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• W2007721876 abstract "Phospholipase D (PLD) activity is elevated in Ras-transformed NIH 3T3 cells. This difference in PLD activity between Ras-transformed and nontransformed parental cells disappeared in isolated membranes from these cells. In reconstitution experiments, heat-denatured cytosolic fractions from Ras-transformed, but not parental, NIH 3T3 cells elevated PLD activity in isolated membranes. This heat-resistant PLD-stimulating activity from the Ras-transformed cells was sensitive to proteases and passed through a 1-kDa MW cutoff membrane, suggesting that the factor is a peptide of less than 10 amino acids. The ability of this PLD-stimulating factor, designated PLD-SF, to elevate PLD activity in isolated membranes was restricted to the caveolin-enriched light membranes, where many signaling molecules are localized. PLD-SF was also elevated in v-Src- and v-Raf-transformed cells and in serum-stimulated NIH 3T3 cells. PLD-SF was detected in a variety of rat tissues but was highest in testes, where a large percentage of cells are dividing. A similar low molecular weight PLD-stimulating activity was found in actively dividing, but not stationary yeast, cells. The data here provide evidence for a highly conserved PLD-stimulating peptide that is elevated in response to mitogenic stimuli." @default.
• W2007721876 created "2016-06-24" @default.
• W2007721876 creator A5013486072 @default.
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• W2007721876 date "2000-05-01" @default.
• W2007721876 modified "2023-09-27" @default.
• W2007721876 title "A Low Molecular Weight Factor from Dividing Cells Activates Phospholipase D in Caveolin-Enriched Membrane Microdomains" @default.
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• W2007721876 doi "https://doi.org/10.1006/abbi.2000.1766" @default.
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