecithin for improved antioxidant activity in combination with tocopherol in emulsions and bulk oil." In 2022 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2022. http://dx.doi.org/10.21748/dsey3101.
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