Evidence for Rho-mediated agonist stimulation of phospholipase D in rat1 fibroblasts. Effects of Clostridium botulinum C3 exoenzyme.
作者： Kenneth C. Malcolm , Cassondra M. Elliott , John H. Exton
关键词: In vitro 、 Agonist 、 Lysophosphatidic acid 、 Actin 、 Stimulation 、 Cytochalasin D 、 Biology 、 Cell biology 、 RHOA 、 Phospholipase D
摘要: Small GTP-binding proteins of the Rho family are implicated in vitro regulation phosphatidylcholine hydrolysis by phospholipase D (PLD). However, their role agonist-stimulated PLD activity whole cells is not clear. The ribosyltransferase C3 from Clostridium botulinum modifies and inhibits function. When introduced into rat1 fibroblasts scrape-loading, inhibited stimulated lysophosphatidic acid (LPA), endothelin-1, or phorbol ester. Neither time course nor agonist dose response for LPA-stimulated was altered C3-treated cells. In contrast to effects on activity, phosphatidylinositol-phospholipase C Surprisingly, treatment led a decrease amount RhoA protein, indicating that loss partly due proteins. As described previously, inhibition actin filament formation. disruption filaments with cytochalasin caused only minor activity. Interestingly, stimulation LPA rapid enrichment particulate fraction cell lysates. These data support an vivo separate its fiber
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