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dc.contributor.authorHu, T. H.zh_CN
dc.contributor.authorExton, J. H.zh_CN
dc.identifier.citationBiochemical and Biophysical Research Communications,327(4):1047-1051zh_CN
dc.description.abstract1-Butanol is commonly used as a substrate for phospholipase D (PLD) activity measurement. Surprisingly we found that, in the presence of 30 mM 1-butanol (standard PLD assay conditions), PLD1 activity in COS-7 cells was lost after incubation for 2 min. In contrast, in the presence of the protein kinase C (PKC) inhibitor staurosporine or dominant negative PKCalpha D481E, the activity was sustained for at least 30 min. The binding between PLD1 and PKCalpha was also lost after 2 min incubation with 30 mM 1-butanol while staurosporine and D481E maintained the binding. 1-Butanol at 2 mM did not inhibit PLD1 basal activity or PLD1 binding to PKCalpha, and staurosporine and PKCalpha D481E produced a constant increase in PLD1 basal activity of 2-fold. These results indicate that 1-butanol is inhibitory to PLD1 activity by reducing its association with PKCalpha, and that the concentration of 1-butanol is an important consideration in assaying basal PLD1 activity. (C) 2004 Elsevier Inc. All rights reserved.zh_CN
dc.subjectphospholipase Dzh_CN
dc.subjectprotein kinase Czh_CN
dc.subjectbasal activityzh_CN
dc.titleI-Butanol interferes with phospholipase D1 and protein kinase C alpha association and inhibits phospholipase D1 basal activityzh_CN

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