Results 151 to 160 of about 41,701 (205)
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Journal of Biochemistry, 2002
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins (PGs) and leukotrienes (LTs). The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
I, Kudo, M, Murakami
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Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins (PGs) and leukotrienes (LTs). The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
I, Kudo, M, Murakami
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Seminars in Cell and Developmental Biology, 1997
There is a well established role for various phospholipases involved in the production of intracellular signals at the plasma membrane. In contrast much less is known of their role in other intracellular compartments, however, emerging evidence would suggest that some of these enzymes are also involved in the production of signals within the nucleus ...
Nullin Divecha
exaly +4 more sources
There is a well established role for various phospholipases involved in the production of intracellular signals at the plasma membrane. In contrast much less is known of their role in other intracellular compartments, however, emerging evidence would suggest that some of these enzymes are also involved in the production of signals within the nucleus ...
Nullin Divecha
exaly +4 more sources
Seminars in Cell & Developmental Biology, 1997
The central role that different phospholipases play in many signal transduction pathways has been intensively studied by classical biochemical and molecular approaches. One approach not extensively pursued, has been the use of yeast as a model system for functional analysis of different aspects of phospholipase signalling.
, de Tiani M, , Torgler, , Meldrum
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The central role that different phospholipases play in many signal transduction pathways has been intensively studied by classical biochemical and molecular approaches. One approach not extensively pursued, has been the use of yeast as a model system for functional analysis of different aspects of phospholipase signalling.
, de Tiani M, , Torgler, , Meldrum
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Seminars in Cell & Developmental Biology, 1997
Phospholipase D catalyses the hydrolysis of phosphatidylcholine to generate phosphatidate. The regulation of PLD activity is complex involving a number of small GTP binding proteins, but in particular Arf and Rho, phosphatidylinositol 4,5-bisphosphate and protein kinase C.
, Wakelam, , Hodgkin, , Martin, , Saqib
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Phospholipase D catalyses the hydrolysis of phosphatidylcholine to generate phosphatidate. The regulation of PLD activity is complex involving a number of small GTP binding proteins, but in particular Arf and Rho, phosphatidylinositol 4,5-bisphosphate and protein kinase C.
, Wakelam, , Hodgkin, , Martin, , Saqib
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Biochemistry and Cell Biology, 2004
Phospholipase D catalyses the hydrolysis of the phosphodiester bond of glycerophospholipids to generate phosphatidic acid and a free headgroup. Phospholipase D activities have been detected in simple to complex organisms from viruses and bacteria to yeast, plants, and mammals.
Mark, McDermott +2 more
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Phospholipase D catalyses the hydrolysis of the phosphodiester bond of glycerophospholipids to generate phosphatidic acid and a free headgroup. Phospholipase D activities have been detected in simple to complex organisms from viruses and bacteria to yeast, plants, and mammals.
Mark, McDermott +2 more
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Seminars in Cell & Developmental Biology, 1997
Mammalian cells contain multiple structurally different phospholipase A2 enzymes that hydrolyse sn-2 fatty acid from membrane phospholipid. The low molecular weight secreted forms act extracellularly both as lipolytic enzymes and as agonists that bind to specific cell surface receptors.
, Gijón, , Leslie
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Mammalian cells contain multiple structurally different phospholipase A2 enzymes that hydrolyse sn-2 fatty acid from membrane phospholipid. The low molecular weight secreted forms act extracellularly both as lipolytic enzymes and as agonists that bind to specific cell surface receptors.
, Gijón, , Leslie
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Prostaglandins, Leukotrienes and Essential Fatty Acids, 2003
Considerable progress has been made in characterizing the individual participant enzymes and their relative contributions in the generation of eicosanoids, lipid mediators derived from arachidonic acid, such as prostaglandins and leukotrienes. However, the role of individual phospholipase (PL) A(2) enzymes in providing arachidonic acid to the ...
Bruno L, Diaz, Jonathan P, Arm
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Considerable progress has been made in characterizing the individual participant enzymes and their relative contributions in the generation of eicosanoids, lipid mediators derived from arachidonic acid, such as prostaglandins and leukotrienes. However, the role of individual phospholipase (PL) A(2) enzymes in providing arachidonic acid to the ...
Bruno L, Diaz, Jonathan P, Arm
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Phospholipases of the myocardium
1987The myocardium contains diverse cellular components and heterogeneous phospholipid-containing membranes. The major phospholipids are phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositnol, sphingomyelin and cardiolipin. The phospholipases capable of hydrolyzing these membrane lipids include phospholipase A, lysophospholipase, and ...
W B, Weglicki, M G, Low
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2018
Phospholipases are lipolytic enzymes that hydrolyze phospholipid substrates at specific ester bonds. Phospholipases are widespread in nature and play very diverse roles from aggression in snake venom to signal transduction, lipid mediator production, and metabolite digestion in humans. Phospholipases vary considerably in structure, function, regulation,
Ahmed, Aloulou +4 more
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Phospholipases are lipolytic enzymes that hydrolyze phospholipid substrates at specific ester bonds. Phospholipases are widespread in nature and play very diverse roles from aggression in snake venom to signal transduction, lipid mediator production, and metabolite digestion in humans. Phospholipases vary considerably in structure, function, regulation,
Ahmed, Aloulou +4 more
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Inhibition of phospholipase A2 and phospholipase C by polyamines
Archives of Biochemistry and Biophysics, 1978Abstract The polyamines spermine, spermidine, and putrescine inhibit the activity of phospholipase A2 (Naja naja) and phospholipase C (Clostridium welchii) on phospholipid vesicles and mitochondrial membranes as sources of substrate phospholipids. The inhibitory effect is highest for spermine and lowest for putrescine.
A M, Sechi +4 more
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