| pubmed-article:18559668 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18559668 | lifeskim:mentions | umls-concept:C1157380 | lld:lifeskim |
| pubmed-article:18559668 | lifeskim:mentions | umls-concept:C1327414 | lld:lifeskim |
| pubmed-article:18559668 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:18559668 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:18559668 | pubmed:dateCreated | 2008-6-18 | lld:pubmed |
| pubmed-article:18559668 | pubmed:abstractText | Choline cytidylyltransferase (CCT) is the rate-limiting enzyme in the phosphatidylcholine biosynthetic pathway. Here, we demonstrate that CCT alpha-mediated phosphatidylcholine synthesis is required to maintain normal Golgi structure and function as well as cytokine secretion from the Golgi complex. CCT alpha is localized to the trans-Golgi region and its expression is increased in lipopolysaccharide (LPS)-stimulated wild-type macrophages. Although LPS triggers transient reorganization of Golgi morphology in wild-type macrophages, similar structural alterations persist in CCT alpha-deficient cells. Pro-tumor necrosis factor alpha and interleukin-6 remain lodged in the secretory compartment of CCT alpha-deficient macrophages after LPS stimulation. However, the lysosomal-mediated secretion pathways for interleukin-1 beta secretion and constitutive apolipoprotein E secretion are unaltered. Exogenous lysophosphatidylcholine restores LPS-stimulated secretion from CCT alpha-deficient cells, and elevated diacylglycerol levels alone do not impede secretion of pro-tumor necrosis factor alpha or interleukin-6. These results identify CCT alpha as a key component in membrane biogenesis during LPS-stimulated cytokine secretion from the Golgi complex. | lld:pubmed |
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| pubmed-article:18559668 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18559668 | pubmed:citationSubset | IM | lld:pubmed |
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