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Human Eosinophil Lysophospholipase (Charcot-Leyden Crystal Protein): Molecular Cloning, Expression, and Potential Functions in Asthma
Published in Gerald J. Gleich, A. Barry Kay, Eosinophils in Allergy and Inflammation, 2019
Steven J. Ackerman, Zeqi Zhou, Daniel G. Tenen, Mike A. Clark, Yuan-Po Tu, Charles G. Irvin
Although it has been suggested that lysophospholipases may catabolize potentially toxic and membrane-perturbatory lysophosphatides, studies of erythrocyte membrane lysophospholipase have shown that it promotes complement-mediated erythrocyte lysis, potentially by altering the stoichiometric balance of phospholipid and free fatty acid (30). These observations suggest a role for lysophospholipases such as CLC protein in altering membrane fluidity and/or integrity and a potential need for intracellular regulation of the enzyme activity of this protein in eosinophils (and basophils). By altering the balance between phospholipids and free fatty acids in membranes, CLC protein might act synergistically to enhance the cytotoxicity or helminthotoxicity of eosinophil granule cationic proteins, such as MBP, ECP, or EPO, which have been shown to alter membrane structure (42). At noncytolytic concentrations, lysophospholipids also possess multiple pro- and anti-inflammatory properties, including potentiation of mast cell histamine release, stimulation or inhibition of membrane-bound enzymes such as adenylate and guanylate cyclases, inhibition of prostaglandin synthesis and platelet aggregation, modification of membrane fluidity, and potentiation of humoral and cellmediated immune responses (reviewed in 43, 44) and thus could act as modulators of inflammation. Catabolism by CLC protein of lysophosphatides generated at sites of eosinophil-, basophil-, or mast-cell-mediated inflammation could be a physiologically significant activity of this lysophospholipase.
Lipids of Dermatophytes
Published in Rajendra Prasad, Mahmoud A. Ghannoum, Lipids of Pathogenic Fungi, 2017
Removal of the cytotoxic lysophospholipids produced by the action of intracellular or extracellular phospholipase A could be one of the major functions of lysophospholipase. Lysophospholipase activity in E. floccosum was found to be present in both mitochondrial as well as the microsomal fraction.79 It was stimulated by Ca2+, ethanol and non-ionic detergents but was inhibited by EDTA, Fe2+ and Hg2+. Among various -SH group reagents, only sodium fluoride was inhibitory to E. floccosum enzyme while others were mild activators.35
Enzymes
Published in Stephen W. Carmichael, Susan L. Stoddard, The Adrenal Medulla 1986 - 1988, 2017
Stephen W. Carmichael, Susan L. Stoddard
Husebye and Flatmark (1987) characterized phospholipase activities of chromaffin vesicle membranes isolated from the bovine adrenal medulla. The vesicles contain a phospholipase activity. The preparations also revealed a phospholipase Aj activity. The membranes also contain a lysophospholipase activity that accounts for the major part of the deacylation of membrane phospholipids.
Elevated lysophosphatidic acid levels in the serum and cerebrospinal fluid in patients with multiple sclerosis: therapeutic response and clinical implication
Published in Neurological Research, 2018
Dongxiao Jiang, Weiping Ju, Xijun Wu, Xia Zhan
Lysophospholipase D is important for serum LPA synthesis. Autotaxin is a secreted lysophospholipase D that increases hydrolysis of lysophosphatidylcholine to produce LPA. Autotaxin has been found to be elevated in the serum and CSF of MS patients. In an animal model of MS, autotoxin (also known as phosphodiesterase 1α) was only decreased at the onset of clinical symptom before the occurrence of demyelination. These findings suggest that autotoxin expression may be only elevated during relapse of MS, but may not be during disease remission. Since we found that the LPA levels in the serum and CSF were significantly higher in MS patients in relapse than in MS patients in remission, it is possible that elevated autotoxin may contribute to the increased levels of LPA in the serum and CSF.
Balamuthia mandrillaris: pathogenesis, diagnosis, and treatment
Published in Expert Opinion on Orphan Drugs, 2020
Mohammad Ridwane Mungroo, Naveed Ahmed Khan, Ruqaiyyah Siddiqui
It was reported that, when supplemented with calcium ions, B. mandrillaris has enzymatic activity against monoacylglycerol, diacylphosphatidylglycerol, and diacylphosphatidylcholine [12]. It was also observed that fatty acids were released from diacylglycerolipids and triacylglycerolipids due to lipase activities and that B. mandrillaris produced lysophospholipase A that is responsible for the hydrolysis of monoacylglycerophospholipids [12].