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Investigation of the Pathomechanism of Chronic Cough Using an In Vitro Approach
Clinical &Experimental Allergy, Volume 55, Issue 3, Page 247-249, March 2025.
Umesh Singh, Jonathan A. Bernstein
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Seminars in Cell & Developmental Biology, 1997
Phospholipase D catalyses the hydrolysis of phosphatidylcholine to generate phosphatidate. The regulation of PLD activity is complex involving a number of small GTP binding proteins, but in particular Arf and Rho, phosphatidylinositol 4,5-bisphosphate and protein kinase C.
, Wakelam, , Hodgkin, , Martin, , Saqib
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Phospholipase D catalyses the hydrolysis of phosphatidylcholine to generate phosphatidate. The regulation of PLD activity is complex involving a number of small GTP binding proteins, but in particular Arf and Rho, phosphatidylinositol 4,5-bisphosphate and protein kinase C.
, Wakelam, , Hodgkin, , Martin, , Saqib
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Biochemistry and Cell Biology, 2004
Phospholipase D catalyses the hydrolysis of the phosphodiester bond of glycerophospholipids to generate phosphatidic acid and a free headgroup. Phospholipase D activities have been detected in simple to complex organisms from viruses and bacteria to yeast, plants, and mammals.
Mark, McDermott +2 more
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Phospholipase D catalyses the hydrolysis of the phosphodiester bond of glycerophospholipids to generate phosphatidic acid and a free headgroup. Phospholipase D activities have been detected in simple to complex organisms from viruses and bacteria to yeast, plants, and mammals.
Mark, McDermott +2 more
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The transphosphatidylation activity of phospholipase D
Molecular and Cellular Biochemistry, 1996Transphosphatidylation activity is a characteristic and remarkable property of phospholipase D (PLD) and has been studied in plants and mammalian tissues. This reaction is often used to confirm the properties and/or abnormalities of PLD activity. The mechanism for activating PLD transphosphatidylation seems multiple.
Vincenzo Panagia +5 more
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Kinetics of myocardial phospholipase D
Molecular and Cellular Biochemistry, 1996Myocardial phospholipase D (PLD) is located in different subcellular membranes, including sarcolemma (SL) and sarcoplasmic reticulum (SR). In this study, the kinetics of PLD-dependent hydrolytic and transphosphatidylation activities were examined in SL and SR fractions isolated from rat heart by measuring the formation of phosphatidic acid and ...
Song-Yan Liu +4 more
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Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 1996
Abstract:Phospholipase D is an ubiquitous enzyme that hydrolyzes phosphatidylcholine to phosphatidic acid and choline. Its cellular actions are related to the production of phosphatidic acid and include alterations to cell growth, shape, and secretion.
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Abstract:Phospholipase D is an ubiquitous enzyme that hydrolyzes phosphatidylcholine to phosphatidic acid and choline. Its cellular actions are related to the production of phosphatidic acid and include alterations to cell growth, shape, and secretion.
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Phospholipase D in cellular senescence
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 1999Cellular senescence appears to be an important part of organismal aging. Cellular senescence is characterized by flattened enlarged morphology, inhibition of DNA replication in response to growth factors, inability to phosphorylate the pRb tumor suppressor protein, inability to produce c-fos or AP-1 and overexpression of a variety of genes, notably p21
Lina M. Obeid, Mark E. Venable
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Structure and regulation of phospholipase D
Trends in Pharmacological Sciences, 1996Phosphar:S~:~oline-specific phos>holipase D (PLDs) are phosphodi‘stemses that catalyse the hydrolysis If phosphatidylcholine (PC) to pmjute phosphatidic acid (PA) and :holine. Diverse stimuli mcreasePLD activity in many cells and PA, or a netabolite of this lipid, is probably he orimarv mediator of PLD-initia , ited cell signalltng.
Michael A. Frohman +2 more
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Phospholipase D in Tetrahymena: activity and significance
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 1999Abstract We detected phospholipase D in three species of ciliates: Tetrahymena: T. thermophila, T. pyriformis and T. setosa in nutrient medium supplemented with ethanol in in vivo systems, by the appearance of phosphatidylethanol. The calcium ionophore A23187 increased the synthesis of phosphatidylethanol, as compared with untreated controls.
Rasmussen, M., Rasmussen, L.
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