PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21908590-0 2011 An albumin-associated PLA2-like activity inactivates surfactant phosphatidylcholine secreted from fetal type II pneumocytes. Phosphatidylcholines 64-83 phospholipase A2 group IIA Homo sapiens 22-26 22173044-5 2012 RESULTS: BAL sPLA2 enzyme activity was markedly elevated in ARDS samples relative to healthy subjects when measured by ex vivo hydrolysis of both phosphatidylglycerol (PG) and phosphatidylcholine (PC). Phosphatidylcholines 176-195 phospholipase A2 group IIA Homo sapiens 13-18 22173044-5 2012 RESULTS: BAL sPLA2 enzyme activity was markedly elevated in ARDS samples relative to healthy subjects when measured by ex vivo hydrolysis of both phosphatidylglycerol (PG) and phosphatidylcholine (PC). Phosphatidylcholines 197-199 phospholipase A2 group IIA Homo sapiens 13-18 22494626-2 2012 Among sPLA(2)s, the human group X (hGX)-sPLA(2) has the highest catalytic activity towards phosphatidylcholine (PC), the major phospholipid of cell membranes and blood lipoproteins. Phosphatidylcholines 91-110 phospholipase A2 group IIA Homo sapiens 6-13 22494626-2 2012 Among sPLA(2)s, the human group X (hGX)-sPLA(2) has the highest catalytic activity towards phosphatidylcholine (PC), the major phospholipid of cell membranes and blood lipoproteins. Phosphatidylcholines 112-114 phospholipase A2 group IIA Homo sapiens 6-13 23604781-6 2013 The data presented here show that: (1) group X secretory PLA2 (sPLA2) is about threefold more active than group V sPLA2 in releasing sn-2 fatty acids from DHA regioisomers, and (2) EL shows its specificity for DHA PtdCho species in a concentration independent manner, suggesting that the enzyme could play a major role in generating free sn-1-DHA or/and sn-2-DHA lysoPtdCho from the regioisomers in the BBB. Phosphatidylcholines 214-220 phospholipase A2 group IIA Homo sapiens 63-68 16461407-5 2006 By using phosphatidylcholine/phosphatidylglycerol model systems, we show that local enrichment of anionic lipids into fluid domains triggers PLA2-IIA activity. Phosphatidylcholines 9-28 phospholipase A2 group IIA Homo sapiens 141-145 24061892-1 2010 Secreted group X phospholipase A2 (sPLA2-X) is one of the most effective mammalian PLA2 enzymes at hydrolyzing plasma lipoproteins and phospholipids in the membranes of intact cells, due in particular to its relatively high binding affinity to zwitterionic phospholipid substrates, such as phosphatidylcholine. Phosphatidylcholines 290-309 phospholipase A2 group IIA Homo sapiens 36-40 20153800-8 2010 Among secreted PLA2s (sPLA2), the group X sPLA2 (PLA2GX), due to its very high activity towards phosphatidylcholine the main phospholipid of LDL, became an attractive target in atherosclerosis. Phosphatidylcholines 96-115 phospholipase A2 group IIA Homo sapiens 15-20 20153800-8 2010 Among secreted PLA2s (sPLA2), the group X sPLA2 (PLA2GX), due to its very high activity towards phosphatidylcholine the main phospholipid of LDL, became an attractive target in atherosclerosis. Phosphatidylcholines 96-115 phospholipase A2 group IIA Homo sapiens 22-27 20153800-8 2010 Among secreted PLA2s (sPLA2), the group X sPLA2 (PLA2GX), due to its very high activity towards phosphatidylcholine the main phospholipid of LDL, became an attractive target in atherosclerosis. Phosphatidylcholines 96-115 phospholipase A2 group IIA Homo sapiens 42-47 20044023-0 2010 Oxidized phosphatidylcholine stimulates activity of secretory phospholipase A2 group IIA and abolishes sphingomyelin-induced inhibition of the enzyme. Phosphatidylcholines 9-28 phospholipase A2 group IIA Homo sapiens 85-88 17980167-2 2007 Of 10 mammalian secreted phospholipase A(2) (sPLA(2)) enzymes identified to date, group V and X sPLA(2)s, which are two potent plasma membrane-acting sPLA(2)s, are capable of preventing host cells from being infected with adenovirus, and this anti-viral action depends on the conversion of phosphatidylcholine (PC) to lysophosphatidylcholine (LPC) in the host cell membrane. Phosphatidylcholines 290-309 phospholipase A2 group IIA Homo sapiens 16-43 17980167-2 2007 Of 10 mammalian secreted phospholipase A(2) (sPLA(2)) enzymes identified to date, group V and X sPLA(2)s, which are two potent plasma membrane-acting sPLA(2)s, are capable of preventing host cells from being infected with adenovirus, and this anti-viral action depends on the conversion of phosphatidylcholine (PC) to lysophosphatidylcholine (LPC) in the host cell membrane. Phosphatidylcholines 290-309 phospholipase A2 group IIA Homo sapiens 45-52 17980167-2 2007 Of 10 mammalian secreted phospholipase A(2) (sPLA(2)) enzymes identified to date, group V and X sPLA(2)s, which are two potent plasma membrane-acting sPLA(2)s, are capable of preventing host cells from being infected with adenovirus, and this anti-viral action depends on the conversion of phosphatidylcholine (PC) to lysophosphatidylcholine (LPC) in the host cell membrane. Phosphatidylcholines 311-313 phospholipase A2 group IIA Homo sapiens 16-43 17980167-2 2007 Of 10 mammalian secreted phospholipase A(2) (sPLA(2)) enzymes identified to date, group V and X sPLA(2)s, which are two potent plasma membrane-acting sPLA(2)s, are capable of preventing host cells from being infected with adenovirus, and this anti-viral action depends on the conversion of phosphatidylcholine (PC) to lysophosphatidylcholine (LPC) in the host cell membrane. Phosphatidylcholines 311-313 phospholipase A2 group IIA Homo sapiens 45-52 17197234-3 2007 In contrast to PtdCho, which was readily hydrolyzed by group V and X sPLA(2)s, and to a lesser extent by group IIA sPLA(2), the minor ethanolamine, inositol and serine glycerophospholipids exhibited marked resistance to hydrolysis by all three sPLA(2)s. Phosphatidylcholines 15-21 phospholipase A2 group IIA Homo sapiens 69-75 19712054-5 2009 The ratios of the lyso derivatives of phosphatidyl choline, ethanolamine and serine obtained here together with the known distribution of these phospholipids among cell membranes, suggest that most PLA(2) hydrolysis takes place on the cell surface. Phosphatidylcholines 38-58 phospholipase A2 group IIA Homo sapiens 198-204 17321580-3 2007 Phosphatidylcholine, the principal component of pulmonary surfactant that maintains small airway patency, is hydrolyzed by sPLA(2). Phosphatidylcholines 0-19 phospholipase A2 group IIA Homo sapiens 123-130 17321580-11 2007 The combined actions of sPLA(2) and lysophospholipase produced dose-dependent and time-dependent losses of surfactant function, concomitant with hydrolysis of phosphatidylcholine and lysophosphatidylcholine. Phosphatidylcholines 159-178 phospholipase A2 group IIA Homo sapiens 24-53 12111845-5 2002 Treatment of (3)H-AA-labeled cortical neurons with mildly toxic concentrations of sPLA(2) (25 ng/ml, 1.78 nM) for 45 min resulted in a two- to threefold higher loss of (3)H-AA from phosphatidylcholine (PC) than from phosphatidylethanolamine (PE) and in minor changes in other phospholipids. Phosphatidylcholines 181-200 phospholipase A2 group IIA Homo sapiens 82-89 12111845-5 2002 Treatment of (3)H-AA-labeled cortical neurons with mildly toxic concentrations of sPLA(2) (25 ng/ml, 1.78 nM) for 45 min resulted in a two- to threefold higher loss of (3)H-AA from phosphatidylcholine (PC) than from phosphatidylethanolamine (PE) and in minor changes in other phospholipids. Phosphatidylcholines 202-204 phospholipase A2 group IIA Homo sapiens 82-89 7772034-4 1995 The presence of certain membrane-bound anions can enhance hydrolysis of PC by the mammalian secreted PLA2S. Phosphatidylcholines 72-74 phospholipase A2 group IIA Homo sapiens 101-106 10207008-2 1999 We have demonstrated that human group V PLA2 (hsPLA2-V) can bind phosphatidylcholine (PC) membranes and hydrolyze PC substrates much more efficiently than human group IIa PLA2, which makes it better suited for acting on the outer plasma membrane (Han, S.-K., Yoon, E. T., and Cho, W. (1998) Biochem. Phosphatidylcholines 65-84 phospholipase A2 group IIA Homo sapiens 40-44 10207008-2 1999 We have demonstrated that human group V PLA2 (hsPLA2-V) can bind phosphatidylcholine (PC) membranes and hydrolyze PC substrates much more efficiently than human group IIa PLA2, which makes it better suited for acting on the outer plasma membrane (Han, S.-K., Yoon, E. T., and Cho, W. (1998) Biochem. Phosphatidylcholines 65-84 phospholipase A2 group IIA Homo sapiens 48-52 10207008-2 1999 We have demonstrated that human group V PLA2 (hsPLA2-V) can bind phosphatidylcholine (PC) membranes and hydrolyze PC substrates much more efficiently than human group IIa PLA2, which makes it better suited for acting on the outer plasma membrane (Han, S.-K., Yoon, E. T., and Cho, W. (1998) Biochem. Phosphatidylcholines 86-88 phospholipase A2 group IIA Homo sapiens 40-44 10207008-2 1999 We have demonstrated that human group V PLA2 (hsPLA2-V) can bind phosphatidylcholine (PC) membranes and hydrolyze PC substrates much more efficiently than human group IIa PLA2, which makes it better suited for acting on the outer plasma membrane (Han, S.-K., Yoon, E. T., and Cho, W. (1998) Biochem. Phosphatidylcholines 86-88 phospholipase A2 group IIA Homo sapiens 48-52 9507109-1 1998 Phosphatidyl-choline (PC) vesicles and normal cell membranes are resistant to hydrolysis by human group II secreted PLA2, an enzyme that can attain high concentrations in extracellular fluids during many inflammatory processes. Phosphatidylcholines 0-20 phospholipase A2 group IIA Homo sapiens 116-120 9507109-1 1998 Phosphatidyl-choline (PC) vesicles and normal cell membranes are resistant to hydrolysis by human group II secreted PLA2, an enzyme that can attain high concentrations in extracellular fluids during many inflammatory processes. Phosphatidylcholines 22-24 phospholipase A2 group IIA Homo sapiens 116-120 11112443-6 2000 Finally, recombinant expression of hGIIF sPLA(2) in Escherichia coli shows that the enzyme is Ca(2+)-dependent, maximally active at pH 7-8, and hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference. Phosphatidylcholines 183-202 phospholipase A2 group IIA Homo sapiens 41-48 10839997-2 2000 We showed that hVPLA(2) can bind phosphatidylcholine membranes and hydrolyse phosphatidylcholine molecules much more efficiently than human group-IIa PLA(2), which accounts for its high activity on the outer plasma membrane of mammalian cells. Phosphatidylcholines 33-52 phospholipase A2 group IIA Homo sapiens 17-23 10839997-2 2000 We showed that hVPLA(2) can bind phosphatidylcholine membranes and hydrolyse phosphatidylcholine molecules much more efficiently than human group-IIa PLA(2), which accounts for its high activity on the outer plasma membrane of mammalian cells. Phosphatidylcholines 77-96 phospholipase A2 group IIA Homo sapiens 17-23 10839997-6 2000 Together, these steric and electrostatic properties of the active site of hVPLA(2) allow for effective binding and hydrolysis of a bulky cationic choline head group of phosphatidylcholine, which is unique among mammalian secretory PLA(2)s. Phosphatidylcholines 168-187 phospholipase A2 group IIA Homo sapiens 231-238 10898226-2 2000 Recently, we reported that lysophosphatidylcholine (L-PC), the PLA2 hydrolysis product of phosphatidylcholine (PC), stimulates bacterial translocation (BT) in an enterocyte cell-culture model. Phosphatidylcholines 31-50 phospholipase A2 group IIA Homo sapiens 63-67 10898226-2 2000 Recently, we reported that lysophosphatidylcholine (L-PC), the PLA2 hydrolysis product of phosphatidylcholine (PC), stimulates bacterial translocation (BT) in an enterocyte cell-culture model. Phosphatidylcholines 54-56 phospholipase A2 group IIA Homo sapiens 63-67 10898226-8 2000 Thin-layer chromatography (TLC) was utilized to verify PLA2 hydrolysis of PC to L-PC. Phosphatidylcholines 74-76 phospholipase A2 group IIA Homo sapiens 55-59 10898226-13 2000 PLA2 mediates hydrolysis of PC to L-PC when both are applied to the apical surface of cultured enterocyte monolayers, resulting in increased BT and increased TEER with no damage to monolayer integrity. Phosphatidylcholines 28-30 phospholipase A2 group IIA Homo sapiens 0-4 9748327-8 1998 Although this enzyme shows a modest ( approximately 50%) reduction in activity when anionic substrates are used under standard assay conditions, the activity of the enzyme on phosphatidylcholine vesicles and cell membranes is dramatically increased compared with human sPLA2. Phosphatidylcholines 175-194 phospholipase A2 group IIA Homo sapiens 269-274 9299527-1 1997 Synthetic melittin inhibited the enzymatic activity of secretory phospholipase A2 (PLA2) from various sources, including bee and snake venoms, bovine pancreas, and synovial fluid from rheumatoid arthritis patients, irrespective of substrate (e.g., [14C]-phosphatidylcholine or phosphatidylethanolamine vesicles and [3H]-oleic acid-labeled E.coli). Phosphatidylcholines 254-273 phospholipase A2 group IIA Homo sapiens 83-87 9219902-6 1997 Whereas venom PLA2 was cytolytic in the presence of either phosphatidylcholine or phosphatidylethanolamine (PE), rh-sPLA2 caused cell death only in the presence of PE. Phosphatidylcholines 59-78 phospholipase A2 group IIA Homo sapiens 14-18 9178697-6 1997 Increased biliary immunoreactive PLA2-II levels in multiple cholesterol stones were associated with a concomitant increase in the lysophosphatidylcholine to phosphatidylcholine ratio; free arachidonate, protein, and hexosamine concentrations; and gallbladder bile viscosity. Phosphatidylcholines 134-153 phospholipase A2 group IIA Homo sapiens 33-37 1906891-6 1991 The rIL-1-stimulated PLA2 had an alkaline pH optimum, and phosphatidylethanolamine was preferred over phosphatidylcholine as substrate. Phosphatidylcholines 102-121 phospholipase A2 group IIA Homo sapiens 21-25 8068732-7 1994 Interestingly, PLA2 able to induce platelet activation efficiently hydrolyse phosphatidylcholine, while those inactive on platelets did not. Phosphatidylcholines 77-96 phospholipase A2 group IIA Homo sapiens 15-19 8068732-9 1994 Moreover, the ability of PLA2 to induce platelet activation is not related to its structural group (I, II, III) but rather to its origin (venom vs. mammalian) and capacity to hydrolyse phosphatidylcholine, the major phospholipid of the outer leaflet of the plasma membrane. Phosphatidylcholines 185-204 phospholipase A2 group IIA Homo sapiens 25-29 2758074-1 1989 The specificity of snake venom phospholipase A2(PLA2) towards a number of phospholipid (PL) substrates, e. g., phosphatidylcholine (PC), phosphatidylglycerol (PG), phosphatidylethanolamine (PE) and phosphatidylinositol (PI) organized in Triton X-100 mixed micelles, liposomes and proteoliposomes was studied. Phosphatidylcholines 111-130 phospholipase A2 group IIA Homo sapiens 48-52 2073400-2 1990 A novel method for determination of PLA2 activity in intact cell membranes with a fluorescent analogue of phosphatidylcholine, was employed. Phosphatidylcholines 106-125 phospholipase A2 group IIA Homo sapiens 36-40 2758074-1 1989 The specificity of snake venom phospholipase A2(PLA2) towards a number of phospholipid (PL) substrates, e. g., phosphatidylcholine (PC), phosphatidylglycerol (PG), phosphatidylethanolamine (PE) and phosphatidylinositol (PI) organized in Triton X-100 mixed micelles, liposomes and proteoliposomes was studied. Phosphatidylcholines 132-134 phospholipase A2 group IIA Homo sapiens 48-52 3949762-1 1986 Purification of human platelet phospholipase A2 (PLA2) from a particulate fraction by ion-exchange chromatography at 4 degrees C yielded a single peak of enzyme activity, which catalyzed the hydrolysis of arachidonic acid from the 2-position of phosphatidylcholine (PtdCho) and phosphatidylethanolamine (PtdEtn). Phosphatidylcholines 245-264 phospholipase A2 group IIA Homo sapiens 49-53 3949762-1 1986 Purification of human platelet phospholipase A2 (PLA2) from a particulate fraction by ion-exchange chromatography at 4 degrees C yielded a single peak of enzyme activity, which catalyzed the hydrolysis of arachidonic acid from the 2-position of phosphatidylcholine (PtdCho) and phosphatidylethanolamine (PtdEtn). Phosphatidylcholines 266-272 phospholipase A2 group IIA Homo sapiens 49-53 31739040-6 2020 Both enzymes have improved thermostability compared to mammalian pancreatic sPLA2 since they are active and stable at 55 C, with specific activities of 320 and 190 U mg-1 measured on phosphatidylcholine, respectively. Phosphatidylcholines 184-203 phospholipase A2 group IIA Homo sapiens 76-81 25118676-11 2014 The anticoagulant potency of Nk-PLA2beta which is higher than that of Nk-PLA2alpha is corroborated by its superior catalytic activity, its higher capacity for binding to phosphatidylcholine, and its greater strength of thrombin inhibition. Phosphatidylcholines 170-189 phospholipase A2 group IIA Homo sapiens 32-40