Relevant bibliographies by topics / Phospolipase A2

Academic literature on the topic 'Phospolipase A2'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Phospolipase A2"

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Taketo, Makoto Mark, and Masahiro Sonoshita. "Phospolipase A2 and apoptosis." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1585, no. 2-3 (December 2002): 72–76. http://dx.doi.org/10.1016/s1388-1981(02)00326-8.

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Pasaribu, B. O., A. Wijaya, and A. Hamid. "Soluble amyloid-B and secretory phospolipase A2." Journal of the Neurological Sciences 283, no. 1-2 (August 2009): 280. http://dx.doi.org/10.1016/j.jns.2009.02.157.

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Ali, Irshad, William B. Campbell, and Sushil K. Sarna. "Impaired activation of cytosolic phospolipase A2 in inflamed canine colonic circular muscle." Gastroenterology 119, no. 1 (July 2000): 62–70. http://dx.doi.org/10.1053/gast.2000.8558.

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Pasaribu, B. O., A. Wijaya, and A. Hamid. "Relationship between soluble amyloid beta and secretory phospolipase A2 to the progression of Alzheimer's disease." Journal of the Neurological Sciences 283, no. 1-2 (August 2009): 288–89. http://dx.doi.org/10.1016/j.jns.2009.02.187.

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Arthur, G., L. Page, T. Mock, and P. C. Choy. "The catabolism of plasmenylcholine in the guinea pig heart." Biochemical Journal 236, no. 2 (June 1, 1986): 475–80. http://dx.doi.org/10.1042/bj2360475.

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The hydrolysis of the alkenyl bonds of plasmenylcholine and plasmenylethanolamine by plasmalogenase, followed by hydrolysis of the resultant lysophospholipid by lysophospholipase, has been postulated as the major pathway for the catabolism of these plasmalogens. However, the postulation was based solely on the presence of plasmalogenase activity towards plasmenylethanolamine and plasmenylcholine in the brain. In this study we have demonstrated the absence of plasmalogenase activity for plasmenylcholine in the guinea pig heart under a wide range of experimental conditions. Plasmenylcholine was hydrolysed by phospolipase A2 activities in cardiac microsomal, mitochondrial and cytosolic fractions. Phospholipase A2 activities in these fractions had an alkaline pH optimum and were enhanced by Ca2+. The enzymes also displayed high specificity for plasmenylcholine with linoleoyl or oleoyl at the C-2 position. Lysoplasmalogenase activity for lysoplasmenycholine was also detected and characterized in the microsomal and mitochondrial fractions. Since the cardiac plasmalogenase is only active towards plasmenylethanolamine but not plasmenylcholine, the catabolism of these two plasmalogens must be different from each other. We postulate that the major pathway for the catabolism of plasmenycholine involves the hydrolysis of the C-2 fatty acid by phospholipase A2, and hydrolysis of the vinyl ether group of the resultant lysoplasmenylcholine by lysoplasmalogenase.
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Reddy, S., R. Bose, G. H. Rao, and M. Murthy. "Phospholipase A2 activation in human neutrophils requires influx of extracellular Ca2+ and leukotriene B4." American Journal of Physiology-Cell Physiology 268, no. 1 (January 1, 1995): C138—C146. http://dx.doi.org/10.1152/ajpcell.1995.268.1.c138.

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We have demonstrated that phospolipase A2 (PLA2) activation in human neutrophils requires both the influx of extracellular Ca2+ and leukotriene B4 (LTB4). Surprisingly, the eicosanoids (LTB4 and its omega-oxidation products) formed were quantitatively very similar in both thapsigargin (Thap)- and A-23187-stimulated neutrophils. In contrast, Thap had very little effect on the activation of PLA2 when 5-lipoxygenase (5-LO) was blocked by BW755C or MK-886, whereas A-23187 caused a substantial activation. The lack of PLA2 activation in Thap-stimulated neutrophils results from the inhibition of LTB4 formation in the presence of 5-LO inhibitors. It appears that A-23187 activates both LTB4-dependent and -independent PLA2, whereas Thap activates LTB4-dependent PLA2. Experiments with ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid demonstrated that activation of Thap-sensitive PLA2 and 5-LO requires the influx of Ca2+. Neither the transient elevation of cytosolic Ca2+ from intracellular stores nor the sustained Ca2+ influx alone without LTB4 appears sufficient to cause the activation of LTB4-dependent PLA2. We suggest that the activation of LTB4-dependent PLA2 involves 1) a sustained elevation of cytosolic Ca2+ coupled to the influx of extracellular Ca2+ and 2) a coupling between LTB4 and its receptor. We conclude that LTB4-dependent PLA2 plays an important role in the poststimulatory formation of lipid mediators such as prostaglandins, leukotrienes, and platelet-activating factor.
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Dewi, Nadifa Kartika, Mila Citrawati, Dhigna Luthfiyani, and Harli Amir Mahmudji. "The relationship of secretory phospholipase A2 type IIA levels with glomerulus filtration rate in type 2 DM patients." JFIOnline | Print ISSN 1412-1107 | e-ISSN 2355-696X 12, no. 1 (January 31, 2020): 60–67. http://dx.doi.org/10.35617/jfionline.v12i1.51.

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Phospolipase / sPLA2 type IIA is mediator that connects pathogenesis diabetes and its complications. Diabetic nephropathy is the most frequent microvascular complications, with albumin urine and changes in glomerular filtration rate. The aim was to discover the relation between sPLA2 type IIA levels in diabetic patients with glomerular filtration rate (GFR). This study used crossectional method in 62 samples in RSJ. Prof. Dr. Soerojo Magelang. Sampling was done by total sampling and medical record used as instrument. This research conducted in patients with sPLA2 type IIA levels and has complete laboratory examination data carried out in 2016. The results showed that the level of sPLA2 type IIA was very high in diabetic patients and GFR was below normal. Pearson correlation analysis showed that there was no significant correlation between type IIA sPLA2 with GFR (p=0.318), with a positive but very weak correlation (r=0.129) with diabetic duration of 8 years. Pearson correlation analysis was conducted in 21 samples which GFR values were ≤60 (p=0.0712) resulted a negative direction (r=-0.086) with diabetes duration of 11 years. It was shown that diabetic patients with increased the level of sPLA2 type IIA and longer period of diabetes will affect the decrease in GFR value.
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Kaniawati, Marita, Andi Wijaya, and Anwar Susanto. "The Correlations Between Concentrations of Myeloperoxidase, Serum Amyloid-A Protein and Scretory Phospolipase A-2 with Proinflammatory HDL in Healthy Male Person." Indonesian Biomedical Journal 1, no. 1 (April 1, 2009): 53. http://dx.doi.org/10.18585/inabj.v1i1.83.

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BACKGROUND: Low-HDL cholesterol is a risk factor of CAD. Although levels of HDLC are within normal limit in some patients, they suffer CAD. These normal HDL-C levels might become pro-inflammatoric. This study is to measure the correlations between myeloperoxidase (MPO), serum amyloid-A (SAA) protein, and secretoryphospholipase-A2 (sPLA2) with inflammatory status of HDL-C.METHODS: This was a cross-sectional study recruited 49 subjects with high HDL-C (> 40 mg/dL) and 31 subjects with low HDL-C (< 40 mg/dL). HDL-C was determined into antiinflammatory and proinflammatory based on levels of Apo A-1 and hs-CRP. Concentrations of MPO, SAA and s-PLA2 were measured by ELISA method. Levels of Apo A-1 was determined by immunoturbidimetric method. Multiple logistic regression analysis was done using inflammatory status of HDL-C as dependent variables and levels of MPO, SAA, sPLA2, ages, total cholesterol and triglycerides as independent variables.RESULTS: Patient’s age was 43.4 + 8.3 year, HDL-C was 43.1 + 9.5 mg/dL, Apo A-1 was 128.3 + 21.5 mg/dL, hs-CRP was 1.92 + 3.0 mg/dL. Concentrations of MPO, SAA and sPLA2 successively were 63.2 + 16.9 ng/mL, 7015.6 + 5021.1 ng/mL and 1340.2 + 406.3 pg/mL. Multiple logistic regression analysis showed that SAA is an independent predictor of pro-inflammatory status of HDL-C in high HDL-C group with prevalence ratio of 11.74 (95% CI : 2.51 – 54.84; P = 0.002). In contrast, MPO and sPLA2 were not independent predictor with PR of 1.26 (95% CI : 0.30 – 5.23; P = 0.75) and of 0.94 (95% CI : 0.23 – 3.91; P = 0.93).CONCLUSIONS: SAA is an independent predictor of pro-inflammatory HDL-C even in subjects with high HDL-C.KEYWORDS: Atherosclerosis, Apo A-I, serum amyloid A protein, secretory phospholipase A2, myeloperoxidase
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Clark, Mike A., John S. Bomalaski, Theresa M. Conway, Jill Wartell, and Stanley T. Crooke. "Differential effects of aspirin and dexamethasone on phospolipase A2 and C activities and arachidonic acid release from endothelial cells in respose to bradykinin and leukotriene D4." Prostaglandins 32, no. 5 (November 1986): 703–8. http://dx.doi.org/10.1016/0090-6980(86)90192-9.

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KUMAR, GANDEPALLI PRATAP, AMOS SAMKUMAR R, PREMNATH D, and DAVID PAULRAJ RS. "Molecular docking and dynamic simulation studies of pentacyclictriterpenoids from euphorbiaceae Plants with snake venom phospolipase a2 And acostatin proteins." International Journal of Pharma and Bio Sciences 7, no. 4 (October 17, 2016). http://dx.doi.org/10.22376/ijpbs.2016.7.4.b402-411.

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Dissertations / Theses on the topic "Phospolipase A2"

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Kemparaju, K. "Characterization of immunologically cross-reacting Phospolipase A2 Toxins from Indian Saw Scaled Viper (Echis Carinatus) Venom." Thesis, 1995. http://hdl.handle.net/2009/1333.

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