Results 21 to 30 of about 9,957 (215)

Phospholipase A2 Biochemistry [PDF]

open access: yesCardiovascular Drugs and Therapy, 2008
The phospholipase A(2) (PLA(2)) superfamily consists of many different groups of enzymes that catalyze the hydrolysis of the sn-2 ester bond in a variety of different phospholipids. The products of this reaction, a free fatty acid, and lysophospholipid have many different important physiological roles.
Burke, John E, Dennis, Edward A
openaire   +4 more sources

Subcellular localization of the phospholipases A of rat heart: evidence for a cytosolic phospholipase A1.

open access: yesJournal of Lipid Research, 1985
During myocardial ischemia increased levels of lysoglycerophospholipids have been reported which may be deleterious to myocardial function. Phospholipases are presumed to be important in the regulation of this process.
G Nalbone, K Y Hostetler
doaj   +1 more source

Signal-activated phospholipase regulation of leukocyte chemotaxis

open access: yesJournal of Lipid Research, 2009
Signal-activated phospholipases are a recent focus of the rapidly growing field of lipid signaling. The extent of their impact on the pathways regulating diverse cell functions is beginning to be appreciated.
Martha K. Cathcart
doaj   +1 more source

Evaluation of the Brazilian functional fruit Morinda citrifolia as phospholipases A2 and proteases modulator

open access: yesPhytomedicine Plus, 2021
Morinda citrifolia is a plant widely consumed as food and used in folk medicine. However, there is little scientific information regarding its therapeutic properties. In this study, aqueous extracts from the peel and pulp of M.
Tamara Rezende Marques   +7 more
doaj   +1 more source

Lysosomal phospholipase A2

open access: yesBiochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2019
Lysosomal phospholipase A2 (PLA2G15) is a ubiquitous enzyme uniquely characterized by a subcellular localization to the lysosome and late endosome. PLA2G15 has an acidic pH optimum, is calcium independent, and acts as a transacylase in the presence of N-acetyl-sphingosine as an acceptor.
James A, Shayman, John J G, Tesmer
openaire   +2 more sources

Group XV phospholipase A2, a lysosomal phospholipase A2 [PDF]

open access: yesProgress in Lipid Research, 2011
A phospholipase A₂ was identified from MDCK cell homogenates with broad specificity toward glycerophospholipids including phosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, and phosphatidylglycerol. The phospholipase has the unique ability to transacylate short chain ceramides.
James A. Shayman   +4 more
openaire   +1 more source

AASLD practice guidance on drug, herbal, and dietary supplement–induced liver injury

open access: yes, 2022
Hepatology, EarlyView.
Robert J. Fontana   +6 more
wiley   +1 more source

The relationship between lipoprotein-associated phospholipase A2 with cardiovascular risk factors in testosterone deficiency

open access: yesUrology Research and Practice, 2019
Objective: Lipoprotein-associated phospholipase A2 (Lp-PLA2) which is believed to play a role in atherosclerotic inflammatory process due to its function in hydrolysis of phospholipids and release of pro-inflammatory products, is considered as a novel ...
Mustafa Keleşoğlu   +6 more
doaj   +1 more source

Secretory Phospholipase A2

open access: yesBiological and Pharmaceutical Bulletin, 2004
Secretory phospholipase A2 (sPLA2) is a growing family of structurally related, disulfide-rich, low molecular weight, lipolytic enzymes with a His-Asp catalytic dyad. sPLA2s are distributed in a wide variety of vertebrate and invertebrate animals, plants, bacteria, and viruses, and there are 10 catalytically active sPLA2 isozymes in mammals.
Murakami, Makoto, Kudo, Ichiro
openaire   +3 more sources

Novel Bradykinin-Potentiating Peptides and Three-Finger Toxins from Viper Venom: Combined NGS Venom Gland Transcriptomics and Quantitative Venom Proteomics of the Azemiops feae Viper

open access: yesBiomedicines, 2020
Feae’s viper Azemipos feae belongs to the Azemiopinae subfamily of the Viperidae family. The effects of Viperidae venoms are mostly coagulopathic with limited neurotoxicity manifested by phospholipases A2. From A.
Vladislav V. Babenko   +10 more
doaj   +1 more source

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