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• W2071754818 abstract "The mammalian Ras GTPase-activating protein (p120Ras-GAP) interacts with activated members of the Ras superfamily of GTP-binding proteins to accelerate their deactivation by sharply increasing their rates of GTP hydrolysis. Among the Ras-family proteins interacting with p120Ras-GAP is Rap1A/Krev1, whose activity is not affected by p120Ras-GAP but which competes with Ras for p120Ras-GAP. A second protein that interacts with p120Ras-GAP is p190Rac-GAP, which activates the GTPase of guanine nucleotide-binding proteins of the Rho family (including Rac1 and Rac2). Both these p120Ras-GAP-binding proteins are of interest in connection with the regulation of the respiratory burst oxidase, Rap1A/Krev1 because it copurifies with cytochrome b558, and p190Rac-GAP because it inhibits the Rac2-dependent activation of the respiratory burst oxidase in a cell-free system. Using an 18-mer antisense oligonucleotide, we were able to decrease the expression of p120Ras-GAP in Epstein-Barr virus-transformed B lymphocytes. Under conditions where p120Ras-GAP expression was significantly depressed by antisense oligonucleotides, we observed a 40% increase in protein kinase C-dependent but not receptor-dependent O2⋅¯ production. In contrast, sense and scrambled oligonucleotides had no effect on either p120Ras-GAP expression or O2⋅¯ production. Our results suggest a role for p120Ras-GAP as a negative regulator in the protein kinase C-mediated activation of the respiratory burst oxidase. The mammalian Ras GTPase-activating protein (p120Ras-GAP) interacts with activated members of the Ras superfamily of GTP-binding proteins to accelerate their deactivation by sharply increasing their rates of GTP hydrolysis. Among the Ras-family proteins interacting with p120Ras-GAP is Rap1A/Krev1, whose activity is not affected by p120Ras-GAP but which competes with Ras for p120Ras-GAP. A second protein that interacts with p120Ras-GAP is p190Rac-GAP, which activates the GTPase of guanine nucleotide-binding proteins of the Rho family (including Rac1 and Rac2). Both these p120Ras-GAP-binding proteins are of interest in connection with the regulation of the respiratory burst oxidase, Rap1A/Krev1 because it copurifies with cytochrome b558, and p190Rac-GAP because it inhibits the Rac2-dependent activation of the respiratory burst oxidase in a cell-free system. Using an 18-mer antisense oligonucleotide, we were able to decrease the expression of p120Ras-GAP in Epstein-Barr virus-transformed B lymphocytes. Under conditions where p120Ras-GAP expression was significantly depressed by antisense oligonucleotides, we observed a 40% increase in protein kinase C-dependent but not receptor-dependent O2⋅¯ production. In contrast, sense and scrambled oligonucleotides had no effect on either p120Ras-GAP expression or O2⋅¯ production. Our results suggest a role for p120Ras-GAP as a negative regulator in the protein kinase C-mediated activation of the respiratory burst oxidase." @default.
• W2071754818 created "2016-06-24" @default.
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• W2071754818 date "1996-04-01" @default.
• W2071754818 modified "2023-10-17" @default.
• W2071754818 title "Enhancement of Protein Kinase C-dependent<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML altimg=si1.gif><mml:mrow><mml:msubsup><mml:mtext>O</mml:mtext><mml:mn>2</mml:mn><mml:mover accent=true><mml:mo>⋅</mml:mo><mml:mo>¯</mml:mo></mml:mover></mml:msubsup></mml:mrow></mml:math>Production in Epstein-Barr Virus-transformed B Lymphocytes by p120Ras-GAP Antisense Oligonucleotide" @default.
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• W2071754818 doi "https://doi.org/10.1074/jbc.271.16.9320" @default.
• W2071754818 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8621595" @default.
• W2071754818 hasPublicationYear "1996" @default.
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