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• W2111312578 abstract "Using differential screening of cytokine-activated versus resting porcine aortic endothelial cells (PAEC), we have isolated a member of the family of Ras/GTP-binding proteins. The cDNA encodes a 34-kilodalton protein showing 97% homology to Gem, a gene recently isolated from activated T cells, likely representing its porcine homologue. The amino acid sequence differs from the Ras consensus by the absence of a C-terminal isoprenylation site and a glycine to glutamic acid substitution in the third GTP-binding domain. We report here, that pigGem mRNA is strongly inducible in PAEC upon activation by either IL-1α, TNFα or lipopolysaccharide (LPS). Low constitutive expression is found in several organs. Epitope-tagged pigGem transfected into endothelial cells (EC) localizes to the cytoplasm and to the inner side of the plasma membrane. Structural features of Gem and its indelibility apparently restricted to T cells and endothelial cells, together with Rad, a GTPase overexpressed in skeletal muscle cells of type II diabetic individuals, define a new branch within the superfamily of GTP-binding proteins." @default.
• W2111312578 created "2016-06-24" @default.
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• W2111312578 date "1997-01-01" @default.
• W2111312578 modified "2023-10-18" @default.
• W2111312578 title "Gem, a GTP-Binding Protein from Mitogen-Stimulated T Cells, is Induced in Endothelial Cells Upon Activation by Inflammatory Cytokines" @default.
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• W2111312578 doi "https://doi.org/10.3109/10623329709044158" @default.
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