Differential regulation of mammalian phospholipase D isoforms and their functional involvement in receptor-mediated endocytosis and oncogenic invasion.
Item
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Title
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Differential regulation of mammalian phospholipase D isoforms and their functional involvement in receptor-mediated endocytosis and oncogenic invasion.
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Identifier
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AAI3024834
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identifier
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3024834
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Creator
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Shen, Yingjie.
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Contributor
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Adviser: David A. Foster
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Date
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2001
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Language
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English
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Publisher
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City University of New York.
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Subject
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Biology, Cell
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Abstract
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Phospholipase D (PLD) activity is elevated in response to a wide range of extracellular signals. By hydrolyzing the major membrane lipid phosphatidylcholine and generate potential second messenger phosphatidic acid, PLD mediates a variety of cellular physiology.;The research presented in this thesis focused on the enzymatic regulation and cellular functions of mammalian PLD1 and PLD2. These studies have revealed that epidermal growth factor (EGF) and tyrosine kinase v-Src can each elevate PLD activity in rodent fibroblasts, and that PLD2 and PLD1 are sequentially activated and differentially regulated in response to EGF stimulation. Data are also presented demonstrating that both PLD1 and PLD2 mediate EGF-induced receptor endocytosis and the mitogenic signals that are dependent on this process. And finally, it is shown that PLD2 is required for Src-induced cell protrusion and the related motility and oncogenic invasiveness.;These data suggest that PLD participates not only in mitogenic signal transduction, but in morphological transformation and metastasis of tumor cells as well, possibly through facilitating vesicle formation and cytoskeleton reorganization. The differential functions of PLD1 and PLD2 are also discussed.
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Type
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dissertation
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Source
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PQT Legacy CUNY.xlsx
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degree
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Ph.D.
