Direct Inhibition of in Vitro PLD Activity by 4-(2-Aminoethyl)-Benzenesulfonyl Fluoride

While conducting a purification protocol of phospholipase D (PLD) from human granulocytes, we observed that PLD activity was inhibited by a commonly-used protease inhibitor cocktail. Of the six inhibitors present in the cocktail, the serine protease inhibitor, 4-(2-aminoethyl)-benezensulfonyl fluori...

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Published inBiochemical and biophysical research communications Vol. 273; no. 1; pp. 302 - 311
Main Authors Andrews, Brooke, Bond, Kristina, Lehman, Jason A., Horn, Jeffrey M., Dugan, Amy, Gomez-Cambronero, Julia
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 24.06.2000
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Abstract While conducting a purification protocol of phospholipase D (PLD) from human granulocytes, we observed that PLD activity was inhibited by a commonly-used protease inhibitor cocktail. Of the six inhibitors present in the cocktail, the serine protease inhibitor, 4-(2-aminoethyl)-benezensulfonyl fluoride (AEBSF), was found to be the sole inhibitor of PLD. AEBSF caused a loss of neutrophil and purified plant PLD activities in vitro, but not in intact cells at the concentrations used, nor did it affect the related phospholipases A2 and C, that were utilized as specificity controls. The compound AEBSNH2, which has the fluoride replaced by an -NH2 group, failed to affect PLD activity as did other compounds structurally related to AEBSF with known protease inhibitory capabilities. Finally, basal- and agonist-stimulated PLD activity was inhibited in phosphatidylcholine-specific anti-PLD immunoprecipitates (IC50 = 75 μM). These results suggest that AEBSF, in an effect probably unrelated to its anti-proteolytic ability, directly interferes with PLD enzymatic activity, making it a significant compound to begin analyzing the role of PLD in mammalian cell signaling.
AbstractList While conducting a purification protocol of phospholipase D (PLD) from human granulocytes, we observed that PLD activity was inhibited by a commonly-used protease inhibitor cocktail. Of the six inhibitors present in the cocktail, the serine protease inhibitor, 4-(2-aminoethyl)-benezensulfonyl fluoride (AEBSF), was found to be the sole inhibitor of PLD. AEBSF caused a loss of neutrophil and purified plant PLD activities in vitro, but not in intact cells at the concentrations used, nor did it affect the related phospholipases A(2) and C, that were utilized as specificity controls. The compound AEBSNH(2), which has the fluoride replaced by an -NH(2) group, failed to affect PLD activity as did other compounds structurally related to AEBSF with known protease inhibitory capabilities. Finally, basal- and agonist-stimulated PLD activity was inhibited in phosphatidylcholine-specific anti-PLD immunoprecipitates (IC(50) = 75 microM). These results suggest that AEBSF, in an effect probably unrelated to its anti-proteolytic ability, directly interferes with PLD enzymatic activity, making it a significant compound to begin analyzing the role of PLD in mammalian cell signaling.
While conducting a purification protocol of phospholipase D (PLD) from human granulocytes, we observed that PLD activity was inhibited by a commonly-used protease inhibitor cocktail. Of the six inhibitors present in the cocktail, the serine protease inhibitor, 4-(2-aminoethyl)-benezensulfonyl fluoride (AEBSF), was found to be the sole inhibitor of PLD. AEBSF caused a loss of neutrophil and purified plant PLD activities in vitro, but not in intact cells at the concentrations used, nor did it affect the related phospholipases A2 and C, that were utilized as specificity controls. The compound AEBSNH2, which has the fluoride replaced by an -NH2 group, failed to affect PLD activity as did other compounds structurally related to AEBSF with known protease inhibitory capabilities. Finally, basal- and agonist-stimulated PLD activity was inhibited in phosphatidylcholine-specific anti-PLD immunoprecipitates (IC50 = 75 μM). These results suggest that AEBSF, in an effect probably unrelated to its anti-proteolytic ability, directly interferes with PLD enzymatic activity, making it a significant compound to begin analyzing the role of PLD in mammalian cell signaling.
Author Dugan, Amy
Lehman, Jason A.
Andrews, Brooke
Gomez-Cambronero, Julia
Horn, Jeffrey M.
Bond, Kristina
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Issue 1
Keywords PLD
protease inhibitor
signal transduction
neutrophils
Language English
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Snippet While conducting a purification protocol of phospholipase D (PLD) from human granulocytes, we observed that PLD activity was inhibited by a commonly-used...
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StartPage 302
SubjectTerms Brassica - cytology
Brassica - drug effects
Brassica - enzymology
Cells, Cultured
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - isolation & purification
Enzyme Inhibitors - pharmacology
Humans
Hydrogen-Ion Concentration
Inhibitory Concentration 50
neutrophils
Neutrophils - cytology
Neutrophils - drug effects
Neutrophils - enzymology
Phosphatidylcholines - metabolism
Phospholipase D - antagonists & inhibitors
Phospholipase D - isolation & purification
Phospholipase D - metabolism
Phospholipases A - metabolism
PLD
Precipitin Tests
protease inhibitor
signal transduction
Signal Transduction - drug effects
Substrate Specificity
Sulfones - chemistry
Sulfones - isolation & purification
Sulfones - pharmacology
Time Factors
Type C Phospholipases - metabolism
Title Direct Inhibition of in Vitro PLD Activity by 4-(2-Aminoethyl)-Benzenesulfonyl Fluoride
URI https://dx.doi.org/10.1006/bbrc.2000.2938
https://www.ncbi.nlm.nih.gov/pubmed/10873602
Volume 273
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