Results 221 to 230 of about 124,441 (260)

Structure and regulation of phospholipase D

Trends in Pharmacological Sciences, 1996
Phosphar:S~:~oline-specific phos>holipase D (PLDs) are phosphodi‘stemses that catalyse the hydrolysis If phosphatidylcholine (PC) to pmjute phosphatidic acid (PA) and :holine. Diverse stimuli mcreasePLD activity in many cells and PA, or a netabolite of this lipid, is probably he orimarv mediator of PLD-initia , ited cell signalltng.
A J, Morris, J, Engebrecht, M A, Frohman
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Phospholipase D in cellular senescence

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 1999
Cellular senescence appears to be an important part of organismal aging. Cellular senescence is characterized by flattened enlarged morphology, inhibition of DNA replication in response to growth factors, inability to phosphorylate the pRb tumor suppressor protein, inability to produce c-fos or AP-1 and overexpression of a variety of genes, notably p21
M E, Venable, L M, Obeid
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The transphosphatidylation activity of phospholipase D

Molecular and Cellular Biochemistry, 1996
Transphosphatidylation activity is a characteristic and remarkable property of phospholipase D (PLD) and has been studied in plants and mammalian tissues. This reaction is often used to confirm the properties and/or abnormalities of PLD activity. The mechanism for activating PLD transphosphatidylation seems multiple.
C H, Yu, S Y, Liu, V, Panagia
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Dimerization of Phospholipase D Isozymes

Biochemical and Biophysical Research Communications, 2002
Two mammalian phospholipase D (PLD) isozymes (PLD1 and PLD2) have been reported. In this study, we differentially tagged these isozymes with enhanced green fluorescent protein (EGFP-rPLD1 and EGFP-rPLD2) or Xpress peptide epitope (Xpress-rPLD1 and Xpress-rPLD2) to examine the association between these isozymes.
Yoonseok, Kam, John H, Exton
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Isolation of an Activator for Phospholipase D

Nature, 1959
WHILE working on the purification of phospholipase D for use in connexion with other studies on phos-pholipids1 we observed that incubation with the enzyme released choline from commercial soy bean lecithin, but not from synthetic L-α-dipalmitoyl lecithin or carefully purified lecithins from egg, yeast and soy beans.
H, WEISS, H E, SPIEGEL, E, TITUS
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Phospholipase D structure and regulation

Chemistry and Physics of Lipids, 1999
The recent identification of cDNA clones for phospholipase D has opened the door to new types of investigations into its structure and regulation. PLD activity has been found to be encoded by at least two different genes that contain catalytic domains that relate their mechanism of action to phosphodiesterases. In vivo roles for PLD suggest that it may
M A, Frohman, A J, Morris
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Measurement of Phospholipase D Activity

Analytical Biochemistry, 1997
Phosphodiesteric cleavage of phosphatidylcholine by members of a growing family of phospholipases D produces choline and phosphatidic acid. These enzymes can also catalyse a transphosphatidylation reaction in which the aliphatic chain of a primary alcohol is transferred to the phosphatidyl moiety of the phosphatidic acid product.
A J, Morris, M A, Frohman, J, Engebrecht
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Phospholipase D and cell signaling

Current Opinion in Immunology, 1993
Phospholipase D, which hydrolyzes phospholipids (primarily phosphatidylcholine) to generate phosphatidic acid, has emerged as a critical component in cellular signal transduction. Research during the past year has confirmed and extended the view that phosphatidic acid and its dephosphorylated product, sn-1,2-diacylglycerol, are important intracellular ...
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The Preparation of Phospholipids by Phospholipase D

1978
The transfer of the phosphatidyl residue from egg phosphatidylcholine to primary alkanols catalyzed by phospholipase D was systematically investigated. It was demonstrated that 1) the chain length of the alkanols is of critical importance, e.g. transphosphatidylation does not occur to alkanols or alkandiols with more than six carbon atoms; 2) double or
S, Kovatchev, H, Eibl
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Biochemical Analysis of Phospholipase D

2007
Phospholipase D (PLD) is distributed widely in nature, being present in various isoforms in bacteria, protozoa, fungi, plants, and animals. It catalyzes the hydrolysis of phospholipids, primarily phosphatidylcholine (PC), into phosphatidic acid (PA) and the head group, choline.
H Alex, Brown, Lee G, Henage, Anita M, Preininger, Yun, Xiang, John H, Exton   +4 more
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