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phospholipase/ödem
Länken sparas på Urklipp
Sida 1 från 546 resultat
Darapladib, a lipoprotein-associated phospholipase A2 inhibitor, in diabetic macular edema: a 3-month placebo-controlled study.
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OBJECTIVE
To investigate the potential of lipoprotein-associated phospholipase A2 inhibition as a novel mechanism to reduce edema and improve vision in center-involved diabetic macular edema (DME).
METHODS
Prospective, multicenter, randomized, double-masked, placebo-controlled phase IIa
Comparison of the enzymatic and edema-producing activities of two venom phospholipase A2 enzymes.
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The edema-producing activity of NNAVPLA2, an acidic phospholipase A2 (PLA2) enzyme from Naja naja atra venom (NNAV), was less potent than that of TMVPLA2 II, a basic PLA2 from Trimeresurus mucrosquamatus venom (TMV). These edema-forming effects were greatly suppressed by pretreatment of rats with
Recombinant human type II phospholipase A2 lacks edema producing activity in rat.
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The rat paw edema-inducing, acute inflammatory activity of four snake venom phospholipase A2S (PLA2) (Naja naja, Naja mocambique mocambique, Crotalus atrox and recombinant Naja naja naja) and of recombinant human type II PLA2 (rh-PLA2) found in rheumatoid synovial fluid, were compared after a bolus
Pulmonary inflammation and edema induced by phospholipase A2: global gene analysis and effects on aquaporins and Na+/K+-ATPase.
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Victims of snakebite quickly succumb to severe respiratory failure, which can be fatal if left untreated. One of the most toxic components of snake venom is phospholipase A2 (PLA2; EC 3.1.1.4). PLA2 isolated from the elapid, Naja sputatrix, induced pulmonary inflammation and edema when administered
Edema-inducing activity of phospholipase A2 purified from human synovial fluid and inhibition by aristolochic acid.
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A neutral-active, Ca2+-dependent phospholipase A2 (PLA2) purified 11,000-fold from human synovial fluid (HSF) induced edema when injected into the mouse foot pad. The edema produced by HSF-PLA2 was dose-dependent and was positively correlated with the dose-dependent in vitro expression of PLA2
Characterization of three edema-inducing phospholipase A2 enzymes from habu (Trimeresurus flavoviridis) venom and their interaction with the alkaloid aristolochic acid.
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A basic phospholipase A2 (PLA2) enzyme, TFV PL-X (pI 9.2) and two acidic PLA2 enzymes, TFV PL-Ia (pI 4.9) and TFV PL-Ib (pI 4.5) were purified from Trimeresurus flavoviridis venom on CM-Sephadex C-25 and QAE-Sephadex A-25 columns, respectively. The basic enzyme exists as a monomer, whereas the
Edema toxin impairs anthracidal phospholipase A2 expression by alveolar macrophages.
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Bacillus anthracis, the etiological agent of anthrax, is a spore-forming gram-positive bacterium. Infection with this pathogen results in multisystem dysfunction and death. The pathogenicity of B. anthracis is due to the production of virulence factors, including edema toxin (ET). Recently, we
Discovery of Potent and Orally Active Lipoprotein-Associated Phospholipase A2 (Lp-PLA2) Inhibitors as a Potential Therapy for Diabetic Macular Edema.
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Lipoprotein-associated phospholipase A2 (Lp-PLA2) is considered to be a promising therapeutic target for several inflammation-associated diseases. Herein, we describe the discovery of a series of pyrimidone derivatives as Lp-PLA2 inhibitors. Systematic structural modifications led to the
Edema formation and degranulation of mast cells by a basic phospholipase A2 purified from Trimeresurus mucrosquamatus snake venom.
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The basic phospholipase A2 (PLA2) purified from Trimeresurus mucrosquamatus snake venom was injected into the subplantar in order to induce edema formation in the rat hind paw. The maximum edema induced by PLA2 was induced at 1-2 hr after injection, and the per cent swelling curve showed a
Phospholipase A2-induced lung edema and its mechanism in isolated perfused guinea pig lung.
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Lung injury induced by phospholipase A2 (PLA2, 0.046 IU/ml perfusate) was studied in a continuous weighing system of isolated perfused guinea pig lungs. The results revealed that lung weight increased progressively during the 30-min perfusion of PLA2. No change of pulmonary arterial pressure was
[Effects of phospholipase A2 on the etiology of pulmonary edema hemodynamics of lesser circulation in intact and vagotomized animals].
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In experiments on white rats, guinea pigs and cats it was shown that intravenous infusion of phospholipase A2 (FLA2) caused the development of pulmonary edema (PE) in guinea pigs, but did not cause it in rats and cats. Bilateral vagotomy on the neck led to the appearance of the expressed edemogenous
Pharmacological modulation of edema induced by Lys-49 and Asp-49 myotoxic phospholipases A2 isolated from the venom of the snake Bothrops asper (terciopelo).
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The pharmacological modulation of edema-forming activity of Bothrops asper myotoxins II and III, Lys-49 and Asp-49 phospholipases A2, respectively, was studied plethysmographically in the mouse foot pad model. Myotoxin III had phospholipase A2 activity, whereas myotoxin II was devoid of enzymatic
The edema inducing activity of phospholipase A2 enzymes.
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The edema inducing activity of phospholipase A2 (PLA2) enzymes from snake venoms and porcine pancreas was investigated using mouse paw as experimental model. All ten PLA2 enzymes exhibited potent edema inducing activity. PLA2, however, is generally not the major edema inducing component of snake
Inhibition of secretory phospholipase A2 activity attenuates acute cardiogenic pulmonary edema induced by isoproterenol infusion in mice after myocardial infarction.
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Several types of secretory phospholipase A2 (sPLA2) are expressed in lung tissue, yielding various eicosanoids that might cause pulmonary edema. This study examined whether inhibition of sPLA2 activity attenuates acute cardiogenic pulmonary edema in mice. Acute cardiogenic pulmonary edema was
Pharmacological study of edema and myonecrosis in mice induced by venom of the bushmaster snake (Lachesis muta muta) and its basic Asp49 phospholipase A(2) (LmTX-I).
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Previous in vitro studies show that Lachesis muta venom and its purified Asp49 phospholipase A(2), named as LmTX-I, display potent neurotoxic and myotoxic activities. Here, an in vivo study was conducted to investigate some pharmacological effects of the venom or its LmTX-I toxin, after
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