Leibovitz's L-15 Medium, 500 mL - Citations

Leibovitz's L-15 Medium, 500 mL - Citations

View additional product information for Leibovitz's L-15 Medium - Citations (11415064, 11415114)

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Citations & References
Abstract
Tumor necrosis factor alpha increases the expression of glycosyltransferases and sulfotransferases responsible for the biosynthesis of sialylated and/or sulfated Lewis x epitopes in the human bronchial mucosa.
Authors Delmotte Philippe; Degroote Sophie; Lafitte Jean-Jacques; Lamblin Geneviève; Perini Jean-Marc; Roussel Philippe;
JournalJ Biol Chem
PubMed ID11679593
'There is increasing evidence that inflammation may affect glycosylation and sulfation of various glycoproteins. The present study reports the effect of tumor necrosis factor alpha (TNF-alpha), a proinflammatory cytokine, on the glycosyl- and sulfotransferases of the human bronchial mucosa responsible for the biosynthesis of Lewis x epitope and of its ... More
Antiapoptotic activity of the free caspase recruitment domain of procaspase-9: a novel endogenous rescue pathway in cell death.
Authors Stephanou Anastasis; Scarabelli Tiziano M; Knight Richard A; Latchman David S;
JournalJ Biol Chem
PubMed ID11825888
Mitochondrial injury initiates proteolytic processing of procaspase-9 into the large and small subunits, leading to apoptotic cell death. Here we show that the free caspase recruitment domain (CARD) released by procaspase-9 processing activates nuclear factor kappaB expression. A procaspase-9 construct with a point mutation that abrogates the release of the ... More
Expression and localization of aquaporin water channels in rat hepatocytes. Evidence for a role in canalicular bile secretion.
Authors Huebert Robert C; Splinter Patrick L; Garcia Fabiana; Marinelli Raul A; LaRusso Nicholas F;
JournalJ Biol Chem
PubMed ID11932260
Although bile formation requires that large volumes of water be rapidly transported across liver epithelia, including hepatocytes, the molecular mechanisms by which water is secreted into bile are obscure. The aquaporins are a family of 10 channel-forming, integral membrane proteins of approximately 28 kDa numbered 0-9 that allow water to ... More