Results 31 to 40 of about 321,900 (228)

Expression of mRNA for phospholipase A(2), cyclooxygenases, and lipoxygenases in cultured human umbilical vascular endothelial and smooth muscle cells and in biopsies from umbilical arteries and veins [PDF]

open access: yes, 1998
Arachidonic acid (AA) is released by phospholipase A(2) (PLA(2)) and then converted into vasoactive and inflammatory eicosanoids by cyclooxygenases (COX) and lipoxygenases (LOX).
Carlsson, Maria   +5 more
core   +1 more source

The phospholipase A2 activity of peroxiredoxin 6[S]

open access: yesJournal of Lipid Research, 2018
Peroxiredoxin 6 (Prdx6) is a Ca2+-independent intracellular phospholipase A2 (called aiPLA2) that is localized to cytosol, lysosomes, and lysosomal-related organelles.
A. Fisher
semanticscholar   +1 more source

Stimulated platelets release equivalent amounts of arachidonate from phosphatidylcholine, phosphatidylethanolamine, and inositides.

open access: yesJournal of Lipid Research, 1988
Thrombin-induced changes in arachidonate content of platelet phospholipids were quantitated to establish the ultimate origins of this eicosanoid precursor.
M J Broekman
doaj   +1 more source

2-Oxoesters: A Novel Class of Potent and Selective Inhibitors of Cytosolic Group IVA Phospholipase A2. [PDF]

open access: yes, 2017
Cytosolic phospholipase A2 (GIVA cPLA2) is the only PLA2 that exhibits a marked preference for hydrolysis of arachidonic acid containing phospholipid substrates releasing free arachidonic acid and lysophospholipids and giving rise to the generation of ...
Barbayianni, Efrosini   +10 more
core   +1 more source

Secretory Phospholipases A2 in Plants [PDF]

open access: yes, 2019
Secreted phospholipases (sPLA2s) in plants are a growing group of enzymes that catalyze the hydrolysis of sn-2 glycerophospholipids to lysophospholipids and free fatty acids. Until today, around only 20 sPLA2s were reported from plants.
Fidelio, Gerardo Daniel   +1 more
core   +1 more source

Lipoquality control by phospholipase A2 enzymes

open access: yesProceedings of the Japan Academy. Series B, Physical and biological sciences, 2017
The phospholipase A2 (PLA2) family comprises a group of lipolytic enzymes that typically hydrolyze the sn-2 position of glycerophospholipids to give rise to fatty acids and lysophospholipids.
M. Murakami
semanticscholar   +1 more source

Substrate-Specific Inhibition Constants for Phospholipase A2 Acting on Unique Phospholipid Substrates in Mixed Micelles and Membranes Using Lipidomics. [PDF]

open access: yes, 2019
Assaying lipolytic enzymes is extremely challenging because they act on water-insoluble lipid substrates, which are normally components of micelles, vesicles, and cellular membranes.
Armando, Aaron   +2 more
core   +6 more sources

Synthesis of photoreactive phosphatidylethanolamine and its interaction with phospholipase A2.

open access: yesJournal of Lipid Research, 1994
A photoreactive derivative of phosphatidylethanolamine, N-(4-azidobenzoyl)phosphatidylethanolamine (AB-PE), was synthesized by acylation of phosphatidylethanolamine with an N-hydroxysuccinimide ester of 4-azidobenzoic acid.
R Rajasekharan, J D Kemp
doaj   +1 more source

Generation of feeder-independent transgene-free iPSC lines from a young-onset Parkinson’s disease (YOPD) patient with a homozygous PLA2G6: c.2222G>A (p. Arg741Gln) mutation (NCBSi003-A) and unaffected heterozygous parent (NCBSi004-A)

open access: yesStem Cell Research, 2023
Phospholipase A2 group 6 (PLA2G6, iPLA2β or PARK14) gene encodes a calcium-independent group 6 phospholipase A2 enzyme and is associated with young-onset autosomal recessive Parkinson’s disease (PD). We generated human induced pluripotent stem cell (iPSC)
Renjitha Gopurappilly   +4 more
doaj   +1 more source

cAMP-Inhibits Cytoplasmic Phospholipase A(2) and Protects Neurons against Amyloid-beta-Induced Synapse Damage [PDF]

open access: yes, 2015
A key event in Alzheimer’s disease (AD) is the production of amyloid-β (Aβ) peptides and the loss of synapses. In cultured neurons Aβ triggered synapse damage as measured by the loss of synaptic proteins. α-synuclein (αSN), aggregates of which accumulate
Bate, C, Williams, A
core   +2 more sources

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